Plastic degrading fusion proteins, methods and uses thereof

Abstract

The present invention relates to fusion proteins capable of degrading plastic polymers. The fusion proteins comprise two or more serin hydrolase domains and comprise the necessary features to efficiently and cost effectively be used in degradation of plastic polymers. Provided herein are also nucleic acids and nucleic acid vectors encoding such fusion proteins and cells comprising the same. Provided herein are also methods of producing such fusion proteins, and methods and uses of degrading plastic polymers using the fusion proteins provided herein.

Description

[0001] PLASTIC DEGRADING FUSION PROTEINS, METHODS AND USES THEREOF FIELD The present invention is in the field of fusion proteins, in particular those for use in plastic and / or plastic polymer degradation. BACKGROUND Plastics are versatile materials affecting almost all aspects of modern human life, addressing all kinds of needs of health, energy, clothing, packaging, new technologies, construction, housing, transport and communication. The annual production of plastics has significantly increased globally since the early 2000s, with expectation to reach 445.25 million metric tons by 2025 (1). In the past decade, plastic production has increased by more than 35% and is expected to grow to 700 Mt in 2030, representing 80 kg of plastics per human being (2). The increased global consumption and production of plastics had come with a cost. Currently, plastic production accounts for 6% of the global oil consumption and will reach 20% by 2050. Additionally, plastics life cycle has a great impact on greenhouse gas emissions, in 2019, plastics were responsible for 1.8 billion tons of CO2 equivalent emissions, which account for 3.4% of the global emissions (3, 4). As a result of the poor plastic waste management, there have been increasing concerns about the negative impact of plastic pollution on ecosystems and human health. Since its commercial application, around 8,300 million tons of plastics have been produced, generating 6,300 million tons of plastic waste. The majority (79%) of this waste has been landfilled, 12% has been incinerated and only 9% has been recycled (5). The majority of this waste is in the form of microplastics (particles and fibers ≈ 5 mm size) which are a ubiquitous pollutant in aquatic and terrestrial environments resulting in acute and chronic toxicity in animals, plants, and microbes as a result of landfill disposal (6, 7). On the other hand, plastic waste incineration results in harmful gas emissions such as methane, carbon monoxide and polyaromatic hydrocarbons, which impose the global carbon cycle exaggerating the greenhouse emissions (8). Considering the impact of plastics on the environment and living organisms, the European Commission communicated “The European Strategy for Plastics in a Circular Economy” combined with the promotion of various other initiatives (the Circular Plastic Alliance, etc.) recommending improved design to facilitate reuse and recycling, and decoupling production from fossil resources. Furthermore, a global plastics treaty involving 175 countries will be established by 2024, signifying a pivotal opportunity to end plastic pollution (9). Polyesters are a broad class of thermoplastic polymers that, depending on their monomer compositions can either be recyclable or biodegradable. Polyethylene terephthalate (PET) is the most popular fossil-based synthetic polymer comprising 18% of the global polymer production (10). It is the most common polymer in the textiles and packaging industries due to its diverse properties such as high chemical, mechanical and thermal resistance, low cost, high transparency, excellent gas-barrier properties (2). PET is industrially synthesized via heating purified terephthalic acid (TPA) with excess ethylene glycol (EG) that results in bis (2-hydroxyethyl) terephthalate (BHET). BHET is then pre-polymerized followed by subsequent melting condensation or solid-state polymerization to yield low molecular weight PET or high molecular weight PET, respectively (11). Enzymatic recycling of post-consumer PET (pc-PET) wastes and the subsequent utilization of the released monomers is considered a sustainable and economically feasible process implementing the circular plastic economy concept and mitigating plastic environmental concerns (12). Unlike chemical degradation of PET that requires high pressure, elevated temperatures and production of toxic gases, bio-based plastic depolymerization via enzymatic processes is more sustainable and environmentally friendly alternative as it can be run at mild pH, moderate temperatures without any hazardous chemicals (13). Moreover, the specificity of the enzymes towards the ester bonds in the PET allows its direct depolymerization from blended (mixed) plastic waste without pre-sorting (14). Since the first report of the cutinase TfH isolated from the actinomycete Thermobifida fusca being a PET hydrolase, research is ongoing to find the best PET hydrolase with the highest activity and stability. Engineering of PET hydrolases is crucial to make the enzymatic recycling process feasible and competitive. Different aspects have been employed to engineer PETases to create efficient enzymes with new properties including enhanced soluble protein expression, improved thermostability, higher reaction turnover rates with versatile substrates. Increased enzymatic thermostability is important for PETase activity, since ideally the enzyme should work around the glass transition (Tg) of the PET which is between 60- 70 °C, and the enzymes should therefore be robust to withstand this temperature. Enzyme synergy is one of the strategies to enhance the enzyme efficiency and increase the PET load in the reaction. One way to achieve enzyme synergy is to mix PET degrading enzymes with different properties and mechanistic activities. As an example, the limitation of Humicola insolens cutinase (HiC) to accumulate bis-(hydroxyethyl) terephthalate BHET and not fully degrade PET was overcome by addition of Candida antarctica lipase B (CALB) to the reaction. CALB is able to catalyze the last step in PET degradation converting BHET to TPA even with elevated BHET concentrations thus overcoming the intermediate accumulation problem, leading to a 7.7-fold increase in PET degradation efficiency. Similar to this concept, the PET degradation activity of bbPET0069, a cutinase-like Type I PET- degrading enzyme, was increased 12.6-fold when combined with CALB in the hydrolysis reaction mixture. However, sourcing, production and purification of several enzymes can be costly and cumbersome, and therefore impact the feasibility of methods of degrading plastic polymers requiring multiple enzymes. Moreover, plastic polymer degradation using current enzymes, alone or in combination, still suffers from low degradation efficiency, enzyme inhibition and lack of thermal stability. Finally, recombinant production of plastic polymer degrading enzymes in active form has been known to be challenging, with several enzymes not being amenable to large scale production. There remains a need for improved plastic degrading proteins which are capable of efficiently degrading plastic polymers, are thermostable and can be expressed recombinantly soluble form in commercially relevant productions systems. BRIEF SUMMARY OF THE INVENTION As discussed, plastic polymer degrading enzymes known in the art suffer from low efficiency, stability and substrate / product inhibition. Moreover, these enzymes may lack thermal stability at temperatures ideal for plastic polymer degradation and may be difficult to produce recombinantly in soluble forms in conventional expression hosts. The fusion proteins capable of degrading plastic polymers provided herein are comprised of two or more serine hydrolase domains and / or plastic binding domains and comprise the necessary features to efficiently and cost effectively be used in degradation of plastic polymers. A first aspect of the present invention, for the first time, provides a fusion protein capable of degrading a plastic polymer, wherein the fusion protein comprises two or more serine hydrolase domains. As shown in the below Examples, such fusion proteins are capable of degrading a variety of plastic polymers efficiently. A benefit of peptides of the present invention over plastic degrading enzymes known in the prior art is that such fusion proteins are highly efficient in degrading a variety of plastic polymers. A further benefit of the fusion protein is that it is thermostable at the required temperature and for sufficient time to efficiently degrade the plastic polymers. Finally, another benefit is that the fusion protein can be efficiently expressed recombinantly and in soluble form. The inventors surprisingly found that two or more serine hydrolase domains could be provided in a single peptide to improve plastic polymer degradation efficiency, thermostability and recombinant expression in soluble form. Polynucleotides encoding one or more of the fusion proteins and vectors comprising such polynucleotides are provided as a second and third aspects of the invention. A fourth aspect of the invention provides a cell comprising the fusion proteins, polynucleotides or vectors according to the invention. A fifth aspect of the invention provides a method of producing the fusion proteins according to the invention. A sixth and a seventh aspect of the invention relate to a method of degrading plastic polymers and uses of the fusion proteins of the invention in such method, respectively. Finally, an eight aspect of the invention provides a kit comprising a fusion protein according to the invention. DETAILED DESCRIPTION OF THE INVENTION A first aspect of the present invention relates to a fusion protein capable of degrading a plastic polymer, wherein the fusion protein comprises two or more serine hydrolase domains. The term “plastic polymer” or “plastic” is used herein to refer to organic polymers formed from chains of carbon atoms, with or without the attachment of oxygen, nitrogen or sulphur atoms. The term encompasses, but is not mean to be limited to, acrylics, polyesters, silicones, polyurethanes, and halogenated plastics. One skilled in the art will appreciate that polyesters encompass Polyethylene terephthalate (PET), Polybutylene adipate terephthalate (PBAT), Polybutylene terephthalate (PBT), Polybutylene succinate (PBS), Polytrimethylene terephthalate (PTT), Polyethylene furan-2,5-dicarboxylate (PEF), Polycaprolactone (PCL), Polylactic acid (PLA), Polyhydroxyalkanoate (PHA) and different combinations of the above. Unless clearly dictated otherwise by context, the term further comprises mixtures comprising of or essentially consisting of plastic polymers, such as waste mixtures consisting at least of 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, or 99% plastic polymers. The term “degradation” of a polymer is used herein to refer to any enzymatic, chemical and / or physical action resulting in a reduction of the mass and / or size of the polymer. One skilled in the art will appreciate that this may include, for example, removal of one or more monomers from said polymer. A “protein”, “peptide” or “polypeptide” is used herein interchangeably in its broadest sense to refer to a compound of two or more subunit amino acids, amino acid analogues, or other peptidomimetics. The term “peptide” thus includes short peptide sequences and also longer polypeptides and proteins, including variants and fusions thereof. As used herein, the term “amino acid” refers to either natural and / or unnatural or synthetic amino acids, including both D or L optical isomers, and amino acid analogues and peptidomimetics. It will be appreciated by persons skilled in the art that the term “amino acid”, as used herein, includes the standard twenty genetically-encoded amino acids and their corresponding stereoisomers in the ‘d’ form (as compared to the natural ‘l’ form), omega- amino acids other naturally-occurring amino acids, unconventional amino acids (e.g., α,α- disubstituted amino acids, N-alkyl amino acids, etc.) and chemically derivatised amino acids (see below). When an amino acid is being specifically enumerated, such as ‘alanine’ or ‘Ala’ or ‘A’, the term refers to both l-alanine and d-alanine unless explicitly stated otherwise. Other unconventional amino acids may also be suitable components for polypeptides of the present invention, as long as the desired functional property is retained by the polypeptide. For the peptides shown, each encoded amino acid residue, where appropriate, is represented by a single letter designation, corresponding to the trivial name of the conventional amino acid. As used herein, the term “fusion protein” or “chimeric protein” refers to a polypeptide comprising at least two domains. A “domain” is to be understood as any sequence or portion of a polypeptide which is characterised by a specific structural and / or functional feature (such as binding to an entity or catalysis of a reaction). By way of example, a protease domain should be understood as any sequence or polypeptide portion which comprises an amino acid sequence corresponding to a known protease, or which is capable of catalysing a reaction corresponding to that catalysed by a known protease. A catalytically active fusion protein may also be referred to as a “fusion enzyme”. One skilled in the art will appreciate that two or more domains may be peptides encoded by the same or different genes, or synthetic peptides. Each domain of the fusion protein may be chemically bonded to each other domain, for example by a peptide bond. Reference to enzyme or protein classes used throughout this specification should be understood based on the general common understanding of a person skilled in the art. In specific cases, enzymes or other protein classes may be referred to by reference to a classification system. Unless dictated otherwise by context, any reference to a classification number (e.g., EC 3) refers to the International Union for Biochemistry and Molecular Biology (IUBMB) enzyme classification system and the references refer to the enzyme commission (EC) number. One skilled in the art will appreciate that the term “serine hydrolase” refers to an enzyme that comprises a conserved serine nucleophile used to hydrolyse amide, ester, and thioester bonds in both protein and small molecule (metabolite) substrates. Serine hydrolases encompass members of the EC 3 class (according to the nomenclature), particularly of classes EC 3.1 and EC 3.4. Serine hydrolase domain(s) In some embodiments of the first aspect of the invention, one or more, two or more, three or more, four or more, five or more or six or more serine hydrolase domains of the fusion protein are catalytically active. In a preferred embodiment, all serine hydrolase domains are catalytically active. The term “catalytically active” is to be understood as the serin hydrolase domain being capable of catalysing at least one reaction. Catalytic activity may be quantified by determining the catalytic constant (kcat) for an enzyme or catalytic domain thereof and its substrate. Similarly, the specificity of catalytic activity of an enzyme or catalytic domain thereof towards its substrate may be defined in terms of the comparative catalytic constants (kcat) of the enzyme or catalytic domain thereof for its substrate as compared to the catalytic constant with respect to the enzyme or catalytic domain thereof and another non-substrate molecule. Typically, the kcatfor the enzyme or catalytic domain thereof with respect to the substrate will be at least 2-fold, preferably 5-fold, more preferably 10-fold greater than the kcatwith respect to the other, non-substrate. More preferably, the kcat will be 50-fold greater, even more preferably 100-fold greater, and yet more preferably 200-fold greater. The catalytic constant of an enzyme or a domain can be determined directly by methods well known in the art. The catalytic constant may, for example, be calculated using Michaelis-Menten Kinetics, where ^^^^^^^^^^^^^^^^= ,and Vmax is the maximum reaction rate and E is the enzyme concentration. These can in turn be calculated based on catalysis product concentrations, which can be determined experimentally by methods well known in the art. By way of example, to calculate the catalytic constant of the hydrolysis of PET to MHET, MHET concentration during the reaction may be determined by spectrophotometric assays, LC-MS, or HPLC. An enzyme or protein of the invention or catalytic domain thereof is preferably capable of catalysing its substrate with an efficiency that is at least two-fold, 10-fold, 50-fold, 100- fold or greater than its efficiency for catalysing another non-substrate molecule. Preferably, the catalytic domain will catalyse only its respective substrate (i.e. will be specific), as described above, and will not catalyse any other molecule in the environment, for example a mixture. However, it will be appreciated that some degree of off-target catalysis may be tolerated, and the skilled person will understand how to determine whether a particular catalytic activity is of the required specificity or not. A serine hydrolase domain, or any other enzyme or protein, may be catalytically inactive for example by mutation or removal of the catalytic site. A catalytically inactive enzyme or other protein may still be capable of specifically binding or associating with a second entity (i.e. a target). In some embodiments, the fusion protein comprises two serine hydrolase domains. In some embodiments, at least one serine hydrolase domain is an esterase, a lipase or a protease, or a catalytically active portion thereof. One skilled in the art will appreciate that esterases, lipases and proteases are known to be catalytically active against at least some plastic polymers and are thus suitable for inclusion as part of the fusion protein. By “esterase” we mean any enzyme capable of hydrolysing an ester bond. For example, esterases are encompassed by the EC 3.1 class. By “lipases” we mean any enzyme catalysing the hydrolysis of a fat (i.e., an ester of fatty acids, for example, triglycerides). By “protease” or “peptidases” we mean any enzyme capably of catalysing the hydrolysis of peptide bonds. For example, proteases are encompassed by the EC 3.4 class. In one embodiment, at least one serine hydrolase domain is a nylonase. By “nylonase” we mean any enzyme capable of hydrolysing nylon, preferably Nylon-6. For example, nylonases are encompassed by the EC 3.5 class, and particularly by the EC 3.5.1.46. In a particular embodiment, the at least one lipase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 9 or 10, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 9 or 10. In some embodiments, there is provided a variant which comprises up to and including 50 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 9 and 10), for example up to and including: 45, 40, 35, 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 (in particular 1 to 5) amino acid substitutions, insertions and / or deletions. One skilled in the art will appreciate that certain proteases, such as proteinase K, have been shown to be catalytically active against certain plastic polymers, such as Polylactic acid (PLA). Accordingly, in some embodiments at least one protease is proteinase K, or a catalytically active portion thereof. In some embodiments, at least one esterase is selected from the group consisting of a PETase, a MHETase, and a cutinase, or a catalytically active portion thereof. By “PETase” or “polyethylene terephthalate hydrolase” we refer to an esterase which is capable to catalysing the hydrolysis of polyethylene terephthalate (PET) monomeric mono- 2-hydroxyethyl terephthalate (MHET). One skilled in the art will appreciate that known PETases are hydrolases that act on the ester bonds and belong to the esterase class (EC 3.1.1., carboxylic ester hydrolases), including carboxylesterases (EC 3.1.1.1, carboxyl ester hydrolases, and EC 3.1.1.2, arylesterase), lipases (EC 3.1.1.3, triacylglycerol lipase) and cutinases (EC 3.1.1.74). Further, PETases may also be classified under the PET hydrolase class (EC 3.1.1.101) of enzymes. In some embodiments, the at least one PETase comprises or consists of an enzyme or a polypeptide other than a cutinase, a lipase or a protease. In a particular embodiment, the at least one PETase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 12, 13 or 14, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 12, 13 or 14. In some embodiments, there is provided a variant which comprises up to and including 50 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 12, 13, 14), for example up to and including: 45, 40, 35, 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 (in particular 1 to 5) amino acid substitutions, insertions and / or deletions. By “MHETase” we refer to any enzyme which is capable of catalysing the hydrolysis of the ester bond of Mono-(2-hydroxyethyl) terephthalic acid (MHET). One skilled in the art will appreciate that such reaction may form terephthalic acid and ethylene glycol. The only known enzyme having exclusively such catalytical activity (also known as MHETase) is classified under the EC 3.1.1.102 class. By “cutinase” we refer to any enzyme which is capable of catalysing the hydrolysis of cutin, particularly any enzyme of the EC 3.1.1.74 class. In a particular embodiment, the at least one cutinase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11. In some embodiments, there is provided a variant which comprises up to and including 50 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 1, 2, 3, 4, 5, 6, 7, 8 or 11), for example up to and including: 45, 40, 35, 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 (in particular 1 to 5) amino acid substitutions, insertions and / or deletions. As detailed in the Examples, the inventors have identified fusion proteins with particularly efficient plastic polymer degradation capabilities. A number of these comprised either a cutinase or a PETase domain. Accordingly, in some embodiments, at least one serine hydrolase domain comprises a cutinase or a PETase, or a catalytically active portion thereof. It will be appreciated by one skilled in the art, that fusion proteins comprising two or more serine hydrolase domains which are different may have increased or complementary plastic polymer degrading capabilities, for example by synergistically targeting the same or different moieties of said plastic polymer or by targeting the plastic polymer and a first degradation product of the same. Accordingly, in some embodiments the amino acid sequences of at least two serine hydrolase domains comprise no more than about 95% sequence identity, such as no more than about 90%, 85%, 80%, 75%, 70%, 65%, 60%, 55% or 50% sequence identity. In an alternative embodiment, the amino acid sequence of two or more serine hydrolase domains is the same. The amino acid sequences of the fusion proteins, serine hydrolase domains or other polypeptides recited herein are defined by a reference to an amino acid sequence which may comprise one or more amino acid substitution at one or more positions. As used herein, the term "substitution" refers to the replacement of an amino acid with another amino acid. Thus, the total number of amino acids remains the same. It will be appreciated that the modifications may occur within the amino acid sequences so long as the modification does not substantially reduce or otherwise modify the desired functional property of the reference polypeptide. Accordingly, in certain embodiments the amino acid sequences as provided herein may be unaltered, or may be variants having no more than one, two or three amino acid substitutions relative to the amino acid sequences recited herein. It is preferred that the amino acid substitution(s) be conservative residue substitution(s). The term "conservative amino acid substitution" is well known in the art and refers to the replacement of an amino acid with a different amino acid having similar biophysical properties. As used herein, the groupings of amino acids having similar biophysical properties are: (a) the nonpolar, hydrophobic amino acids consisting of glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), phenylalanine (Phe), tyrosine (Tyr), tryptophan (Trp), and methionine (Met); (b) the polar, neutral amino acids consisting of serine (Ser), threonine (Thr), asparagine (Asn), and glutamine (Gln); (c) the positively charged, basic amino acids consisting of arginine (Arg), lysine (Lys), and Histidine (His); and (d) the negatively charged, acidic amino acids consisting of aspartic acid (Asp) and glutamic acid (Glu). Thus, a conservative substitution is a substitution of a residue with another from its same group, i.e. (i) the substitution of a nonpolar, hydrophobic amino acid of group (a) with another amino acid of group (a); (ii) the substitution of a polar, neutral amino acid of group (b) with another amino acid of group (b); the substitution of a positively charged, basic amino acid of group (c) with another amino acid of group (c); and / or the substitution of a negatively charged, acidic amino acid of group (d) with another amino acid of group (d). It is appreciated that the amino acids Cys and Pro are not included in the above groupings and / or listing of conservative 5 substitutions because, as well known in the art, these residues are not suitable as general substituents. Where the residue Cys or Pro is to be substituted, as used herein a conservative substitution for Cys is with Ser or Ala, and for Pro is with Ala. As used herein, the term “sequence identity” or “% sequence identity” in connection with amino acid sequences of polypeptides / peptides and / or nucleic acid sequences or nucleic acid molecules describe the number of matches of identical amino acid or nucleic acid residues of two or more aligned sequences as compared to the number of residues making up the overall length of the compared sequences (or the overall compared portions thereof). Using an alignment of two or more sequences or sub-sequences, the percentage of residues that are the same may be determined when the (sub)sequences are compared and aligned for maximum correspondence over a window of comparison, or over a designated region as measured using a sequence comparison algorithm as known in the art, or when manually aligned and visually inspected. Non-limiting examples of algorithms for use in determining sequence identity include, for example, those based on the NCBI BLAST algorithm (Altschul et al., Nucleic Acids Res 25(1997), 3389-3402), CLUSTALW (Thompson, Nucl. Acids Res. 2(1994), 4673-4680) or FASTA (Pearson and Lipman, Proc. Natl. Acad. Sci., 85(1988), 2444). Although the FASTA algorithm typically does not consider internal non-matching deletions or additions in sequences, i.e. gaps, in its calculation, this can be corrected manually to avoid an overestimation of the % sequence identity. CLUSTALW, however, does take sequence gaps into account in its identity calculations. Also available are the BLAST and BLAST 2.0 algorithms (Altschul et al., Nucl Acids Res., 25(1977), 3389). A fusion protein according to the present invention may comprise any serine hydrolase domain selected from the exemplary peptides in Table A. Table A – Exemplary serine hydrolase domains. SEQ Classifi Name or Sequence ID cation originating NO: species 1 Cutinase Uncultured MSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGF bacteria GGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRL ASHGFVVLVINTNSRFDGPDSRASQLSAALNYLRTSSP SAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAA VPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPF YQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISW MKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQ 2 Cutinase Thermobifida MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFG fusca GGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIAS HGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASST VRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIP LTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKR FVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF 3 Cutinase Fusarium solani MRTTRDDLINGNSASCRDVIFIYARGSTETGNLGTLGP pisi SIASNLESAFGKDGVWIQGVGGAYRATLGDNALPRGT SSAAIREMLGLFQQANTKCPDATLIAGGYSQGAALAAA SIEDLDSAIRDKIAGTVLFGYTKNLQNRGRIPNYPADRT KVFCNTGDLVCTGSLIVAAPHLAYGPDARGPAPEFLIEK VRAVRGSA 4 Cutinase Saccharomonos MDNPYERGPDPTEDSIEAIRGPFSVATERVSSFASGFG pora viridis GGTIYYPRETDEGTFGAVAVAPGFTASQGSMSWYGER VASQGFIVFTIDTNTRLDQPGQRGRQLLAALDYLVERS DRKVRERLDPNRLAVMGHSMGGGGSLEATVMRPSLK ASIPLTPWNLDKTWGQVQVPTFIIGAELDTIASVRTHA KPFYESLPSSLPKAYMELDGATHFAPNIPNTTIAKYVIS WLKRFVDEDTRYSQFLCPNPTDRAIEEYRSTCPY 5 Cutinase Humicola MQLGAIENGLESGSANACPDAILIFARGSTEPGNMGIT insolens VGPALANGLESHIRNIWIQGVGGPYDAALATNFLPRGT SQANIDEGKRLFALANQKCPNTPVVAGGYSQGAALIA AAVSELSGAVKEQVKGVALFGYTQNLQNRGGIPNYPR ERTKVFCNVGDAVCTGTLIITPAHLSYTIEARGEAARFL RDRIRA Cutinase Thermomonosp MANPYQRGPDPTESLLRAARGPFAVSEQSVSRLSVSG ora curvata FGGGRIYYPTTTSQGTFGAIAISPGFTASWSSLAWLGP RLASHGFVVIGIETNTRLDQPDSRGRQLLAALDYLTQR SSVRNRVDASRLAVAGHSMGGGGTLEAAKSRTSLKA AIPIAPWNLDKTWPEVRTPTLIIGGELDSIAPVATHSIPF YNSLTNAREKAYLELNNASHFFPQFSNDTMAKFMISW MKRFIDDDTRYDQFLCPPPRAIGDISDYRDTCPHT Cutinase Thermobifida MNPYERGPNPTESMLEARSGPFSVSEERASRFGADGF alba GGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIA SHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASS AVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAI PLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFY NSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLK RFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF Cutinase Uncultured MQVVLGRVRSAGLLAALLALAAWALVWASPSAEAQSN bacteria PYQRGPNPTRSALTTDGPFSVATYSVSRLSVSGFGGG VIYYPTGTTLTFGGIAMSPGYTADASSLAWLGRRLASH GFVVIVINTNSRLDFPDSRASQLSAALNYLRTSSPSAV RARLDANRLAVAGHSMGGGATLRISEQIPTLKAGVPLT PWHTDKTFNTPVPQLIVGAEADTVAPVSQHAIPFYQNL PSTTPKVYVELDNATHFAPNSPNAAISVYTISWMKLWV DNDTRYRQFLCNVNDPALSDFRSNNRHCQ Lipase Thermomyces MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVG lanuginosus SDVTCSENVCPEVDAADATFLYSFEDSGLGDVTGLLAL DNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGC EGHVGFVTSWRSVADTIREQVQNAVNEHPDYRVVFTG HSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRAFA EFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEY WVTSGNDVPVTANDITVVEGIDSTDGNNQGNIPDIPS HLWYFGPISECD Lipase Streptomyces MHQHPHTQRRTRSLSSALAAVAVLVGIGLGPTPGAHA thermolilacinus ADNPYERGPAPTNASIEAVRGPYAVSQATVSSLAVTGF GGGTIYYPTTTSDGTFGAVAISPGYTGTQSSIAWLGPR LASQGFVVFTIDTNTTLDQPDSRGRQLLAALDYLTRVS PLRTRVDSTRLGVMGHSMGGGGSLEAAKSRPSLQAAI PLTPWNLDKTWPEIQTPTLIVGADGDSIAPVSSHAEPF YENLPSSLDRAYLELNGASHFAPNSSNTTIAKYSISWL KRFIDNDTRYEQFLCPLPRPSLTIEEYRGNCPHQS Esterase Thermobifida MANPYERGPNPTNSSIEALRGPFRVDEERVSRLQARGF / halotolerans GGGTIYYPTDNNTFGAVAISPGYTGTQSSISWLGERLA Cutinase SHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSS YSVRNRIDSSRLAAMGHSMGGGGTLRLAERRPDLQAA IPLTPWHTDKTWGSVRVPTLIIGAENDTIASVRSHSEP FYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWL KRFVDDDTRYTQFLCPGPSTGWGSDVEEYRSTCPF 12 PETase Ideonella MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGA sakaiensis GTVYYPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLA SHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNG TSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPS LKAAAPQAPWHSSTNFSSVTVPTLIFACENDSIAPVNS SALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALI GKKGVAWMKRFMDNDTRYSTFACENPNSTAVSDFRT ANCS 13 PETase Polyangium MQTNPYQRGPDPTTRDLEDSRGPFRYASTNVRSPSGY brachysporum GAGTIYYPTDVSGSVGAVAVVPGYLARQSSIRWWGPR LASHGFVVITLDTRSTSDQPASRSAQQMAALRQVVAL SETRSSPIYGKVDPNRLAVMGWSMGGGGTLISARDNP SLKAAVPFAPWHNTANFSGVQVPTLVIACENDTVAPIS RHASSFYNSFSSSLAKAYLEINNGSHTCANTGNSNQA LIGKYGVAWIKRFVDNDTRYSPFLCGAPHQADLRSSRL SEYRESCPY 14 PETase Uncultured MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYT bacteria VSTIRVSSLVPGFGGGTIHYPTNAGGGKMAGIVVIPGY LSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRR DQIEAALQYLVNQSNSSSSPISGMVDSSRLAAVGWS MGGGGTLQLAADGGIKAAIALAPWNSSINDFNRIQVP TLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGG DHWCANGGNIYSALLGKYGVSWMKLHLDQDTRYAPF LCGPNHAAQTLISEYRGNCPY The structural conformation may affect the plastic polymer degradation efficiency and / or the substrate selectivity of the fusion protein. Accordingly, in some embodiments the active sites of the at least two of the serine hydrolase domains are configured: - on the same plane, optionally perpendicular to each other; - projecting outwards from the joining cleft, optionally wherein said cleft results from the linkage between each hydrolase domain; - facing each other, optionally inside said joining client; or - at least one active site of one hydrolase domain extruding outwards and / or at lease one active site of one hydrolase domain facing said joining cleft. The skilled person will appreciate that a joining cleft may be present between each pair of two serine hydrolase domains and / or between a serine hydrolase domain and a polymer binding domain. Accordingly, a fusion protein comprising three serine hydrolase domains may comprise two joining clefts, a fusion protein comprising four serine hydrolase domains may comprise of three joining clefts and so on. By way of example, a fusion protein having the catalytic domains of two or more serine hydrolase domains in close proximity (for example facing each other) may have improved plastic degrading capabilities due to each catalytic domain acting on the same or proximal polymer structure. In an additional or alternative embodiment, the fusion protein comprise at least two serine hydrolase domains in the following order (N-terminal to C-terminal): (a) cutinase – cutinase; (b) cutinase – PETase; (c) cutinase – lipase; (d) PETase – PETase; (e) PETase – cutinase; (f) PETase – lipase; (g) lipase – lipase; (h) lipase – cutinase; or (i) lipase – PETase. Any of the above cutinase, PETase or lipase domains may be any of those described throughout this specification. It will be appreciated that the ordering of the serine hydrolase domains may impact the overall plastic degrading capabilities of the fusion protein. Similarly, the order may affect the heterologous expression efficiency from a host cell and / or the thermal stability of the fusion protein. Polymer binding domain(s) One skilled in the art will appreciate that the fusion protein of the invention may advantageously further comprise one or more polymer binding domain(s), which bind specifically to one or more plastic polymers. Such polymer binding domains may, for example, increase the plastic degrading capabilities of the fusion protein by promoting or increasing binding affinity of the fusion protein to one or more plastic polymers, or by prolonging or stabilizing binding between the fusion protein and one or more plastic polymers, particularly under certain conditions. Accordingly, in some embodiments, the fusion protein further comprises one or more polymer binding domain(s). By “bind specifically” we include the meaning that the domain (or the fusion protein comprising the domain) binds to its target in a manner that can be distinguished from binding to non-target domains (i.e. off-targets). For example, a domain that binds specifically may refer to a domain that binds with higher specificity for the intended target compared with that of a non-intended target. Specificity can be determined based on dissociation constant through routine experiments. Binding affinity or specificity in the context of a domain may be to a particular plastic polymer or a component thereof. Thus, in some embodiments, the one or more polymer binding domains are capable of binding one or more plastic polymer(s). In particular, the plastic polymer(s) may be selected from the group consisting of PET, PTT, PBT, PBS, PEF, PLA, PCL, PBAT and MHET and blends or combinations thereof. In some embodiments, the polymer blends or combinations are in amorphous, semi-crystalline or crystalline form. In some embodiments, the polymer is formed as a foam, powder, fibre, paste, flake or pellet. In a particular embodiment, the one or more polymer binding domains are selected from the group consisting of a hydrophobin, a cellulose binding domain, a carbohydrate binding module, an anchor peptide, an anchor linker peptide, PET binding domain and PHA binding domains. A fusion protein according to the present invention may comprise any polymer binding domain selected from the exemplary peptides in Table B. Table B – Exemplary polymer binding domains. SEQ Sequence ID NO 85 AQAAPGCRVDYAVTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNG TASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSWAGSNPTPASFSLNGTTCTGTVPT TSPTPTPTPTTPTPTPTPTPTPTPTVTPQPTSGFYVDPTTQGYR 86 GGGGSGGGGSYEMPSEEGYQDYEPEA 87 GGGGSGGGGSYSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 88 GGGGSGGGGSGGGGSGGGGSYEMPSEEGYQDYEPEA 89 GSAGSAAGSGYEMPSEEGYQDYEPEA 90 AAAAAAAAAAATFSVTSNWGSGYNFSIVIKNSGTTPIKNWKLEFDYNGNLTQVWDSK ISSKINNHYVITNAGWNGEIPPGGS 91 PPGGNRGTTTTRRPATTTGSSPGPMQYSAIVALFATLAVAAPAQEAAADIAILDGPCTA GVTNNIPMCCGSGILDLLYLDCETPTQATSVLNPLSAVCGRVGLQAKCCTLGIADLGV LCQDALPE 92 PPGGNRGTTTTRRPATTTGSSPGPMKFFAVAALFVASAMASPMGSEGCPGGLTNTVP LCCATNVLGVATLDCSTPTVPVPNVGIFQAHCASKGKQPVCCTVPVAGLGLLCQKPTG AQ 93 GGGGSGGGGSGGGGSGLWSTIKQKGKEAAIAAAKAAGQAALGAL 94 AEAAKEAAKEAAKAYSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 95 PPGGNRGTTTTRRPATTTGSSPGPTQSAFTCTATTASNYAHVQAGRAHDSGGIAYAN GSNQSMGLDNLFYTSTLAQTAAGYYIVGNCP 112 YEMPSEEGYQDYEPEA SEQ Sequence ID NO 113 YSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 114 AGSGYEMPSEEGYQDYEPEA 115 TFSVTSNWGSGYNFSIVIKNSGTTPIKNWKLEFDYNGNLTQVWDSKISSKINNHYVIT NAGWNGEIPPGGS 116 QYSAIVALFATLAVAAPAQEAAADIAILDGPCTAGVTNNIPMCCGSGILDLLYLDCETPT QATSVLNPLSAVCGRVGLQAKCCTLGIADLGVLCQDALPE 117 KFFAVAALFVASAMASPMGSEGCPGGLTNTVPLCCATNVLGVATLDCSTPTVPVPNVG IFQAHCASKGKQPVCCTVPVAGLGLLCQKPTGAQ 118 GLWSTIKQKGKEAAIAAAKAAGQAALGAL 119 YSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 120 AFTCTATTASNYAHVQAGRAHDSGGIAYANGSNQSMGLDNLFYTSTLAQTAAGYYIV GNCP 121 HYGQCGGIGYSGPTVCASGTTCQVLNPYYSQCL In some embodiments, the one or more polymer binding domains comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 85-96 (Table B), a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 85-96. In some embodiments, there is provided a variant which comprises up to and including 50 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 85-96), for example up to and including: 45, 40, 35, 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 (in particular 1 to 5) amino acid substitutions, insertions and / or deletions. Linker(s) In some embodiments, two or more serine hydrolase domains or at least one serine hydrolase domain and at least one polymer binding domain are coupled by a linker. In a particular embodiment, the linker is a polypeptide linker. In some embodiments, the linker is a rigid linker, a semi-rigid linker or a flexible linker. In some embodiments, the fusion protein comprises two or more serine hydrolase domains coupled by a linker comprising: (i) an (EAAAK)n motif wherein n is an integer greater than or equal to 2; or (ii) an amino acid sequence according to any one of SEQ ID NO: 69, 59, 60, 62, 66, or 70. One skilled in the art will appreciate that the use of peptide linkers in fusion proteins is well known in the art. The nature of a peptide linker may be important in the design of fusion proteins, as they connect different protein domains and influence the overall functionality and stability of the fusion protein. Flexible linkers, such as the commonly used glycine-serine linker, provide the necessary flexibility to allow the connected domains to fold and function independently. Rigid linkers, maintain a fixed distance between the domains, which can be beneficial for applications requiring precise spatial orientation and reduced interaction between the domains. Accordingly, in some embodiments the polypeptide linker is a rigid polypeptide linker. In an alternative embodiment, the polypeptide linker is a flexible polypeptide linker. In a particular embodiment, the linker is selected from the group consisting of a polyglycine linker, a polyalanine linker, an alanine-glycine linker, a glycine-serine linker, a histidine linker, threonine-serine linker, a glutamine linker, an asparagine linker. In a particular embodiment, the linker comprises between about 4 to about 40 amino acids, such as between about 5 to about 35 amino acids, about 5 to about 30 amino acids, about 5 to about 25 amino acids, about 5 to about 20 amino acids, about 8 to about 15 amino acids, or about 10 to about 12 amino acids. In some embodiments, the linker comprises an α-helical motif comprising the sequenceEAAAK (SEQ ID NO: 170). In some embodiments the sequence is (EAAAK)n, wherein n isan integer equal to or greater than 2, 3, 4, 5 or 6. In some embodiments, the one or more polymer binding domains are conjugated to one or more of the serine hydrolase domains via a linker. The nature of the peptide linker(s) may influence the structural conformation, the length, the molecular weight and / or other chemical or physical properties of the fusion protein. Therefore, particular peptide linker(s) may increase or improve stability, such as thermal stability, of a fusion protein. Similarly, fusion proteins comprising certain peptide linkers may be heterologously expressed more efficiently in one or more host cells. Accordingly, in some embodiments the fusion protein comprising a linker described herein has increased or improved stability, solubility and / or expression capabilities. In a particular embodiment, the stability, solubility and / or expression capabilities are improved compared to a fusion protein without a linker. In an additional or alternative embodiment, the fusion protein comprises a rigid linker and the stability and / or expression capabilities are improved compared to a fusion protein comprising a flexible linker. As used herein “stability” in referring to a fusion protein or another polypeptide refers to the conditions in which the polypeptide maintains its secondary and / or tertiary structure and / or the conditions in which the polypeptide maintains its function (for example, its polymer degradation activity). The term encompasses conditions such as temperature (thermal stability), osmotic pressure (osmotic stability), pH (pH stability) and similar conditions which will be apparent to one skilled in the art. “Improved stability” or “increased stability” thus refers to the polypeptide being stable in an increased number of conditions (i.e., higher temperature(s), higher or low pH condition(s), etc.). Methods of determining stability or increased stability of a polypeptide in specific conditions are well known in the art. By way of example, the catalytic activity of a polypeptide in specific conditions (e.g., at a specific temperature) can be determined as described throughout this specification and compared to that of a reference polypeptide at the same temperature. If the first polypeptide remains catalytically active in further conditions (i.e., increasing temperature(s)) compared to the reference polypeptide, said first polypeptide has increased or improved thermal stability compared to said reference polypeptide. Additionally or alternatively, the stability or improved stability of a polypeptide can be determined by performing a melting curve analysis, wherein the polypeptide is exposed to a changing condition (e.g., increasing temperature) and the tertiary / secondary polypeptide structure is monitored throughout. The condition at which the polypeptide structure no longer maintains its structure can thus be determined. Suitable methods for determining stability, for example by performing and determining melting curves by protein thermal shift are known in the art, for example from: Son HF, Joo S, Seo H, Sagong HY, Lee SH, Hong H, et al. Structural bioinformatics-based protein engineering of thermo-stable PETase from Ideonella sakaiensis. Enzyme Microb Technol. 2020;141:109656. An alternative method by scanning fluorimetry is also disclosed in: Blazquez-Sanchez P, Vargas JA, Furtado AA, Grinen A, Leonardo DA, Sculaccio SA, et al. Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange. Protein Sci. 2023;32(9):e4757. As used herein, “expression capability” refers to the concentration of a specific polypeptide that is produced and / or secreted by a host cell having one or more copies of a polynucleotide encoding said polypeptide during a specific time interval. The concentration of the specific polypeptide may only encompass polypeptides having a specific function (e.g., having catalytic activity) and / or secondary or tertiary polypeptide structure(s). Accordingly, “improved or increased expression capabilities” refers to a polypeptide that is produced in increased copy number and / or concentration by a host cell having one or more copies of a polynucleotide encoding said polypeptide and / or increased copy number and / or concentration of polypeptides having a specific function (e.g., catalytic activity) and / or polypeptide structure produced by such a host cell. Methods of measuring expression capabilities are well known in the art, for example the expression may be determined quantifying the polypeptide concentration produced by a host cell as described above in specific conditions and cultured for a specific amount of time. Protein quantification is well known in the art, and can be performed for example, using SDS-PAGE, BCA-assay, ELISA, HPLC or similar methods. The inventors have surprisingly identified particular linkers that increase the activity, thermostability and / or expression capabilities of the fusion proteins compared to other linkers. Particularly, the linkers increased the activity and expression capabilities of the fusion protein as compared to the individual serine hydrolase domains and / or plastic binding domains separately. Surprisingly, the inventors showed that when certain linkers were used in the fusion proteins these were insoluble or inactive polypeptides. A particularly advantageous linker is a rigid polypeptide linker of sequence PAVPPPA (SEQ ID NO: 70), which resulted in improved activity, thermostability and expression capabilities of the fusion protein. Other advantageous rigid linkers include EAAAK (SEQ ID NO: 68); PAPAP (SEQ ID NO: 64); and AEAAAKEAAAKA (SEQ ID NO: 63). A fusion protein according to the present invention may comprise any polypeptide linker domain selected from the exemplary peptides in Table C. Table C – Exemplary polypeptide linkers. SEQ ID NO Type Sequence 57 Flexible GGGGSGGGGSGGGGS 58 Flexible GGGGSGGGGSGGGGS 59 Flexible AGAGAGAGAGAGAGA 60 Flexible AGAGAG 61 Flexible GGGGS 62 Flexible GAGAGAGAGAGAGA 63 Rigid AEAAAKEAAAKA 64 Rigid PAPAP 65 Rigid APAPAPAPAPAPAPAPAPAP 66 Rigid EAAAKEAAKEAAK 67 Rigid AEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKEAAAKA 68 Rigid EAAAK 69 Rigid VFNQRKEHKGYMLA 70 Rigid PAVPPPA In some embodiments, the linker(s) comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 57-70 (Table C), a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 57-70. In some embodiments, the linkers comprise up to and including 5 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 57-70), for example up to and including: 5, 4, 3, 2 or 1 amino acid substitutions, insertions and / or deletions. In some embodiments, the linker comprises two or more, three or more, four or more, five or more, six or more, seven or more, eight or more, nine or more or ten or more copies of an amino acid sequence selected from any one of SEQ ID NO: 57-70 (Table C), a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 57-70. Specific fusion proteins The inventors have surprisingly identified a number of fusion proteins according to the first aspect of the invention, which are particularly advantageous in degrading one or more plastic polymers. Such particularly advantageous fusion proteins are demonstrated in detail in the appended non-limiting examples. In a particular embodiment, the fusion protein comprises an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28. In a preferred embodiment, the fusion protein comprises or consist of the amino acid sequence of any of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28, or a variant, fragment or derivative thereof. In some embodiments, there is provided a variant which comprises up to and including 50 amino acid substitutions, insertions or deletions relative to the sequences above (SEQ ID NOs: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28), for example up to and including: 45, 40, 35, 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 (in particular 1 to 5) amino acid substitutions, insertions and / or deletions. Each of the specified fusion proteins comprises two serine hydrolase domains. Exemplary fusion proteins are detailed below: Table D(i) – Exemplary fusion proteins according to the present invention SEQ Sequence ID NO 15 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGANPYQRGPDPTESLLRAARGPFAVSEQSVSRLSVSGFGGG RIYYPTTTSQGTFGAIAISPGFTASWSSLAWLGPRLASHGFVVIGIETNTRLDQPDSRGRQLLA ALDYLTQRSSVRNRVDASRLAVAGHSMGGGGTLEAAKSRTSLKAAIPIAPWNLDKTWPEVRT PTLIIGGELDSIAPVATHSIPFYNSLTNAREKAYLELNNASHFFPQFSNDTMAKFMISWMKRFI DDDTRYDQFLCPPPRAIGDISDYRDTCP 16 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFVFNQRKEHKGYMLASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGV IYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSAA LNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSV PVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKLW VDNDTRYRQFLCNVNDPALCDFRTNNRHCQ 17 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFAGAGAGTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGT VGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNG TSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPTLI FACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRF MDNDTRYSTFACENPNSTAVSDFRTANCS 18 MSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTA DASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRL AVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIP FYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALC DFRTNNRHCQEAAAKEAAKEAAKNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVS TIRVSSLVPGFGGGTIHYPTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTN TIYDQPSQRRDQIEAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGI KAAIALAPWNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHW CANGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPY SEQ Sequence ID NO 19 MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTAR QSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSSSPIYGKVDTA RMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPTLIFACENDSIAPVNS SALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACE NPNSTAVSDFRTANCSGAGAGAGAGAGAGANPYERGPNPTDALLEASSGPFSVSEENVSRL SASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSR AEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLN KNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSV AWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF 20 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFVFNQRKEHKGYMLATNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVY YPTNAGGTVGAIAIVPGYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAAL RQVASLNGTSSSPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNF SSVTVPTLIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKG VAWMKRFMDNDTRYSTFACENPNSTAVSDFRTANCS 21 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFEAAAKEAAKEAAKANPYQRGPDPTESLLRAARGPFAVSEQSVSRLSVSGFGGGRI YYPTTTSQGTFGAIAISPGFTASWSSLAWLGPRLASHGFVVIGIETNTRLDQPDSRGRQLLAA LDYLTQRSSVRNRVDASRLAVAGHSMGGGGTLEAAKSRTSLKAAIPIAPWNLDKTWPEVRTP TLIIGGELDSIAPVATHSIPFYNSLTNAREKAYLELNNASHFFPQFSNDTMAKFMISWMKRFID DDTRYDQFLCPPPRAIGDISDYRDTCP 22 MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTAR QSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSSSPIYGKVDTA RMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPTLIFACENDSIAPVNS SALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACE NPNSTAVSDFRTANCSPAVPPPANPYERGPNPTNSSIEALRGPFRVDEERVSRLQARGFGGGT IYYPTDNNTFGAVAISPGYTGTQSSISWLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAAL DYMVEDSSYSVRNRIDSSRLAAMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVR VPTLIIGAENDTIASVRSHSEPFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFV DDDTRYTQFLCPGPSTGWGSDVEEYRSTCPF 23 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQ SEQ Sequence ID NO 24 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQ 25 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFVFNQRKEHKGYMLAANPYQRGPDPTESLLRAARGPFAVSEQSVSRLSVSGFGGG RIYYPTTTSQGTFGAIAISPGFTASWSSLAWLGPRLASHGFVVIGIETNTRLDQPDSRGRQLLA ALDYLTQRSSVRNRVDASRLAVAGHSMGGGGTLEAAKSRTSLKAAIPIAPWNLDKTWPEVRT PTLIIGGELDSIAPVATHSIPFYNSLTNAREKAYLELNNASHFFPQFSNDTMAKFMISWMKRFI DDDTRYDQFLCPPPRAIGDISDYRDTCP 26 MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHYPTNAG GGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQIEAALQYLVN QSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAPWNSSINDFNRIQVP TLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCANGGNIYSALLGKYGVSWM KLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYGAGAGAGAGAGAGANPYERGPNPTDALL EASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHG FVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLAS QRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDG ATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF 27 MQLGAIENGLESGSANACPDAILIFARGSTEPGNMGITVGPALANGLESHIRNIWIQGVGGPY DAALATNFLPRGTSQANIDEGKRLFALANQKCPNTPVVAGGYSQGAALIAAAVSELSGAVKE QVKGVALFGYTQNLQNRGGIPNYPRERTKVFCNVGDAVCTGTLIITPAHLSYTIEARGEAARFL RDRIRAGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIY YPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSAAL NYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTSVP VLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKLW VDNDTRYRQFLCNVNDPALCDFRTNNRHCQ 28 MANPYERGPNPTNSSIEALRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTG TQSSISWLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSSRL AAMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIASVRSHSE PFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYTQFLCPGPSTGWG SDVEEYRSTCPFAGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSG FGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRA SQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDK TFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTIS WMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQ SEQ Sequence ID NO 173 MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHYPTNAG GGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQIEAALQYLVN QSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAPWNSSINDFNRIQVP TLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCANGGNIYSALLGKYGVSWM KLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYVFNQRKEHKGYMLANPYERGPNPTDALLE ASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGTEASIAWLGERIASHGF VVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAVMGHSMGGGGTLRLAS QRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDG ATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF Table D(ii) – Exemplary fusion proteins comprising polymer binding domains according to the present invention SEQ Sequence IDNO 132 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGSAGSAAGSGYEMPSEEGYQDYEPEA 133 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQAQAAPGCRVDYAVTNQWPGGFGANVTITN LGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSW AGSNPTPASFSLNGTTCTGTVPTTSPTPTPTPTTPTPTPTPTPTPTPTVTPQPTSGFYVDPTTQG YR 134 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTSWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTRRPATTTGSSPGPMKFFAV AALFVASAMASPMGSEGCPGGLTNTVPLCCATNVLGVATLDCSTPTVPVPNVGIFQAHCASK GKQPVCCTVPVAGLGLLCQKPTGAQ SEQ Sequence ID NO 135 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGGGGSGGGGSYEMPSEEGYQDYEPEA 136 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTRRPATTTGSSPGPTQSAFT CTATTASNYAHVQAGRAHDSGGIAYANGSNQSMGLDNLFYTSTLAQTAAGYYIVGNCP 137 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTRRPATTTGSSPGPMQYSAI VALFATLAVAAPAQEAAADIAILDGPCTAGVTNNIPMCCGSGILDLLYLDCETPTQATSVLNPL SAVCGRVGLQAKCCTLGIADLGVLCQDALPE 138 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTRRPATTTGSSPGPTQSHYG QCGGIGYSGPTVCASGTTCQVLNPYYSQCL SEQ Sequence ID NO 139 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQTFSVTSNWGSGYNFSIVIKNSGTTPIKNWK LEFDYNGNLTQVWDSKISSKINNHYVITNAGWNGEIPPGGS 140 MNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAISPGYTGT EASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVRSRIDSSRLAV MGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGADLDTIAPVATHAKPFY NSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVE EYRSTCPFGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGG VIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQLSA ALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAAVPLTPWHTDKTFNTS VPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNSNNAAISVYTISWMKL WVDNDTRYRQFLCNVNDPALCDFRTNNRHCQAEAAKEAAKEAAKAYSRCQLQGFNCVVRSY GLPTIPCCRGLTCRSYFPGSTYGRCQRY 141 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGGGGSGGGGSY SRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 142 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGANPYQRGPNPTRSALTADGPFS VATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVIN TNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLK AAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAP NSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGGGGSGGGGSYE MPSEEGYQDYEPEA SEQ Sequence ID NO 143 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGGGGSGGGGSG GGGSGLWSTIKQKGKEAAIAAAKAAGQAALGAL 144 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTR RPATTTGSSPGPMKFFAVAALFVASAMASPMGSEGCPGGLTNTVPLCCATNVLGVATLDCST PTVPVPNVGIFQAHCASKGKQPVCCTVPVAGLGLLCQKPTGAQ 145 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTR RPATTTGSSPGPTQSAFTCTATTASNYAHVQAGRAHDSGGIAYANGSNQSMGLDNLFYTSTL AQTAAGYYIVGNCP 146 PVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFEDS GLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWRSV ADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRAFA EFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDSTD GNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGANPYQRGPNPTRSALTADGPFSVA TYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTN SRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSLKAA VPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWAPNS NNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQGSAGSAAGSGYEMP SEEGYQDYEPEA SEQ Sequence ID NO 147 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQAQAAPGCRVDYA VTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPW NGSIPTGGTASFGFNGSWAGSNPTPASFSLNGTTCTGTVPTTSPTPTPTPTTPTPTPTPTPTPT PTVTPQPTSGFYVDPTTQGYR 148 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQPPGGNRGTTTTR RPATTTGSSPGPMQYSAIVALFATLAVAAPAQEAAADIAILDGPCTAGVTNNIPMCCGSGILDL LYLDCETPTQATSVLNPLSAVCGRVGLQAKCCTLGIADLGVLCQDALPE 149 MRPVRRAVPQDLLDQFELFSQYSAAAYCAANNHAPVGSDVTCSENVCPEVDAADATFLYSFE DSGLGDVTGLLALDNTNKLIVLSFRGSRSVENWIANLAADLTEISDICSGCEGHVGFVTSWR SVADTIREQVQNAVNEHPDYRVVFTGHSLGGALATIAAAALRGNGYNIDVFSYGAPRVGNRA FAEFLTAQTGGTLYRITHTNDIVPRLPPRDWGYSHSSPEYWVTSGNDVPVTANDITVVEGIDS TDGNNQGNIPDIPSHLWYFGPISECDGAGAGAGAGAGAGASNPYQRGPNPTRSALTADGPF SVATYTVSRLSVSGFGGGVIYYPTGTSLTFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVI NTNSRFDGPDSRASQLSAALNYLRTSSPSAVRARLDANRLAVAGHSMGGGGTLRIAEQNPSL KAAVPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELCNASHWA PNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCDFRTNNRHCQAEAAKEAAKEAA KAYSRCQLQGFNCVVRSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 150 MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVPGYTAR QSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSSSPIYGKVDTA RMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPTLIFACENDSIAPVNS SALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVAWMKRFMDNDTRYSTFACE NPNSTAVSDFRTANCAPAVPPPANPYERGPNPTNSSIEALRGPFRVDEERVSRLQARGFGGGT IYYPTDNNTFGAVAISPGYTGTQSSISWLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAAL DYMVEDSSYSVRNRIDSSRLAAMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVR VPTLIIGAENDTIASVRSHSEPFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFV DDDTRYTQFLCPGPSTGWGSDVEEYRSTCPFGGGGSGGGGSYSRCQLQGFNCVVRSYGLPT IPCCRGLTCRSYFPGSTYGRCQRY Characteristics of the fusion proteins of the invention As detailed throughout this specification, the inventors have surprisingly identified fusion proteins being particularly advantageous for degrading one or more plastic polymers. In some embodiments, the fusion protein has increased or improved thermal stability. Particularly, in some embodiments, the fusion protein has increased or improved thermal stability compared to each constituent serine hydrolase domain separately. As previously discussed, fusion proteins having particularly increased or improved thermal stability are particularly useful in methods of degrading plastic polymers. Without wanting to be bound by theory, having increased thermal stability allows the fusion proteins to be catalytically active at the glass transition temperature of the plastic polymers, thereby increasing plastic polymer degradation activity. Methods of determining thermal stability are known in the art and described throughout this specification. Additionally or alternatively, the fusion proteins having increased or improved thermal stability may also be those remaining catalytically active after exposure to a particular temperature for increased duration. By way of example, a fusion protein being catalytically active after a 2-hour exposure to a particular temperature is to be understood as having increased thermal stability compared to a different protein which is no longer catalytically active after exposure to a particular temperature for the same time duration. In some embodiments, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 37°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 40°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 45°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 50°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 55°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 60°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 65°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 70°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 75°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 80°C. In an additional or alternative embodiment, the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 90°C or at a temperature above 90°C. In a preferred embodiment, the fusion protein is catalytically active after 72 hours at 60°C. Methods of determining catalytic activity of plastic polymer degrading enzymes such as the fusion proteins of the invention are well known in the art. For example, catalytic activity may be measured by determining release of one or more monomers of a plastic polymer incubated in the presence of said enzyme under specific conditions. In some embodiments, catalytic activity is determined by measuring monomer release from a plastic polymer incubated in the presence of the fusion protein. In some embodiments, the plastic polymer is PET and / or the monomer is terephthalic acid. Methods of measuring monomer release from a sample are well established in the art, including for example HPLC. In an additional or alternative embodiment, the fusion protein has increased or improved plastic polymer degradation activity. In preferred embodiments, the fusion protein has increased or improved degradation activity of at least one plastic polymer selected from the group consisting of PET, PTT, PBT, PEF, PLA, PCL, PBAT, PHA, MHET, blends or combinations thereof and mixed plastic waste. In some embodiments, the polymer blends or combinations are in amorphous, semi-crystalline or crystalline form. In some embodiments, the polymer is formed as a foam, powder, fibre, paste, flake or pellet. The fusion protein may have increased or improved degradation activity of two or more, three or more, four or more, five or more, or six or more plastic polymers, optionally wherein the plastic polymers are selected from the group above. In some embodiments, the fusion proteins have increased or improved plastic degradation activity of all polymers from the group above. In some embodiments, the plastic polymer is PET. Particularly, in some embodiments, the PET may be in amorphous, semi-crystalline or crystalline form. Methods of determining the plastic polymer degradation activity of a polypeptide are known in the art. For example, plastic polymer degradation can be determined by contacting the polypeptide (e.g., the fusion protein) with an exemplary plastic polymer (e.g., PET), optionally in solution. The PET can, for example, be in the form of powder, film, pellet, fiber or lump, and as a pure material or mixed plastic waste. PET degradation can be performed in a buffer solution such as 50 – 500 mM Tris-HCl, 50 – 500 mM potassium or sodium phosphate buffer with pH 8 by polypeptide. PET concentration can be 5 g – 500 g / L in the buffer solution. The polypeptides may be purified, for example at a concentration in the range of 0.001 µM – 100mM in the solution. The reaction may be performed at range of 60 – 75 °C. The monomers released from the hydrolysis of the plastic polymer (e.g., PET) can be quantified using HPLC, for example using a UV detector at 260 nm. One skilled in the art will appreciate that different HPLC columns, mobile and stationary phases may be used to separate and determine the concentration of plastic polymer derived monomers. For example, an Aminex HPX-87H column may be used for the separation of ethylene glycol using 0.05 % H2SO4 as mobile phase. Terephthalic acid may be analysed on a C18 column using 20 % acetonitrile with 0.02 % formic acid as mobile phase. The structure of the plastic polymer derived monomers may further be confirmed by Nuclear Magnetic Resonance (NMR). In some embodiments, the fusion protein has increased or improved plastic polymer degradation compared to each constituent serine hydrolase domain separately. In some embodiments, the fusion protein has increased or improved plastic polymer degradation compared to each constituent serine hydrolase domain separately and upon concomitant / sequential additions of said fusion protein. In some embodiments, the fusion protein has increased or improved plastic polymer degradation compared to a reference plastic degrading enzyme. It will be appreciated that the reference plastic degrading enzyme may be any enzyme capable of degrading plastic that has been characterized for its ability to degrade plastic. Many such enzymes are known in the art and will be apparent to the skilled person. By way of example, Leaf- branch Compost Cutinase (LCC) is a known enzyme capable of degrading PET. In some embodiments, LCC comprises or consists of the amino acid sequence according to SEQ ID NO: 1. Accordingly, in some embodiments, the fusion protein of the invention has similar, equal, increased or improved plastic polymer degradation compared to LCC, or a variant or derivative thereof. As detailed above, enzymatic plastic polymer degradation using plastic degrading enzymes known in the art may require pre-treatment of the plastic polymer. As used herein the term “pre-treatment” refers to any action or condition carried out or performed on a plastic polymer or a mixture comprising plastic polymers (i.e., waste mixtures) that is required for efficient subsequent plastic polymer degradation by a plastic polymer degrading enzyme. By way of example, efficient plastic polymer degradation of mixtures comprising plastic polymers and organic material may require pre-treatment with cellulases or other enzymes capable of degrading organic material. In some embodiments, the fusion protein of the invention has increased or improved plastic polymer degradation activity when one or more of the plastic polymers has not been subject to pre-treatment. The pre-treatment may comprise at least one step selected from the group consisting of an enzymatic treatment, a mechanical treatment, a chemical treatment and heat treatment. It will be appreciated that suitable pre-treatment methods of plastic polymers and / or plastic polymer containing mixtures are well known in the art. Additionally, it will be appreciated that the specific pre-treatment method selected by one skilled in the art will depend on the precise nature of the plastic polymer and or mixture containing plastic polymers. In a particular embodiment, the mechanical treatment comprises one or more of grinding, milling, extrusion, spinning, freezing, ultrasound treatment, and / or microwave treatment. In an additional or alternative embodiment, the chemical treatment comprises one or more of pyrolysis, gasification, hydro-cracking, and / or a Fenton reaction. In some embodiments, the fusion protein of the invention has increased or improved resistance to substrate inhibition or product inhibition. As used herein, substrate inhibition refers to a catalytic polypeptide having decreased or reduced catalytic activity due to the presence and / or concentration of a substrate for said catalytic polypeptide. Product inhibition refers to a catalytic polypeptide having decreased or reduced catalytic activity due to the presence and / or concentration of a product produced by said catalytic activity of the polypeptide. Without wanting to be bound by theory, substrate and product inhibition may occur due to unspecific binding of the substrate of product to the catalytic polypeptide such that the catalytic activity is impeded or reduced, for example due to the catalytic site being sterically blocked. One skilled in the art will appreciate that substrate and / or product inhibition of a catalytic polypeptide, such as the fusion proteins of the invention, may be measured by determining the catalytic activity of the polypeptide, such as the plastic degrading activity of the fusion proteins, in the presence of varying concentration of the product, such as the plastic polymers, or the substrate, such as plastic polymer derived monomers. Nucleic acids, vectors and cells of the invention It will be apparent to the skilled person that as the invention provides fusion proteins and polypeptides, the invention also provides corresponding polynucleotides that comprise or consist of a sequence that encodes the peptides of the invention (or domains thereof which are subsequently fused to a peptide of the present invention). The invention provides a DNA polynucleotide that comprises or consists of a sequence that encodes at least one peptide of the invention or at least one domain thereof. The invention also provides an RNA polynucleotide that comprises or consists of a sequence that encodes at least one peptide of the invention or at least one domain thereof. The skilled person will appreciate that a polynucleotide, for example a DNA or RNA polynucleotide, may comprise one or more modifications, for example a phosphorothioate modification. The polynucleotide may also comprise one or more other features, for example a promoter, terminator, or a tag for instance, for example the features typical of an expression cassette. It will be apparent that nucleic acids encoding any polypeptide or fragment thereof of the present invention may not correspond those encoding the same or similar polypeptide or fragment thereof as expressed in nature by the organism from which they derive. Accordingly, the nucleic acids may be altered to introduce substitutions or mutations or may be altered to optimize the expression of the polypeptide or fragment thereof in a specific host cell (e.g., through codon optimization). Exemplary nucleic acid sequences encoding the serine hydrolase domains disclosed in Table A include those shown in Table E. Table E - Exemplary nucleotide sequences encoding the serine hydrolase domains SEQ Classifi Name or Sequence ID cation originating NO: species 29 Cutinase Uncultured ATGAGCAACCCGTATCAGCGCGGCCCGAACCCGACCCGCAG bacteria CGCGCTGACCGCGGATGGCCCGTTTAGCGTGGCGACCTATA CCGTGAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCGT GATTTATTATCCGACCGGCACCAGCCTGACCTTTGGCGGCAT TGCGATGAGCCCGGGCTATACCGCGGATGCGAGCAGCCTGG CGTGGCTGGGCCGCCGCCTGGCGAGCCATGGCTTTGTGGTG CTGGTGATTAACACCAACAGCCGCTTTGATGGCCCGGATAGC CGCGCGAGCCAGCTGAGCGCGGCGCTGAACTATCTGCGCAC CAGCAGCCCGAGCGCGGTGCGCGCGCGCCTGGATGCGAAC CGCCTGGCGGTGGCGGGCCATAGCATGGGCGGCGGCGGCA CCCTGCGCATTGCGGAACAGAACCCGAGCCTGAAAGCGGCG GTGCCGCTGACCCCGTGGCATACCGATAAAACCTTTAACACC AGCGTGCCGGTGCTGATTGTGGGCGCGGAAGCGGATACCGT GGCGCCGGTGAGCCAGCATGCGATTCCGTTTTATCAGAACCT GCCGAGCACCACCCCGAAAGTGTATGTGGAACTGTGCAACG CGAGCCATTGGGCGCCGAACAGCAACAACGCGGCGATTAGC GTGTATACCATTAGCTGGATGAAACTGTGGGTGGATAACGAT ACCCGCTATCGCCAGTTTCTGTGCAACGTGAACGATCCGGCG CTGTGCGATTTTCGCACCAACAACCGCCATTGCCAG 30 Cutinase Thermobifid ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCT a fusca GCTGGAAGCGAGCAGCGGCCCGTTTAGCGTGAGCGAAGAAA ACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGCAC SEQ Classifi Name or Sequence ID cation originating NO: species CATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGC GATTAGCCCGGGCTATACCGGCACCGAAGCGAGCATTGCGT GGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGGTGATT ACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGC GCGGAACAGCTGAACGCGGCGCTGAACCATATGATTAACCG CGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCAGCCGCC TGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCT GCGCCTGGCGAGCCAGCGCCCGGATCTGAAAGCGGCGATTC CGCTGACCCCGTGGCATCTGAACAAAAACTGGAGCAGCGTG ACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATT GCGCCGGTGGCGACCCATGCGAAACCGTTTTATAACAGCCT GCCGAGCAGCATTAGCAAAGCGTATCTGGAACTGGATGGCG CGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCA AATATAGCGTGGCGTGGCTGAAACGCTTTGTGGATAACGATA CCCGCTATACCCAGTTTCTGTGCCCGGGCCCGCGCGATGGC CTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTT 31 Cutinase Fusarium ATGCGCACCACCCGCGATGATCTGATTAACGGCAACAGCGC solani pisi GAGCTGCCGCGATGTGATTTTTATTTATGCGCGCGGCAGCAC CGAAACCGGCAACCTGGGCACCCTGGGCCCGAGCATTGCGA GCAACCTGGAAAGCGCGTTTGGCAAAGATGGCGTGTGGATT CAGGGCGTGGGCGGCGCGTATCGCGCGACCCTGGGCGATA ACGCGCTGCCGCGCGGCACCAGCAGCGCGGCGATTCGCGA AATGCTGGGCCTGTTTCAGCAGGCGAACACCAAATGCCCGG ATGCGACCCTGATTGCGGGCGGCTATAGCCAGGGCGCGGCG CTGGCGGCGGCGAGCATTGAAGATCTGGATAGCGCGATTCG CGATAAAATTGCGGGCACCGTGCTGTTTGGCTATACCAAAAA CCTGCAGAACCGCGGCCGCATTCCGAACTATCCGGCGGATC GCACCAAAGTGTTTTGCAACACCGGCGATCTGGTGTGCACC GGCAGCCTGATTGTGGCGGCGCCGCATCTGGCGTATGGCCC GGATGCGCGCGGCCCGGCGCCGGAATTTCTGATTGAAAAAG TGCGCGCGGTGCGCGGCAGCGCG 32 Cutinase Saccharomo ATGGATAACCCGTATGAACGCGGCCCGGATCCGACCGAAGA nospora TAGCATTGAAGCGATTCGCGGCCCGTTTAGCGTGGCGACCG viridis AACGCGTGAGCAGCTTTGCGAGCGGCTTTGGCGGCGGCACC ATTTATTATCCGCGCGAAACCGATGAAGGCACCTTTGGCGCG GTGGCGGTGGCGCCGGGCTTTACCGCGAGCCAGGGCAGCA TGAGCTGGTATGGCGAACGCGTGGCGAGCCAGGGCTTTATT GTGTTTACCATTGATACCAACACCCGCCTGGATCAGCCGGGC CAGCGCGGCCGCCAGCTGCTGGCGGCGCTGGATTATCTGGT GGAACGCAGCGATCGCAAAGTGCGCGAACGCCTGGATCCGA ACCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGG CAGCCTGGAAGCGACCGTGATGCGCCCGAGCCTGAAAGCGA GCATTCCGCTGACCCCGTGGAACCTGGATAAAACCTGGGGC CAGGTGCAGGTGCCGACCTTTATTATTGGCGCGGAACTGGA TACCATTGCGAGCGTGCGCACCCATGCGAAACCGTTTTATGA AAGCCTGCCGAGCAGCCTGCCGAAAGCGTATATGGAACTGG ATGGCGCGACCCATTTTGCGCCGAACATTCCGAACACCACCA TTGCGAAATATGTGATTAGCTGGCTGAAACGCTTTGTGGATG AAGATACCCGCTATAGCCAGTTTCTGTGCCCGAACCCGACCG ATCGCGCGATTGAAGAATATCGCAGCACCTGCCCGTAT 33 Cutinase Humicola ATGCAGCTGGGCGCGATTGAAAACGGCCTGGAAAGCGGCAG insolens CGCGAACGCGTGCCCGGATGCGATTCTGATTTTTGCGCGCG GCAGCACCGAACCGGGCAACATGGGCATTACCGTGGGCCCG SEQ Classifi Name or Sequence ID cation originating NO: species GCGCTGGCGAACGGCCTGGAAAGCCATATTCGCAACATTTG GATTCAGGGCGTGGGCGGCCCGTATGATGCGGCGCTGGCG ACCAACTTTCTGCCGCGCGGCACCAGCCAGGCGAACATTGA TGAAGGCAAACGCCTGTTTGCGCTGGCGAACCAGAAATGCC CGAACACCCCGGTGGTGGCGGGCGGCTATAGCCAGGGCGC GGCGCTGATTGCGGCGGCGGTGAGCGAACTGAGCGGCGCG GTGAAAGAACAGGTGAAAGGCGTGGCGCTGTTTGGCTATAC CCAGAACCTGCAGAACCGCGGCGGCATTCCGAACTATCCGC GCGAACGCACCAAAGTGTTTTGCAACGTGGGCGATGCGGTG TGCACCGGCACCCTGATTATTACCCCGGCGCATCTGAGCTAT ACCATTGAAGCGCGCGGCGAAGCGGCGCGCTTTCTGCGCGA TCGCATTCGCGCG 34 Cutinase Thermomon ATGGCGAACCCGTATCAGCGCGGCCCGGATCCGACCGAAAG ospora CCTGCTGCGCGCGGCGCGCGGCCCGTTTGCGGTGAGCGAA curvata CAGAGCGTGAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCG GCCGCATTTATTATCCGACCACCACCAGCCAGGGCACCTTTG GCGCGATTGCGATTAGCCCGGGCTTTACCGCGAGCTGGAGC AGCCTGGCGTGGCTGGGCCCGCGCCTGGCGAGCCATGGCTT TGTGGTGATTGGCATTGAAACCAACACCCGCCTGGATCAGCC GGATAGCCGCGGCCGCCAGCTGCTGGCGGCGCTGGATTATC TGACCCAGCGCAGCAGCGTGCGCAACCGCGTGGATGCGAGC CGCCTGGCGGTGGCGGGCCATAGCATGGGCGGCGGCGGCA CCCTGGAAGCGGCGAAAAGCCGCACCAGCCTGAAAGCGGC GATTCCGATTGCGCCGTGGAACCTGGATAAAACCTGGCCGG AAGTGCGCACCCCGACCCTGATTATTGGCGGCGAACTGGAT AGCATTGCGCCGGTGGCGACCCATAGCATTCCGTTTTATAAC AGCCTGACCAACGCGCGCGAAAAAGCGTATCTGGAACTGAA CAACGCGAGCCATTTTTTTCCGCAGTTTAGCAACGATACCAT GGCGAAATTTATGATTAGCTGGATGAAACGCTTTATTGATGA TGATACCCGCTATGATCAGTTTCTGTGCCCGCCGCCGCGCGC GATTGGCGATATTAGCGATTATCGCGATACCTGCCCGCATAC C 35 Cutinase Thermobifid ATGAACCCGTATGAACGCGGCCCGAACCCGACCGAAAGCAT a alba GCTGGAAGCGCGCAGCGGCCCGTTTAGCGTGAGCGAAGAAC GCGCGAGCCGCTTTGGCGCGGATGGCTTTGGCGGCGGCAC CATTTATTATCCGCGCGAAAACAACACCTATGGCGCGATTGC GATTAGCCCGGGCTATACCGGCACCCAGAGCAGCATTGCGT GGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGGTGATT GCGATTGATACCAACACCACCCTGGATCAGCCGGATAGCCG CGCGCGCCAGCTGAACGCGGCGCTGGATTATATGCTGACCG ATGCGAGCAGCGCGGTGCGCAACCGCATTGATGCGAGCCGC CTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCC TGCGCCTGGCGAGCCAGCGCCCGGATCTGAAAGCGGCGATT CCGCTGACCCCGTGGCATCTGAACAAAAGCTGGCGCGATAT TACCGTGCCGACCCTGATTATTGGCGCGGAATATGATACCAT TGCGAGCGTGACCCTGCATAGCAAACCGTTTTATAACAGCAT TCCGAGCCCGACCGATAAAGCGTATCTGGAACTGGATGGCG CGAGCCATTTTGCGCCGAACATTACCAACAAAACCATTGGCA TGTATAGCGTGGCGTGGCTGAAACGCTTTGTGGATGAAGATA CCCGCTATACCCAGTTTCTGTGCCCGGGCCCGCGCACCGGC CTGCTGAGCGATGTGGAAGAATATCGCAGCACCTGCCCGTTT 36 Cutinase Uncultured ATGCAGGTGGTGCTGGGCCGCGTGCGCAGCGCGGGCCTGC bacteria TGGCGGCGCTGCTGGCGCTGGCGGCGTGGGCGCTGGTGTG SEQ Classifi Name or Sequence ID cation originating NO: species GGCGAGCCCGAGCGCGGAAGCGCAGAGCAACCCGTATCAG CGCGGCCCGAACCCGACCCGCAGCGCGCTGACCACCGATGG CCCGTTTAGCGTGGCGACCTATAGCGTGAGCCGCCTGAGCG TGAGCGGCTTTGGCGGCGGCGTGATTTATTATCCGACCGGC ACCACCCTGACCTTTGGCGGCATTGCGATGAGCCCGGGCTA TACCGCGGATGCGAGCAGCCTGGCGTGGCTGGGCCGCCGC CTGGCGAGCCATGGCTTTGTGGTGATTGTGATTAACACCAAC AGCCGCCTGGATTTTCCGGATAGCCGCGCGAGCCAGCTGAG CGCGGCGCTGAACTATCTGCGCACCAGCAGCCCGAGCGCGG TGCGCGCGCGCCTGGATGCGAACCGCCTGGCGGTGGCGGG CCATAGCATGGGCGGCGGCGCGACCCTGCGCATTAGCGAAC AGATTCCGACCCTGAAAGCGGGCGTGCCGCTGACCCCGTGG CATACCGATAAAACCTTTAACACCCCGGTGCCGCAGCTGATT GTGGGCGCGGAAGCGGATACCGTGGCGCCGGTGAGCCAGC ATGCGATTCCGTTTTATCAGAACCTGCCGAGCACCACCCCGA AAGTGTATGTGGAACTGGATAACGCGACCCATTTTGCGCCGA ACAGCCCGAACGCGGCGATTAGCGTGTATACCATTAGCTGG ATGAAACTGTGGGTGGATAACGATACCCGCTATCGCCAGTTT CTGTGCAACGTGAACGATCCGGCGCTGAGCGATTTTCGCAG CAACAACCGCCATTGCCAG 37 Lipase Thermomyc ATGCGCCCGGTGCGCCGCGCGGTGCCGCAGGATCTGCTGG es ATCAGTTTGAACTGTTTAGCCAGTATAGCGCGGCGGCGTATT lanuginosus GCGCGGCGAACAACCATGCGCCGGTGGGCAGCGATGTGAC CTGCAGCGAAAACGTGTGCCCGGAAGTGGATGCGGCGGATG CGACCTTTCTGTATAGCTTTGAAGATAGCGGCCTGGGCGATG TGACCGGCCTGCTGGCGCTGGATAACACCAACAAACTGATTG TGCTGAGCTTTCGCGGCAGCCGCAGCGTGGAAAACTGGATT GCGAACCTGGCGGCGGATCTGACCGAAATTAGCGATATTTG CAGCGGCTGCGAAGGCCATGTGGGCTTTGTGACCAGCTGGC GCAGCGTGGCGGATACCATTCGCGAACAGGTGCAGAACGCG GTGAACGAACATCCGGATTATCGCGTGGTGTTTACCGGCCAT AGCCTGGGCGGCGCGCTGGCGACCATTGCGGCGGCGGCGC TGCGCGGCAACGGCTATAACATTGATGTGTTTAGCTATGGCG CGCCGCGCGTGGGCAACCGCGCGTTTGCGGAATTTCTGACC GCGCAGACCGGCGGCACCCTGTATCGCATTACCCATACCAA CGATATTGTGCCGCGCCTGCCGCCGCGCGATTGGGGCTATA GCCATAGCAGCCCGGAATATTGGGTGACCAGCGGCAACGAT GTGCCGGTGACCGCGAACGATATTACCGTGGTGGAAGGCAT TGATAGCACCGATGGCAACAACCAGGGCAACATTCCGGATAT TCCGAGCCATCTGTGGTATTTTGGCCCGATTAGCGAATGCGA T 38 Lipase Streptomyc ATGCATCAGCATCCGCATACCCAGCGCCGCACCCGCAGCCT es GAGCAGCGCGCTGGCGGCGGTGGCGGTGCTGGTGGGCATT thermolilaci GGCCTGGGCCCGACCCCGGGCGCGCATGCGGCGGATAACC nus CGTATGAACGCGGCCCGGCGCCGACCAACGCGAGCATTGAA GCGGTGCGCGGCCCGTATGCGGTGAGCCAGGCGACCGTGA GCAGCCTGGCGGTGACCGGCTTTGGCGGCGGCACCATTTAT TATCCGACCACCACCAGCGATGGCACCTTTGGCGCGGTGGC GATTAGCCCGGGCTATACCGGCACCCAGAGCAGCATTGCGT GGCTGGGCCCGCGCCTGGCGAGCCAGGGCTTTGTGGTGTTT ACCATTGATACCAACACCACCCTGGATCAGCCGGATAGCCGC GGCCGCCAGCTGCTGGCGGCGCTGGATTATCTGACCCGCGT GAGCCCGCTGCGCACCCGCGTGGATAGCACCCGCCTGGGC SEQ Classifi Name or Sequence ID cation originating NO: species GTGATGGGCCATAGCATGGGCGGCGGCGGCAGCCTGGAAG CGGCGAAAAGCCGCCCGAGCCTGCAGGCGGCGATTCCGCTG ACCCCGTGGAACCTGGATAAAACCTGGCCGGAAATTCAGAC CCCGACCCTGATTGTGGGCGCGGATGGCGATAGCATTGCGC CGGTGAGCAGCCATGCGGAACCGTTTTATGAAAACCTGCCG AGCAGCCTGGATCGCGCGTATCTGGAACTGAACGGCGCGAG CCATTTTGCGCCGAACAGCAGCAACACCACCATTGCGAAATA TAGCATTAGCTGGCTGAAACGCTTTATTGATAACGATACCCG CTATGAACAGTTTCTGTGCCCGCTGCCGCGCCCGAGCCTGAC CATTGAAGAATATCGCGGCAACTGCCCGCATCAGAGC 39 Esterase Thermobifid ATGGCGAACCCGTATGAACGCGGCCCGAACCCGACCAACAG / a CAGCATTGAAGCGCTGCGCGGCCCGTTTCGCGTGGATGAAG Cutinase halotolerans AACGCGTGAGCCGCCTGCAGGCGCGCGGCTTTGGCGGCGG CACCATTTATTATCCGACCGATAACAACACCTTTGGCGCGGT GGCGATTAGCCCGGGCTATACCGGCACCCAGAGCAGCATTA GCTGGCTGGGCGAACGCCTGGCGAGCCATGGCTTTGTGGTG ATGACCATTGATACCAACACCACCCTGGATCAGCCGGATAGC CGCGCGAGCCAGCTGGATGCGGCGCTGGATTATATGGTGGA AGATAGCAGCTATAGCGTGCGCAACCGCATTGATAGCAGCC GCCTGGCGGCGATGGGCCATAGCATGGGCGGCGGCGGCAC CCTGCGCCTGGCGGAACGCCGCCCGGATCTGCAGGCGGCG ATTCCGCTGACCCCGTGGCATACCGATAAAACCTGGGGCAG CGTGCGCGTGCCGACCCTGATTATTGGCGCGGAAAACGATA CCATTGCGAGCGTGCGCAGCCATAGCGAACCGTTTTATAACA GCCTGCCGGGCAGCCTGGATAAAGCGTATCTGGAACTGGAT GGCGCGAGCCATTTTGCGCCGAACCTGAGCAACACCACCAT TGCGAAATATAGCATTAGCTGGCTGAAACGCTTTGTGGATGA TGATACCCGCTATACCCAGTTTCTGTGCCCGGGCCCGAGCAC CGGCTGGGGCAGCGATGTGGAAGAATATCGCAGCACCTGCC CGTTT 40 PETase Ideonella ATGACCAACCCGTATGCGCGCGGCCCGAACCCGACCGCGGC sakaiensis GAGCCTGGAAGCGAGCGCGGGCCCGTTTACCGTGCGCAGCT TTACCGTGAGCCGCCCGAGCGGCTATGGCGCGGGCACCGTG TATTATCCGACCAACGCGGGCGGCACCGTGGGCGCGATTGC GATTGTGCCGGGCTATACCGCGCGCCAGAGCAGCATTAAAT GGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATT ACCATTGATACCAACAGCACCCTGGATCAGCCGGAAAGCCG CAGCAGCCAGCAGATGGCGGCGCTGCGCCAGGTGGCGAGC CTGAACGGCACCAGCAGCAGCCCGATTTATGGCAAAGTGGA TACCGCGCGCATGGGCGTGATGGGCTGGAGCATGGGCGGC GGCGGCAGCCTGATTAGCGCGGCGAACAACCCGAGCCTGAA AGCGGCGGCGCCGCAGGCGCCGTGGCATAGCAGCACCAAC TTTAGCAGCGTGACCGTGCCGACCCTGATTTTTGCGTGCGAA AACGATAGCATTGCGCCGGTGAACAGCAGCGCGCTGCCGAT TTATGATAGCATGAGCCGCAACGCGAAACAGTTTCTGGAAAT TAACGGCGGCAGCCATAGCTGCGCGAACAGCGGCAACAGCA ACCAGGCGCTGATTGGCAAAAAAGGCGTGGCGTGGATGAAA CGCTTTATGGATAACGATACCCGCTATAGCACCTTTGCGTGC GAAAACCCGAACAGCACCGCGGTGAGCGATTTTCGCACCGC GAACTGCAGC 41 PETase Polyangium ATGCAGACCAACCCGTATCAGCGCGGCCCGGATCCGACCAC brachysporu CCGCGATCTGGAAGATAGCCGCGGCCCGTTTCGCTATGCGA m GCACCAACGTGCGCAGCCCGAGCGGCTATGGCGCGGGCAC SEQ Classifi Name or Sequence ID cation originating NO: species CATTTATTATCCGACCGATGTGAGCGGCAGCGTGGGCGCGG TGGCGGTGGTGCCGGGCTATCTGGCGCGCCAGAGCAGCATT CGCTGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGT GATTACCCTGGATACCCGCAGCACCAGCGATCAGCCGGCGA GCCGCAGCGCGCAGCAGATGGCGGCGCTGCGCCAGGTGGT GGCGCTGAGCGAAACCCGCAGCAGCCCGATTTATGGCAAAG TGGATCCGAACCGCCTGGCGGTGATGGGCTGGAGCATGGGC GGCGGCGGCACCCTGATTAGCGCGCGCGATAACCCGAGCCT GAAAGCGGCGGTGCCGTTTGCGCCGTGGCATAACACCGCGA ACTTTAGCGGCGTGCAGGTGCCGACCCTGGTGATTGCGTGC GAAAACGATACCGTGGCGCCGATTAGCCGCCATGCGAGCAG CTTTTATAACAGCTTTAGCAGCAGCCTGGCGAAAGCGTATCT GGAAATTAACAACGGCAGCCATACCTGCGCGAACACCGGCA ACAGCAACCAGGCGCTGATTGGCAAATATGGCGTGGCGTGG ATTAAACGCTTTGTGGATAACGATACCCGCTATAGCCCGTTT CTGTGCGGCGCGCCGCATCAGGCGGATCTGCGCAGCAGCC GCCTGAGCGAATATCGCGAAAGCTGCCCGTAT 42 PETase Uncultured ATGAACCCGCCGGGCGGCGATCCGGATCCGGGCTGCCAGAC bacteria CGATTGCAACTATCAGCGCGGCCCGGATCCGACCGATGCGT ATCTGGAAGCGGCGAGCGGCCCGTATACCGTGAGCACCATT CGCGTGAGCAGCCTGGTGCCGGGCTTTGGCGGCGGCACCAT TCATTATCCGACCAACGCGGGCGGCGGCAAAATGGCGGGCA TTGTGGTGATTCCGGGCTATCTGAGCTTTGAAAGCAGCATTG AATGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTG ATGACCATTGATACCAACACCATTTATGATCAGCCGAGCCAG CGCCGCGATCAGATTGAAGCGGCGCTGCAGTATCTGGTGAA CCAGAGCAACAGCAGCAGCAGCCCGATTAGCGGCATGGTGG ATAGCAGCCGCCTGGCGGCGGTGGGCTGGAGCATGGGCGG CGGCGGCACCCTGCAGCTGGCGGCGGATGGCGGCATTAAA GCGGCGATTGCGCTGGCGCCGTGGAACAGCAGCATTAACGA TTTTAACCGCATTCAGGTGCCGACCCTGATTTTTGCGTGCCA GCTGGATGCGATTGCGCCGGTGGCGCTGCATGCGAGCCCGT TTTATAACCGCATTCCGAACACCACCCCGAAAGCGTTTTTTGA AATGACCGGCGGCGATCATTGGTGCGCGAACGGCGGCAACA TTTATAGCGCGCTGCTGGGCAAATATGGCGTGAGCTGGATG AAACTGCATCTGGATCAGGATACCCGCTATGCGCCGTTTCTG TGCGGCCCGAACCATGCGGCGCAGACCCTGATTAGCGAATA TCGCGGCAACTGCCCGTAT Exemplary nucleic acid sequences encoding the polymer binding domains disclosed in Table B include those shown in Table F. Table F - Exemplary nucleotide sequences encoding the polymer binding domains SEQ Sequence ID NO 97 GCACAGGCAGCTCCTGGTTGTCGTGTCGATTATGCAGTGACCAACCAGTGGCCGGGCGGT TTTGGTGCGAATGTTACTATTACTAACCTGGGCGATCCGGTTTCCAGCTGGAAACTGGATTG GACCTATACCGCTGGTCAGCGTATCCAGCAACTGTGGAACGGTACCGCTTCTACCAACGGC GGTCAGGTTTCTGTGACTTCTCTGCCGTGGAACGGCTCCATCCCAACCGGCGGTACCGCCA GCTTCGGTTTTAACGGCTCTTGGGCGGGCAGCAACCCGACCCCTGCTTCTTTTTCCCTGAAC GGTACTACCTGTACCGGTACCGTACCGACTACCTCCCCGACTCCGACCCCTACCCCGACCA CGCCGACCCCTACCCCGACCCCGACTCCAACCCCTACGCCAACTGTCACTCCGCAACCGAC CTCTGGTTTCTACGTTGATCCGACGACCCAGGGTTACCGC 98 GGCGGTGGCGGTAGCGGTGGCGGTGGCTCCTACGAGATGCCGTCCGAAGAGGGCTACCA GGACTATGAGCCGGAAGCG 99 GGCGGTGGCGGTTCTGGCGGTGGCGGTTCTTACTCCCGCTGCCAGCTGCAGGGTTTTAAC TGTGTAGTTCGCTCCTATGGCCTCCCGACTATTCCGTGTTGCCGCGGTCTGACCTGTCGCTC CTACTTCCCTGGTTCTACGTACGGCCGTTGTCAACGCTAC 100 GGTGGCGGTGGCTCTGGTGGCGGTGGCTCTGGTGGCGGTGGCTCCGGCGGTGGCGGTTC CTACGAAATGCCGAGCGAGGAAGGTTATCAGGATTACGAACCGGAAGCT 101 GGCTCTGCCGGTAGCGCCGCGGGCTCCGGCTATGAAATGCCGTCTGAGGAAGGTTACCAG GACTATGAACCGGAAGCC 102 GCGGCTGCAGCGGCTGCAGCGGCTGCGGCAGCTACCTTTTCTGTAACGTCCAACTGGGGT AGCGGCTACAACTTCTCCATCGTTATCAAAAACTCCGGCACCACGCCGATCAAAAACTGGAA ACTGGAGTTCGACTACAACGGCAACCTGACCCAGGTATGGGATAGCAAAATCTCTTCCAAA ATCAATAACCACTACGTTATCACCAACGCTGGTTGGAACGGCGAAATTCCGCCTGGCGGCA GC 103 CCACCGGGTGGCAACCGCGGTACTACCACGACTCGTCGCCCGGCTACTACCACTGGCTCTA GCCCGGGTCCTATGCAGTACTCCGCGATCGTTGCCCTGTTCGCCACCCTGGCTGTGGCGGC TCCGGCACAGGAGGCCGCGGCAGATATTGCGATCCTGGATGGTCCATGTACGGCGGGTGT GACTAATAACATCCCGATGTGCTGTGGCTCCGGCATTCTGGATCTCCTGTACCTGGACTGT GAAACCCCAACTCAGGCGACCTCTGTTCTGAACCCACTGTCCGCGGTATGCGGCCGTGTGG GTCTGCAAGCTAAATGTTGCACGCTCGGTATCGCGGATCTGGGTGTACTGTGCCAGGATGC TCTGCCGGAG 104 CCGCCTGGCGGTAACCGTGGCACCACTACCACTCGCCGTCCGGCCACCACTACCGGTTCTT CCCCGGGCCCAATGAAATTCTTTGCTGTAGCGGCACTGTTCGTGGCGTCCGCAATGGCCTC TCCGATGGGCTCTGAAGGTTGCCCAGGCGGTCTGACCAACACTGTTCCGCTGTGTTGCGCG ACGAACGTGCTGGGTGTAGCTACGCTGGATTGCTCTACCCCGACCGTGCCAGTACCGAACG TTGGCATCTTCCAGGCACATTGCGCTAGCAAAGGCAAACAGCCGGTGTGTTGCACTGTTCC AGTGGCCGGCCTGGGCCTCCTGTGTCAGAAACCTACCGGCGCCCAG 105 GGCGGTGGCGGTTCCGGCGGTGGCGGTTCTGGCGGTGGCGGTAGCGGTCTGTGGTCTAC CATCAAACAGAAAGGCAAGGAAGCGGCAATCGCCGCTGCGAAAGCAGCTGGTCAGGCCGC TCTGGGTGCTCTG 106 GCTGAAGCAGCTAAAGAAGCAGCTAAAGAAGCTGCGAAAGCCTATAGCCGTTGTCAGCTGC AGGGTTTTAACTGCGTGGTACGTTCTTATGGTCTGCCTACTATTCCGTGTTGCCGTGGTCTG ACGTGTCGTTCTTATTTCCCTGGTAGCACCTATGGCCGTTGCCAGCGTTAC 107 CCTCCGGGTGGCAACCGTGGTACTACCACTACCCGCCGTCCGGCGACCACTACCGGTTCTT CCCCGGGCCCGACTCAGAGCGCGTTTACTTGTACGGCGACCACTGCATCTAACTACGCCCA CGTGCAGGCAGGCCGTGCGCACGACTCCGGCGGTATCGCATACGCAAACGGCAGCAACCA GAGCATGGGTCTGGACAACCTGTTCTACACGTCCACCCTGGCTCAGACCGCGGCAGGCTAC TATATCGTTGGTAACTGCCCG 108 CCACCGGGTGGCAACCGTGGCACCACGACCACTCGCCGTCCGGCTACTACCACTGGTTCTT CCCCTGGTCCTACCCAATCTCACTATGGTCAGTGTGGTGGCATTGGCTACTCCGGCCCAAC CGTTTGTGCGTCTGGTACCACTTGTCAGGTCCTCAACCCGTACTATTCCCAGTGCCTG 122 TACGAGATGCCGTCCGAAGAGGGCTACCAGGACTATGAGCCGGAAGCG 123 TACTCCCGCTGCCAGCTGCAGGGTTTTAACTGTGTAGTTCGCTCCTATGGCCTCCCGACTAT TCCGTGTTGCCGCGGTCTGACCTGTCGCTCCTACTTCCCTGGTTCTACGTACGGCCGTTGTC AACGCTAC SEQ Sequence ID NO 124 GCGGGCTCCGGCTATGAAATGCCGTCTGAGGAAGGTTACCAGGACTATGAACCGGAAGCC 125 ACCTTTTCTGTAACGTCCAACTGGGGTAGCGGCTACAACTTCTCCATCGTTATCAAAAACTC CGGCACCACGCCGATCAAAAACTGGAAACTGGAGTTCGACTACAACGGCAACCTGACCCAG GTATGGGATAGCAAAATCTCTTCCAAAATCAATAACCACTACGTTATCACCAACGCTGGTTG GAACGGCGAAATTCCGCCTGGCGGCAGC 126 ATGCAGTACTCCGCGATCGTTGCCCTGTTCGCCACCCTGGCTGTGGCGGCTCCGGCACAG GAGGCCGCGGCAGATATTGCGATCCTGGATGGTCCATGTACGGCGGGTGTGACTAATAAC ATCCCGATGTGCTGTGGCTCCGGCATTCTGGATCTCCTGTACCTGGACTGTGAAACCCCAA CTCAGGCGACCTCTGTTCTGAACCCACTGTCCGCGGTATGCGGCCGTGTGGGTCTGCAAGC TAAATGTTGCACGCTCGGTATCGCGGATCTGGGTGTACTGTGCCAGGATGCTCTGCCGGAG 127 ATGAAATTCTTTGCTGTAGCGGCACTGTTCGTGGCGTCCGCAATGGCCTCTCCGATGGGCT CTGAAGGTTGCCCAGGCGGTCTGACCAACACTGTTCCGCTGTGTTGCGCGACGAACGTGCT GGGTGTAGCTACGCTGGATTGCTCTACCCCGACCGTGCCAGTACCGAACGTTGGCATCTTC CAGGCACATTGCGCTAGCAAAGGCAAACAGCCGGTGTGTTGCACTGTTCCAGTGGCCGGC CTGGGCCTCCTGTGTCAGAAACCTACCGGCGCCCAG 128 GGTCTGTGGTCTACCATCAAACAGAAAGGCAAGGAAGCGGCAATCGCCGCTGCGAAAGCA GCTGGTCAGGCCGCTCTGGGTGCTCTG 129 TATAGCCGTTGTCAGCTGCAGGGTTTTAACTGCGTGGTACGTTCTTATGGTCTGCCTACTAT TCCGTGTTGCCGTGGTCTGACGTGTCGTTCTTATTTCCCTGGTAGCACCTATGGCCGTTGCC AGCGTTAC 130 GCGTTTACTTGTACGGCGACCACTGCATCTAACTACGCCCACGTGCAGGCAGGCCGTGCGC ACGACTCCGGCGGTATCGCATACGCAAACGGCAGCAACCAGAGCATGGGTCTGGACAACC TGTTCTACACGTCCACCCTGGCTCAGACCGCGGCAGGCTACTATATCGTTGGTAACTGCCC G 131 CACTATGGTCAGTGTGGTGGCATTGGCTACTCCGGCCCAACCGTTTGTGCGTCTGGTACCA CTTGTCAGGTCCTCAACCCGTACTATTCCCAGTGCCTG Exemplary nucleic acid sequences encoding the polypeptide linkers disclosed in Table C include those shown in Table G Table G - Exemplary nucleic acid sequences encoding the polypeptide linkers SEQ Type Sequence ID NO 71 Flexible GGTGGCGGTGGCTCCGGCGGTGGCGGTTCTGGTGGCGGTGGCTCC 72 Flexible GGTGGCGGTGGCTCTGGTGGCGGTGGCTCCGGTGGCGGTGGCTCT 73 Flexible GCTGGTGCTGGTGCTGGCGCTGGTGCTGGCGCAGGCGCGGGTGCT 74 Flexible GCTGGCGCTGGCGCGGGT 75 Flexible GGCGGTGGCGGCTCC 76 Flexible GGTGCGGGTGCCGGCGCCGGTGCGGGCGCGGGTGCGGGCGCT 77 Rigid GCGGAGGCTGCAGCTAAAGAAGCTGCCGCGAAAGCA 78 Rigid CCGGCCCCAGCTCCT 79 Rigid GCGCCGGCTCCGGCACCGGCACCGGCGCCGGCGCCGGCGCCGGCTCCTGC ACCGGCCCCG 80 Rigid GAAGCAGCTGCGAAAGAAGCGGCTAAAGAAGCTGCTAAA 81 Rigid GCGGAAGCGGCCGCGAAAGAAGCTGCAGCTAAAGAAGCTGCAGCCAAGGA GGCGGCCGCTAAA GCGCTGGAAGCGGAAGCCGCGGCAAAAGAAGCAGCGGCTAAGGAAGCGGC CGCGAAAGAAGCT GCGGCAAAGGCG 82 Rigid GAGGCGGCTGCTAAG SEQ Type Sequence ID NO 83 Rigid GTTTTCAACCAGCGTAAAGAACATAAAGGTTACATGCTGGCG 84 Rigid CCAGCTGTGCCTCCGCCGGCT Exemplary nucleic acid sequences encoding the fusion proteins disclosed in Table D(i) and(ii) include those shown in Table H(i) and H(ii). Table H(i) - Exemplary nucleic acid sequences encoding the fusion proteins SEQ Sequence ID NO 43 ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGGCGCGG GCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGAACCCGTATCAGCGCGGCCCGGA TCCGACCGAAAGCCTGCTGCGCGCGGCGCGCGGCCCGTTTGCGGTGAGCGAACAGAGCGT GAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCCGCATTTATTATCCGACCACCACCAGC CAGGGCACCTTTGGCGCGATTGCGATTAGCCCGGGCTTTACCGCGAGCTGGAGCAGCCTG GCGTGGCTGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATTGGCATTGAAACCAACA CCCGCCTGGATCAGCCGGATAGCCGCGGCCGCCAGCTGCTGGCGGCGCTGGATTATCTGA CCCAGCGCAGCAGCGTGCGCAACCGCGTGGATGCGAGCCGCCTGGCGGTGGCGGGCCATA GCATGGGCGGCGGCGGCACCCTGGAAGCGGCGAAAAGCCGCACCAGCCTGAAAGCGGCG ATTCCGATTGCGCCGTGGAACCTGGATAAAACCTGGCCGGAAGTGCGCACCCCGACCCTGA TTATTGGCGGCGAACTGGATAGCATTGCGCCGGTGGCGACCCATAGCATTCCGTTTTATAAC AGCCTGACCAACGCGCGCGAAAAAGCGTATCTGGAACTGAACAACGCGAGCCATTTTTTTCC GCAGTTTAGCAACGATACCATGGCGAAATTTATGATTAGCTGGATGAAACGCTTTATTGATG ATGATACCCGCTATGATCAGTTTCTGTGCCCGCCGCCGCGCGCGATTGGCGATATTAGCGAT TATCGCGATACCTGCCCG 44 ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGTGTTTAA CCAGCGCAAAGAACATAAAGGCTATATGCTGGCGAGCAACCCGTATCAGCGCGGCCCGAAC CCGACCCGCAGCGCGCTGACCGCGGATGGCCCGTTTAGCGTGGCGACCTATACCGTGAGC CGCCTGAGCGTGAGCGGCTTTGGCGGCGGCGTGATTTATTATCCGACCGGCACCAGCCTGA CCTTTGGCGGCATTGCGATGAGCCCGGGCTATACCGCGGATGCGAGCAGCCTGGCGTGGC TGGGCCGCCGCCTGGCGAGCCATGGCTTTGTGGTGCTGGTGATTAACACCAACAGCCGCTT TGATGGCCCGGATAGCCGCGCGAGCCAGCTGAGCGCGGCGCTGAACTATCTGCGCACCAG CAGCCCGAGCGCGGTGCGCGCGCGCCTGGATGCGAACCGCCTGGCGGTGGCGGGCCATA GCATGGGCGGCGGCGGCACCCTGCGCATTGCGGAACAGAACCCGAGCCTGAAAGCGGCG GTGCCGCTGACCCCGTGGCATACCGATAAAACCTTTAACACCAGCGTGCCGGTGCTGATTG TGGGCGCGGAAGCGGATACCGTGGCGCCGGTGAGCCAGCATGCGATTCCGTTTTATCAGAA CCTGCCGAGCACCACCCCGAAAGTGTATGTGGAACTGTGCAACGCGAGCCATTGGGCGCCG AACAGCAACAACGCGGCGATTAGCGTGTATACCATTAGCTGGATGAAACTGTGGGTGGATA ACGATACCCGCTATCGCCAGTTTCTGTGCAACGTGAACGATCCGGCGCTGTGCGATTTTCGC ACCAACAACCGCCATTGCCAG ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGCGGGCG CGGGCGCGGGCACCAACCCGTATGCGCGCGGCCCGAACCCGACCGCGGCGAGCCTGGAA GCGAGCGCGGGCCCGTTTACCGTGCGCAGCTTTACCGTGAGCCGCCCGAGCGGCTATGGC GCGGGCACCGTGTATTATCCGACCAACGCGGGCGGCACCGTGGGCGCGATTGCGATTGTG CCGGGCTATACCGCGCGCCAGAGCAGCATTAAATGGTGGGGCCCGCGCCTGGCGAGCCAT GGCTTTGTGGTGATTACCATTGATACCAACAGCACCCTGGATCAGCCGGAAAGCCGCAGCA GCCAGCAGATGGCGGCGCTGCGCCAGGTGGCGAGCCTGAACGGCACCAGCAGCAGCCCG ATTTATGGCAAAGTGGATACCGCGCGCATGGGCGTGATGGGCTGGAGCATGGGCGGCGGC GGCAGCCTGATTAGCGCGGCGAACAACCCGAGCCTGAAAGCGGCGGCGCCGCAGGCGCC GTGGCATAGCAGCACCAACTTTAGCAGCGTGACCGTGCCGACCCTGATTTTTGCGTGCGAA AACGATAGCATTGCGCCGGTGAACAGCAGCGCGCTGCCGATTTATGATAGCATGAGCCGCA ACGCGAAACAGTTTCTGGAAATTAACGGCGGCAGCCATAGCTGCGCGAACAGCGGCAACAG CAACCAGGCGCTGATTGGCAAAAAAGGCGTGGCGTGGATGAAACGCTTTATGGATAACGAT ACCCGCTATAGCACCTTTGCGTGCGAAAACCCGAACAGCACCGCGGTGAGCGATTTTCGCA CCGCGAACTGCAGC ATGAGCAACCCGTATCAGCGCGGCCCGAACCCGACCCGCAGCGCGCTGACCGCGGATGGC CCGTTTAGCGTGGCGACCTATACCGTGAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGC GTGATTTATTATCCGACCGGCACCAGCCTGACCTTTGGCGGCATTGCGATGAGCCCGGGCT ATACCGCGGATGCGAGCAGCCTGGCGTGGCTGGGCCGCCGCCTGGCGAGCCATGGCTTTG TGGTGCTGGTGATTAACACCAACAGCCGCTTTGATGGCCCGGATAGCCGCGCGAGCCAGCT GAGCGCGGCGCTGAACTATCTGCGCACCAGCAGCCCGAGCGCGGTGCGCGCGCGCCTGGA TGCGAACCGCCTGGCGGTGGCGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCATTGC GGAACAGAACCCGAGCCTGAAAGCGGCGGTGCCGCTGACCCCGTGGCATACCGATAAAAC CTTTAACACCAGCGTGCCGGTGCTGATTGTGGGCGCGGAAGCGGATACCGTGGCGCCGGT GAGCCAGCATGCGATTCCGTTTTATCAGAACCTGCCGAGCACCACCCCGAAAGTGTATGTG GAACTGTGCAACGCGAGCCATTGGGCGCCGAACAGCAACAACGCGGCGATTAGCGTGTATA CCATTAGCTGGATGAAACTGTGGGTGGATAACGATACCCGCTATCGCCAGTTTCTGTGCAAC GTGAACGATCCGGCGCTGTGCGATTTTCGCACCAACAACCGCCATTGCCAGGAAGCGGCGG CGAAAGAAGCGGCGAAAGAAGCGGCGAAAAACCCGCCGGGCGGCGATCCGGATCCGGGC TGCCAGACCGATTGCAACTATCAGCGCGGCCCGGATCCGACCGATGCGTATCTGGAAGCGG CGAGCGGCCCGTATACCGTGAGCACCATTCGCGTGAGCAGCCTGGTGCCGGGCTTTGGCG GCGGCACCATTCATTATCCGACCAACGCGGGCGGCGGCAAAATGGCGGGCATTGTGGTGAT TCCGGGCTATCTGAGCTTTGAAAGCAGCATTGAATGGTGGGGCCCGCGCCTGGCGAGCCAT GGCTTTGTGGTGATGACCATTGATACCAACACCATTTATGATCAGCCGAGCCAGCGCCGCG ATCAGATTGAAGCGGCGCTGCAGTATCTGGTGAACCAGAGCAACAGCAGCAGCAGCCCGAT TAGCGGCATGGTGGATAGCAGCCGCCTGGCGGCGGTGGGCTGGAGCATGGGCGGCGGCG GCACCCTGCAGCTGGCGGCGGATGGCGGCATTAAAGCGGCGATTGCGCTGGCGCCGTGGA ACAGCAGCATTAACGATTTTAACCGCATTCAGGTGCCGACCCTGATTTTTGCGTGCCAGCTG GATGCGATTGCGCCGGTGGCGCTGCATGCGAGCCCGTTTTATAACCGCATTCCGAACACCA CCCCGAAAGCGTTTTTTGAAATGACCGGCGGCGATCATTGGTGCGCGAACGGCGGCAACAT TTATAGCGCGCTGCTGGGCAAATATGGCGTGAGCTGGATGAAACTGCATCTGGATCAGGAT ACCCGCTATGCGCCGTTTCTGTGCGGCCCGAACCATGCGGCGCAGACCCTGATTAGCGAAT ATCGCGGCAACTGCCCGTAT ATGACCAACCCGTATGCGCGCGGCCCGAACCCGACCGCGGCGAGCCTGGAAGCGAGCGCG GGCCCGTTTACCGTGCGCAGCTTTACCGTGAGCCGCCCGAGCGGCTATGGCGCGGGCACC GTGTATTATCCGACCAACGCGGGCGGCACCGTGGGCGCGATTGCGATTGTGCCGGGCTATA CCGCGCGCCAGAGCAGCATTAAATGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCAACAGCACCCTGGATCAGCCGGAAAGCCGCAGCAGCCAGCAGAT GGCGGCGCTGCGCCAGGTGGCGAGCCTGAACGGCACCAGCAGCAGCCCGATTTATGGCAA AGTGGATACCGCGCGCATGGGCGTGATGGGCTGGAGCATGGGCGGCGGCGGCAGCCTGA TTAGCGCGGCGAACAACCCGAGCCTGAAAGCGGCGGCGCCGCAGGCGCCGTGGCATAGCA GCACCAACTTTAGCAGCGTGACCGTGCCGACCCTGATTTTTGCGTGCGAAAACGATAGCATT GCGCCGGTGAACAGCAGCGCGCTGCCGATTTATGATAGCATGAGCCGCAACGCGAAACAGT TTCTGGAAATTAACGGCGGCAGCCATAGCTGCGCGAACAGCGGCAACAGCAACCAGGCGCT GATTGGCAAAAAAGGCGTGGCGTGGATGAAACGCTTTATGGATAACGATACCCGCTATAGC ACCTTTGCGTGCGAAAACCCGAACAGCACCGCGGTGAGCGATTTTCGCACCGCGAACTGCA GCGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGAACCCGTATGAACG CGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGCCCGTTTAGCGTGAGCGA AGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGCACCATTTATTATCCGCGC GAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATACCGGCACCGAAGCGAGC ATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGGTGATTACCATTGATACCAT TACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAACGCGGCGCTGAACCATATG ATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCAGCCGCCTGGCGGTGATG GGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGCCAGCGCCCGGATCTGAAA GCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGAGCAGCGTGACCGTGCCGA CCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGCGACCCATGCGAAACCGTT TTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAACTGGATGGCGCGACCCAT TTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTGGCGTGGCTGAAACGCTT TGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCCCGCGCGATGGCCTGTTT GGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTT ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGTGTTTAA CCAGCGCAAAGAACATAAAGGCTATATGCTGGCGACCAACCCGTATGCGCGCGGCCCGAAC CCGACCGCGGCGAGCCTGGAAGCGAGCGCGGGCCCGTTTACCGTGCGCAGCTTTACCGTG AGCCGCCCGAGCGGCTATGGCGCGGGCACCGTGTATTATCCGACCAACGCGGGCGGCACC GTGGGCGCGATTGCGATTGTGCCGGGCTATACCGCGCGCCAGAGCAGCATTAAATGGTGG GGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATTACCATTGATACCAACAGCACCCTGG ATCAGCCGGAAAGCCGCAGCAGCCAGCAGATGGCGGCGCTGCGCCAGGTGGCGAGCCTGA ACGGCACCAGCAGCAGCCCGATTTATGGCAAAGTGGATACCGCGCGCATGGGCGTGATGG GCTGGAGCATGGGCGGCGGCGGCAGCCTGATTAGCGCGGCGAACAACCCGAGCCTGAAAG CGGCGGCGCCGCAGGCGCCGTGGCATAGCAGCACCAACTTTAGCAGCGTGACCGTGCCGA CCCTGATTTTTGCGTGCGAAAACGATAGCATTGCGCCGGTGAACAGCAGCGCGCTGCCGAT TTATGATAGCATGAGCCGCAACGCGAAACAGTTTCTGGAAATTAACGGCGGCAGCCATAGC TGCGCGAACAGCGGCAACAGCAACCAGGCGCTGATTGGCAAAAAAGGCGTGGCGTGGATG AAACGCTTTATGGATAACGATACCCGCTATAGCACCTTTGCGTGCGAAAACCCGAACAGCAC CGCGGTGAGCGATTTTCGCACCGCGAACTGCAGC ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGAAGCGGC GGCGAAAGAAGCGGCGAAAGAAGCGGCGAAAGCGAACCCGTATCAGCGCGGCCCGGATCC GACCGAAAGCCTGCTGCGCGCGGCGCGCGGCCCGTTTGCGGTGAGCGAACAGAGCGTGAG CCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCCGCATTTATTATCCGACCACCACCAGCCAG GGCACCTTTGGCGCGATTGCGATTAGCCCGGGCTTTACCGCGAGCTGGAGCAGCCTGGCGT GGCTGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATTGGCATTGAAACCAACACCCG CCTGGATCAGCCGGATAGCCGCGGCCGCCAGCTGCTGGCGGCGCTGGATTATCTGACCCA GCGCAGCAGCGTGCGCAACCGCGTGGATGCGAGCCGCCTGGCGGTGGCGGGCCATAGCAT GGGCGGCGGCGGCACCCTGGAAGCGGCGAAAAGCCGCACCAGCCTGAAAGCGGCGATTC CGATTGCGCCGTGGAACCTGGATAAAACCTGGCCGGAAGTGCGCACCCCGACCCTGATTAT TGGCGGCGAACTGGATAGCATTGCGCCGGTGGCGACCCATAGCATTCCGTTTTATAACAGC CTGACCAACGCGCGCGAAAAAGCGTATCTGGAACTGAACAACGCGAGCCATTTTTTTCCGCA GTTTAGCAACGATACCATGGCGAAATTTATGATTAGCTGGATGAAACGCTTTATTGATGATG ATACCCGCTATGATCAGTTTCTGTGCCCGCCGCCGCGCGCGATTGGCGATATTAGCGATTAT CGCGATACCTGCCCG ATGACCAACCCGTATGCGCGCGGCCCGAACCCGACCGCGGCGAGCCTGGAAGCGAGCGCG GGCCCGTTTACCGTGCGCAGCTTTACCGTGAGCCGCCCGAGCGGCTATGGCGCGGGCACC GTGTATTATCCGACCAACGCGGGCGGCACCGTGGGCGCGATTGCGATTGTGCCGGGCTATA CCGCGCGCCAGAGCAGCATTAAATGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCAACAGCACCCTGGATCAGCCGGAAAGCCGCAGCAGCCAGCAGAT GGCGGCGCTGCGCCAGGTGGCGAGCCTGAACGGCACCAGCAGCAGCCCGATTTATGGCAA AGTGGATACCGCGCGCATGGGCGTGATGGGCTGGAGCATGGGCGGCGGCGGCAGCCTGA TTAGCGCGGCGAACAACCCGAGCCTGAAAGCGGCGGCGCCGCAGGCGCCGTGGCATAGCA GCACCAACTTTAGCAGCGTGACCGTGCCGACCCTGATTTTTGCGTGCGAAAACGATAGCATT GCGCCGGTGAACAGCAGCGCGCTGCCGATTTATGATAGCATGAGCCGCAACGCGAAACAGT TTCTGGAAATTAACGGCGGCAGCCATAGCTGCGCGAACAGCGGCAACAGCAACCAGGCGCT GATTGGCAAAAAAGGCGTGGCGTGGATGAAACGCTTTATGGATAACGATACCCGCTATAGC ACCTTTGCGTGCGAAAACCCGAACAGCACCGCGGTGAGCGATTTTCGCACCGCGAACTGCA GCCCGGCGGTGCCGCCGCCGGCGAACCCGTATGAACGCGGCCCGAACCCGACCAACAGCA GCATTGAAGCGCTGCGCGGCCCGTTTCGCGTGGATGAAGAACGCGTGAGCCGCCTGCAGG CGCGCGGCTTTGGCGGCGGCACCATTTATTATCCGACCGATAACAACACCTTTGGCGCGGT GGCGATTAGCCCGGGCTATACCGGCACCCAGAGCAGCATTAGCTGGCTGGGCGAACGCCT GGCGAGCCATGGCTTTGTGGTGATGACCATTGATACCAACACCACCCTGGATCAGCCGGAT AGCCGCGCGAGCCAGCTGGATGCGGCGCTGGATTATATGGTGGAAGATAGCAGCTATAGC GTGCGCAACCGCATTGATAGCAGCCGCCTGGCGGCGATGGGCCATAGCATGGGCGGCGGC GGCACCCTGCGCCTGGCGGAACGCCGCCCGGATCTGCAGGCGGCGATTCCGCTGACCCCG TGGCATACCGATAAAACCTGGGGCAGCGTGCGCGTGCCGACCCTGATTATTGGCGCGGAAA ACGATACCATTGCGAGCGTGCGCAGCCATAGCGAACCGTTTTATAACAGCCTGCCGGGCAG CCTGGATAAAGCGTATCTGGAACTGGATGGCGCGAGCCATTTTGCGCCGAACCTGAGCAAC ACCACCATTGCGAAATATAGCATTAGCTGGCTGAAACGCTTTGTGGATGATGATACCCGCTA TACCCAGTTTCTGTGCCCGGGCCCGAGCACCGGCTGGGGCAGCGATGTGGAAGAATATCG CAGCACCTGCCCGTTT ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGGCGCGG GCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGAGCAACCCGTATCAGCGCGGCCC GAACCCGACCCGCAGCGCGCTGACCGCGGATGGCCCGTTTAGCGTGGCGACCTATACCGT GAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCGTGATTTATTATCCGACCGGCACCAG CCTGACCTTTGGCGGCATTGCGATGAGCCCGGGCTATACCGCGGATGCGAGCAGCCTGGC GTGGCTGGGCCGCCGCCTGGCGAGCCATGGCTTTGTGGTGCTGGTGATTAACACCAACAGC CGCTTTGATGGCCCGGATAGCCGCGCGAGCCAGCTGAGCGCGGCGCTGAACTATCTGCGC ACCAGCAGCCCGAGCGCGGTGCGCGCGCGCCTGGATGCGAACCGCCTGGCGGTGGCGGG CCATAGCATGGGCGGCGGCGGCACCCTGCGCATTGCGGAACAGAACCCGAGCCTGAAAGC GGCGGTGCCGCTGACCCCGTGGCATACCGATAAAACCTTTAACACCAGCGTGCCGGTGCTG ATTGTGGGCGCGGAAGCGGATACCGTGGCGCCGGTGAGCCAGCATGCGATTCCGTTTTATC AGAACCTGCCGAGCACCACCCCGAAAGTGTATGTGGAACTGTGCAACGCGAGCCATTGGGC GCCGAACAGCAACAACGCGGCGATTAGCGTGTATACCATTAGCTGGATGAAACTGTGGGTG GATAACGATACCCGCTATCGCCAGTTTCTGTGCAACGTGAACGATCCGGCGCTGTGCGATTT TCGCACCAACAACCGCCATTGCCAG ATGCGCCCGGTGCGCCGCGCGGTGCCGCAGGATCTGCTGGATCAGTTTGAACTGTTTAGCC AGTATAGCGCGGCGGCGTATTGCGCGGCGAACAACCATGCGCCGGTGGGCAGCGATGTGA CCTGCAGCGAAAACGTGTGCCCGGAAGTGGATGCGGCGGATGCGACCTTTCTGTATAGCTT TGAAGATAGCGGCCTGGGCGATGTGACCGGCCTGCTGGCGCTGGATAACACCAACAAACTG ATTGTGCTGAGCTTTCGCGGCAGCCGCAGCGTGGAAAACTGGATTGCGAACCTGGCGGCG GATCTGACCGAAATTAGCGATATTTGCAGCGGCTGCGAAGGCCATGTGGGCTTTGTGACCA GCTGGCGCAGCGTGGCGGATACCATTCGCGAACAGGTGCAGAACGCGGTGAACGAACATC CGGATTATCGCGTGGTGTTTACCGGCCATAGCCTGGGCGGCGCGCTGGCGACCATTGCGG CGGCGGCGCTGCGCGGCAACGGCTATAACATTGATGTGTTTAGCTATGGCGCGCCGCGCGT GGGCAACCGCGCGTTTGCGGAATTTCTGACCGCGCAGACCGGCGGCACCCTGTATCGCATT ACCCATACCAACGATATTGTGCCGCGCCTGCCGCCGCGCGATTGGGGCTATAGCCATAGCA GCCCGGAATATTGGGTGACCAGCGGCAACGATGTGCCGGTGACCGCGAACGATATTACCGT GGTGGAAGGCATTGATAGCACCGATGGCAACAACCAGGGCAACATTCCGGATATTCCGAGC CATCTGTGGTATTTTGGCCCGATTAGCGAATGCGATGGCGCGGGCGCGGGCGCGGGCGCG GGCGCGGGCGCGGGCGCGAGCAACCCGTATCAGCGCGGCCCGAACCCGACCCGCAGCGC GCTGACCGCGGATGGCCCGTTTAGCGTGGCGACCTATACCGTGAGCCGCCTGAGCGTGAG CGGCTTTGGCGGCGGCGTGATTTATTATCCGACCGGCACCAGCCTGACCTTTGGCGGCATT GCGATGAGCCCGGGCTATACCGCGGATGCGAGCAGCCTGGCGTGGCTGGGCCGCCGCCTG GCGAGCCATGGCTTTGTGGTGCTGGTGATTAACACCAACAGCCGCTTTGATGGCCCGGATA GCCGCGCGAGCCAGCTGAGCGCGGCGCTGAACTATCTGCGCACCAGCAGCCCGAGCGCGG TGCGCGCGCGCCTGGATGCGAACCGCCTGGCGGTGGCGGGCCATAGCATGGGCGGCGGC GGCACCCTGCGCATTGCGGAACAGAACCCGAGCCTGAAAGCGGCGGTGCCGCTGACCCCG TGGCATACCGATAAAACCTTTAACACCAGCGTGCCGGTGCTGATTGTGGGCGCGGAAGCGG ATACCGTGGCGCCGGTGAGCCAGCATGCGATTCCGTTTTATCAGAACCTGCCGAGCACCAC CCCGAAAGTGTATGTGGAACTGTGCAACGCGAGCCATTGGGCGCCGAACAGCAACAACGC GGCGATTAGCGTGTATACCATTAGCTGGATGAAACTGTGGGTGGATAACGATACCCGCTATC GCCAGTTTCTGTGCAACGTGAACGATCCGGCGCTGTGCGATTTTCGCACCAACAACCGCCAT TGCCAG ATGAACCCGTATGAACGCGGCCCGAACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGC CCGTTTAGCGTGAGCGAAGAAAACGTGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGC ACCATTTATTATCCGCGCGAAAACAACACCTATGGCGCGGTGGCGATTAGCCCGGGCTATA CCGGCACCGAAGCGAGCATTGCGTGGCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCATTACCACCCTGGATCAGCCGGATAGCCGCGCGGAACAGCTGAAC GCGGCGCTGAACCATATGATTAACCGCGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCA GCCGCCTGGCGGTGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGC CAGCGCCCGGATCTGAAAGCGGCGATTCCGCTGACCCCGTGGCATCTGAACAAAAACTGGA GCAGCGTGACCGTGCCGACCCTGATTATTGGCGCGGATCTGGATACCATTGCGCCGGTGGC GACCCATGCGAAACCGTTTTATAACAGCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAAC TGGATGGCGCGACCCATTTTGCGCCGAACATTCCGAACAAAATTATTGGCAAATATAGCGTG GCGTGGCTGAAACGCTTTGTGGATAACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCC CGCGCGATGGCCTGTTTGGCGAAGTGGAAGAATATCGCAGCACCTGCCCGTTTGTGTTTAA CCAGCGCAAAGAACATAAAGGCTATATGCTGGCGGCGAACCCGTATCAGCGCGGCCCGGAT CCGACCGAAAGCCTGCTGCGCGCGGCGCGCGGCCCGTTTGCGGTGAGCGAACAGAGCGTG AGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCCGCATTTATTATCCGACCACCACCAGCC AGGGCACCTTTGGCGCGATTGCGATTAGCCCGGGCTTTACCGCGAGCTGGAGCAGCCTGG CGTGGCTGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATTGGCATTGAAACCAACAC CCGCCTGGATCAGCCGGATAGCCGCGGCCGCCAGCTGCTGGCGGCGCTGGATTATCTGAC CCAGCGCAGCAGCGTGCGCAACCGCGTGGATGCGAGCCGCCTGGCGGTGGCGGGCCATA GCATGGGCGGCGGCGGCACCCTGGAAGCGGCGAAAAGCCGCACCAGCCTGAAAGCGGCG ATTCCGATTGCGCCGTGGAACCTGGATAAAACCTGGCCGGAAGTGCGCACCCCGACCCTGA TTATTGGCGGCGAACTGGATAGCATTGCGCCGGTGGCGACCCATAGCATTCCGTTTTATAAC AGCCTGACCAACGCGCGCGAAAAAGCGTATCTGGAACTGAACAACGCGAGCCATTTTTTTCC GCAGTTTAGCAACGATACCATGGCGAAATTTATGATTAGCTGGATGAAACGCTTTATTGATG ATGATACCCGCTATGATCAGTTTCTGTGCCCGCCGCCGCGCGCGATTGGCGATATTAGCGAT TATCGCGATACCTGCCCG ATGAACCCGCCGGGCGGCGATCCGGATCCGGGCTGCCAGACCGATTGCAACTATCAGCGC GGCCCGGATCCGACCGATGCGTATCTGGAAGCGGCGAGCGGCCCGTATACCGTGAGCACC ATTCGCGTGAGCAGCCTGGTGCCGGGCTTTGGCGGCGGCACCATTCATTATCCGACCAACG CGGGCGGCGGCAAAATGGCGGGCATTGTGGTGATTCCGGGCTATCTGAGCTTTGAAAGCA GCATTGAATGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGGTGATGACCATTGATAC CAACACCATTTATGATCAGCCGAGCCAGCGCCGCGATCAGATTGAAGCGGCGCTGCAGTAT CTGGTGAACCAGAGCAACAGCAGCAGCAGCCCGATTAGCGGCATGGTGGATAGCAGCCGC CTGGCGGCGGTGGGCTGGAGCATGGGCGGCGGCGGCACCCTGCAGCTGGCGGCGGATGG CGGCATTAAAGCGGCGATTGCGCTGGCGCCGTGGAACAGCAGCATTAACGATTTTAACCGC ATTCAGGTGCCGACCCTGATTTTTGCGTGCCAGCTGGATGCGATTGCGCCGGTGGCGCTGC ATGCGAGCCCGTTTTATAACCGCATTCCGAACACCACCCCGAAAGCGTTTTTTGAAATGACC GGCGGCGATCATTGGTGCGCGAACGGCGGCAACATTTATAGCGCGCTGCTGGGCAAATATG GCGTGAGCTGGATGAAACTGCATCTGGATCAGGATACCCGCTATGCGCCGTTTCTGTGCGG CCCGAACCATGCGGCGCAGACCCTGATTAGCGAATATCGCGGCAACTGCCCGTATGGCGCG GGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGAACCCGTATGAACGCGGCCCGA ACCCGACCGATGCGCTGCTGGAAGCGAGCAGCGGCCCGTTTAGCGTGAGCGAAGAAAACG TGAGCCGCCTGAGCGCGAGCGGCTTTGGCGGCGGCACCATTTATTATCCGCGCGAAAACAA CACCTATGGCGCGGTGGCGATTAGCCCGGGCTATACCGGCACCGAAGCGAGCATTGCGTG GCTGGGCGAACGCATTGCGAGCCATGGCTTTGTGGTGATTACCATTGATACCATTACCACCC TGGATCAGCCGGATAGCCGCGCGGAACAGCTGAACGCGGCGCTGAACCATATGATTAACCG CGCGAGCAGCACCGTGCGCAGCCGCATTGATAGCAGCCGCCTGGCGGTGATGGGCCATAG CATGGGCGGCGGCGGCACCCTGCGCCTGGCGAGCCAGCGCCCGGATCTGAAAGCGGCGAT TCCGCTGACCCCGTGGCATCTGAACAAAAACTGGAGCAGCGTGACCGTGCCGACCCTGATT ATTGGCGCGGATCTGGATACCATTGCGCCGGTGGCGACCCATGCGAAACCGTTTTATAACA GCCTGCCGAGCAGCATTAGCAAAGCGTATCTGGAACTGGATGGCGCGACCCATTTTGCGCC GAACATTCCGAACAAAATTATTGGCAAATATAGCGTGGCGTGGCTGAAACGCTTTGTGGATA ACGATACCCGCTATACCCAGTTTCTGTGCCCGGGCCCGCGCGATGGCCTGTTTGGCGAAGT GGAAGAATATCGCAGCACCTGCCCGTTT ATGCAGCTGGGCGCGATTGAAAACGGCCTGGAAAGCGGCAGCGCGAACGCGTGCCCGGAT GCGATTCTGATTTTTGCGCGCGGCAGCACCGAACCGGGCAACATGGGCATTACCGTGGGCC CGGCGCTGGCGAACGGCCTGGAAAGCCATATTCGCAACATTTGGATTCAGGGCGTGGGCG GCCCGTATGATGCGGCGCTGGCGACCAACTTTCTGCCGCGCGGCACCAGCCAGGCGAACA TTGATGAAGGCAAACGCCTGTTTGCGCTGGCGAACCAGAAATGCCCGAACACCCCGGTGGT GGCGGGCGGCTATAGCCAGGGCGCGGCGCTGATTGCGGCGGCGGTGAGCGAACTGAGCG GCGCGGTGAAAGAACAGGTGAAAGGCGTGGCGCTGTTTGGCTATACCCAGAACCTGCAGA ACCGCGGCGGCATTCCGAACTATCCGCGCGAACGCACCAAAGTGTTTTGCAACGTGGGCGA TGCGGTGTGCACCGGCACCCTGATTATTACCCCGGCGCATCTGAGCTATACCATTGAAGCG CGCGGCGAAGCGGCGCGCTTTCTGCGCGATCGCATTCGCGCGGGCGCGGGCGCGGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGAGCAACCCGTATCAGCGCGGCCCGAACCCGACCC GCAGCGCGCTGACCGCGGATGGCCCGTTTAGCGTGGCGACCTATACCGTGAGCCGCCTGA GCGTGAGCGGCTTTGGCGGCGGCGTGATTTATTATCCGACCGGCACCAGCCTGACCTTTGG CGGCATTGCGATGAGCCCGGGCTATACCGCGGATGCGAGCAGCCTGGCGTGGCTGGGCCG CCGCCTGGCGAGCCATGGCTTTGTGGTGCTGGTGATTAACACCAACAGCCGCTTTGATGGC CCGGATAGCCGCGCGAGCCAGCTGAGCGCGGCGCTGAACTATCTGCGCACCAGCAGCCCG AGCGCGGTGCGCGCGCGCCTGGATGCGAACCGCCTGGCGGTGGCGGGCCATAGCATGGG CGGCGGCGGCACCCTGCGCATTGCGGAACAGAACCCGAGCCTGAAAGCGGCGGTGCCGCT GACCCCGTGGCATACCGATAAAACCTTTAACACCAGCGTGCCGGTGCTGATTGTGGGCGCG GAAGCGGATACCGTGGCGCCGGTGAGCCAGCATGCGATTCCGTTTTATCAGAACCTGCCGA GCACCACCCCGAAAGTGTATGTGGAACTGTGCAACGCGAGCCATTGGGCGCCGAACAGCAA CAACGCGGCGATTAGCGTGTATACCATTAGCTGGATGAAACTGTGGGTGGATAACGATACC CGCTATCGCCAGTTTCTGTGCAACGTGAACGATCCGGCGCTGTGCGATTTTCGCACCAACAA CCGCCATTGCCAG ATGGCGAACCCGTATGAACGCGGCCCGAACCCGACCAACAGCAGCATTGAAGCGCTGCGC GGCCCGTTTCGCGTGGATGAAGAACGCGTGAGCCGCCTGCAGGCGCGCGGCTTTGGCGGC GGCACCATTTATTATCCGACCGATAACAACACCTTTGGCGCGGTGGCGATTAGCCCGGGCT ATACCGGCACCCAGAGCAGCATTAGCTGGCTGGGCGAACGCCTGGCGAGCCATGGCTTTGT GGTGATGACCATTGATACCAACACCACCCTGGATCAGCCGGATAGCCGCGCGAGCCAGCTG GATGCGGCGCTGGATTATATGGTGGAAGATAGCAGCTATAGCGTGCGCAACCGCATTGATA GCAGCCGCCTGGCGGCGATGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCCTGGCG GAACGCCGCCCGGATCTGCAGGCGGCGATTCCGCTGACCCCGTGGCATACCGATAAAACCT GGGGCAGCGTGCGCGTGCCGACCCTGATTATTGGCGCGGAAAACGATACCATTGCGAGCG TGCGCAGCCATAGCGAACCGTTTTATAACAGCCTGCCGGGCAGCCTGGATAAAGCGTATCT GGAACTGGATGGCGCGAGCCATTTTGCGCCGAACCTGAGCAACACCACCATTGCGAAATAT AGCATTAGCTGGCTGAAACGCTTTGTGGATGATGATACCCGCTATACCCAGTTTCTGTGCCC GGGCCCGAGCACCGGCTGGGGCAGCGATGTGGAAGAATATCGCAGCACCTGCCCGTTTGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGAGCAACCCGTATCAG CGCGGCCCGAACCCGACCCGCAGCGCGCTGACCGCGGATGGCCCGTTTAGCGTGGCGACC TATACCGTGAGCCGCCTGAGCGTGAGCGGCTTTGGCGGCGGCGTGATTTATTATCCGACCG GCACCAGCCTGACCTTTGGCGGCATTGCGATGAGCCCGGGCTATACCGCGGATGCGAGCA GCCTGGCGTGGCTGGGCCGCCGCCTGGCGAGCCATGGCTTTGTGGTGCTGGTGATTAACA CCAACAGCCGCTTTGATGGCCCGGATAGCCGCGCGAGCCAGCTGAGCGCGGCGCTGAACT ATCTGCGCACCAGCAGCCCGAGCGCGGTGCGCGCGCGCCTGGATGCGAACCGCCTGGCGG TGGCGGGCCATAGCATGGGCGGCGGCGGCACCCTGCGCATTGCGGAACAGAACCCGAGCC TGAAAGCGGCGGTGCCGCTGACCCCGTGGCATACCGATAAAACCTTTAACACCAGCGTGCC GGTGCTGATTGTGGGCGCGGAAGCGGATACCGTGGCGCCGGTGAGCCAGCATGCGATTCC GTTTTATCAGAACCTGCCGAGCACCACCCCGAAAGTGTATGTGGAACTGTGCAACGCGAGC CATTGGGCGCCGAACAGCAACAACGCGGCGATTAGCGTGTATACCATTAGCTGGATGAAAC TGTGGGTGGATAACGATACCCGCTATCGCCAGTTTCTGTGCAACGTGAACGATCCGGCGCT GTGCGATTTTCGCACCAACAACCGCCATTGCCAG Table H(ii) - Exemplary nucleic acid sequences encoding the fusion proteins comprising polymer binding domains SEQ Sequence ID NO151ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGCCCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGGGCTCTGCCGGTAGCGCCGCGGGCTCCGGCTAT GAAATGCCGTCTGAGGAAGGTTACCAGGACTATGAACCGGAAGCC152ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGCCCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGGCACAGGCAGCTCCTGGTTGTCGTGTCGATTATG CAGTGACCAACCAGTGGCCGGGCGGTTTTGGTGCGAATGTTACTATTACTAACCTGGGCGA TCCGGTTTCCAGCTGGAAACTGGATTGGACCTATACCGCTGGTCAGCGTATCCAGCAACTGT GGAACGGTACCGCTTCTACCAACGGCGGTCAGGTTTCTGTGACTTCTCTGCCGTGGAACGG CTCCATCCCAACCGGCGGTACCGCCAGCTTCGGTTTTAACGGCTCTTGGGCGGGCAGCAAC CCGACCCCTGCTTCTTTTTCCCTGAACGGTACTACCTGTACCGGTACCGTACCGACTACCTC CCCGACTCCGACCCCTACCCCGACCACGCCGACCCCTACCCCGACCCCGACTCCAACCCCT ACGCCAACTGTCACTCCGCAACCGACCTCTGGTTTCTACGTTGATCCGACGACCCAGGGTTA CCGC ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGC CCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGCCGCCTGGCGGTAACCGTGGCACCACTACCACTC GCCGTCCGGCCACCACTACCGGTTCTTCCCCGGGCCCAATGAAATTCTTTGCTGTAGCGGC ACTGTTCGTGGCGTCCGCAATGGCCTCTCCGATGGGCTCTGAAGGTTGCCCAGGCGGTCTG ACCAACACTGTTCCGCTGTGTTGCGCGACGAACGTGCTGGGTGTAGCTACGCTGGATTGCT CTACCCCGACCGTGCCAGTACCGAACGTTGGCATCTTCCAGGCACATTGCGCTAGCAAAGG CAAACAGCCGGTGTGTTGCACTGTTCCAGTGGCCGGCCTGGGCCTCCTGTGTCAGAAACCT ACCGGCGCCCAG ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGC CCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGGGCGGTGGCGGTAGCGGTGGCGGTGGCTCCTAC GAGATGCCGTCCGAAGAGGGCTACCAGGACTATGAGCCGGAAGCGATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGCCCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGCCTCCGGGTGGCAACCGTGGTACTACCACTACCC GCCGTCCGGCGACCACTACCGGTTCTTCCCCGGGCCCGACTCAGAGCGCGTTTACTTGTAC GGCGACCACTGCATCTAACTACGCCCACGTGCAGGCAGGCCGTGCGCACGACTCCGGCGG TATCGCATACGCAAACGGCAGCAACCAGAGCATGGGTCTGGACAACCTGTTCTACACGTCC ACCCTGGCTCAGACCGCGGCAGGCTACTATATCGTTGGTAACTGCCCGATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGCCCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGCCACCGGGTGGCAACCGCGGTACTACCACGACTC GTCGCCCGGCTACTACCACTGGCTCTAGCCCGGGTCCTATGCAGTACTCCGCGATCGTTGC CCTGTTCGCCACCCTGGCTGTGGCGGCTCCGGCACAGGAGGCCGCGGCAGATATTGCGAT CCTGGATGGTCCATGTACGGCGGGTGTGACTAATAACATCCCGATGTGCTGTGGCTCCGGC ATTCTGGATCTCCTGTACCTGGACTGTGAAACCCCAACTCAGGCGACCTCTGTTCTGAACCC ACTGTCCGCGGTATGCGGCCGTGTGGGTCTGCAAGCTAAATGTTGCACGCTCGGTATCGCG GATCTGGGTGTACTGTGCCAGGATGCTCTGCCGGAG ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGC CCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGCCACCGGGTGGCAACCGTGGCACCACGACCACTC GCCGTCCGGCTACTACCACTGGTTCTTCCCCTGGTCCTACCCAATCTCACTATGGTCAGTGT GGTGGCATTGGCTACTCCGGCCCAACCGTTTGTGCGTCTGGTACCACTTGTCAGGTCCTCAA CCCGTACTATTCCCAGTGCCTG ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGC CCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGACCTTTTCTGTAACGTCCAACTGGGGTAGCGGCT ACAACTTCTCCATCGTTATCAAAAACTCCGGCACCACGCCGATCAAAAACTGGAAACTGGAG TTCGACTACAACGGCAACCTGACCCAGGTATGGGATAGCAAAATCTCTTCCAAAATCAATAA CCACTACGTTATCACCAACGCTGGTTGGAACGGCGAAATTCCGCCTGGCGGCAGC ATGAACCCCTACGAGCGCGGCCCCAACCCGACCGACGCCCTGCTCGAAGCCAGCAGCGGC CCCTTCTCCGTCAGCGAGGAGAACGTCTCCCGGTTGAGCGCCAGCGGCTTCGGCGGCGGC ACCATCTACTACCCGCGGGAGAACAACACCTACGGTGCGGTGGCGATCTCCCCCGGCTACA CCGGCACTGAGGCTTCCATCGCCTGGCTGGGCGAGCGCATCGCCTCCCACGGCTTCGTCGT CATCACCATCGACACCATCACCACCCTCGACCAGCCGGACAGCCGGGCAGAGCAGCTCAAC GCCGCGCTGAACCACATGATCAACCGGGCGTCCTCCACGGTGCGCAGCCGGATCGATAGCA GCCGACTGGCGGTCATGGGCCACTCCATGGGCGGCGGCGGCACCCTGCGTCTGGCCTCCC AGCGTCCCGACCTGAAGGCCGCCATCCCGCTCACCCCGTGGCACCTCAACAAGAACTGGAG CAGCGTCACCGTGCCGACGCTGATCATCGGGGCCGACCTCGACACGATCGCGCCGGTCGC CACGCACGCGAAACCGTTCTACAACAGCCTGCCGAGCTCCATCAGCAAGGCCTACCTGGAG CTGGACGGCGCAACCCACTTCGCCCCGAACATCCCCAACAAGATCATCGGCAAGTACAGCG TCGCCTGGCTCAAGCGGTTCGTCGACAACGACACCCGCTACACCCAGTTCCTCTGCCCCGG ACCGCGCGACGGACTCTTCGGCGAGGTCGAAGAGTACCGCTCCACCTGCCCGTTCGGCGC GGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGTCCAACCCGTACCAGCGCGGT CCCAACCCCACGCGGAGCGCGCTCACGGCCGACGGGCCGTTCTCGGTGGCAACCTACACC GTTTCGCGGCTCTCGGTGAGCGGCTTCGGGGGCGGGGTGATCTACTACCCCACAGGCACCT CGCTGACCTTCGGCGGGATCGCCATGTCGCCGGGGTACACGGCCGACGCCAGTTCGCTGG CGTGGCTCGGGCGGCGGTTGGCATCGCACGGCTTCGTGGTGCTCGTCATCAACACGAACTC GCGATTCGACGGCCCTGACTCCCGCGCAAGCCAGCTATCGGCGGCGCTGAACTACCTGCG GACGAGCAGCCCCTCAGCCGTACGCGCCCGGCTCGATGCGAACCGCCTGGCCGTTGCGGG GCATTCGATGGGCGGCGGCGGGACCCTCCGCATCGCAGAGCAGAACCCGTCGCTGAAAGC GGCCGTACCGCTCACGCCGTGGCACACCGACAAGACGTTCAACACGTCGGTACCGGTGCTC ATCGTGGGAGCGGAAGCGGACACGGTCGCGCCCGTGAGCCAGCACGCCATTCCGTTCTAC CAGAACTTGCCCTCGACCACGCCGAAGGTGTACGTGGAGCTCTGCAATGCGTCGCACTGGG CGCCCAACAGCAACAACGCGGCGATCTCCGTGTACACCATCTCGTGGATGAAGCTGTGGGT GGATAACGACACCCGCTACCGGCAGTTCCTCTGCAACGTGAACGATCCGGCGCTGTGCGAC TTCCGGACGAACAACCGCCACTGCCAGGCTGAAGCAGCTAAAGAAGCAGCTAAAGAAGCTG CGAAAGCCTATAGCCGTTGTCAGCTGCAGGGTTTTAACTGCGTGGTACGTTCTTATGGTCTG CCTACTATTCCGTGTTGCCGTGGTCTGACGTGTCGTTCTTATTTCCCTGGTAGCACCTATGG CCGTTGCCAGCGTTAC ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGGC GGTGGCGGTTCTGGCGGTGGCGGTTCTTACTCCCGCTGCCAGCTGCAGGGTTTTAACTGTG TAGTTCGCTCCTATGGCCTCCCGACTATTCCGTGTTGCCGCGGTCTGACCTGTCGCTCCTAC TTCCCTGGTTCTACGTACGGCCGTTGTCAACGCTAC ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGGC GGTGGCGGTAGCGGTGGCGGTGGCTCCTACGAGATGCCGTCCGAAGAGGGCTACCAGGAC TATGAGCCGGAAGCG ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGGC GGTGGCGGTTCCGGCGGTGGCGGTTCTGGCGGTGGCGGTAGCGGTCTGTGGTCTACCATC AAACAGAAAGGCAAGGAAGCGGCAATCGCCGCTGCGAAAGCAGCTGGTCAGGCCGCTCTG GGTGCTCTG ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGCCG CCTGGCGGTAACCGTGGCACCACTACCACTCGCCGTCCGGCCACCACTACCGGTTCTTCCC CGGGCCCAATGAAATTCTTTGCTGTAGCGGCACTGTTCGTGGCGTCCGCAATGGCCTCTCC GATGGGCTCTGAAGGTTGCCCAGGCGGTCTGACCAACACTGTTCCGCTGTGTTGCGCGACG AACGTGCTGGGTGTAGCTACGCTGGATTGCTCTACCCCGACCGTGCCAGTACCGAACGTTG GCATCTTCCAGGCACATTGCGCTAGCAAAGGCAAACAGCCGGTGTGTTGCACTGTTCCAGT GGCCGGCCTGGGCCTCCTGTGTCAGAAACCTACCGGCGCCCAG ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGCCT CCGGGTGGCAACCGTGGTACTACCACTACCCGCCGTCCGGCGACCACTACCGGTTCTTCCC CGGGCCCGACTCAGAGCGCGTTTACTTGTACGGCGACCACTGCATCTAACTACGCCCACGT GCAGGCAGGCCGTGCGCACGACTCCGGCGGTATCGCATACGCAAACGGCAGCAACCAGAG CATGGGTCTGGACAACCTGTTCTACACGTCCACCCTGGCTCAGACCGCGGCAGGCTACTAT ATCGTTGGTAACTGCCCGATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACAATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGGC TCTGCCGGTAGCGCCGCGGGCTCCGGCTATGAAATGCCGTCTGAGGAAGGTTACCAGGACT ATGAACCGGAAGCC ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGCA CAGGCAGCTCCTGGTTGTCGTGTCGATTATGCAGTGACCAACCAGTGGCCGGGCGGTTTTG GTGCGAATGTTACTATTACTAACCTGGGCGATCCGGTTTCCAGCTGGAAACTGGATTGGACC TATACCGCTGGTCAGCGTATCCAGCAACTGTGGAACGGTACCGCTTCTACCAACGGCGGTC AGGTTTCTGTGACTTCTCTGCCGTGGAACGGCTCCATCCCAACCGGCGGTACCGCCAGCTT CGGTTTTAACGGCTCTTGGGCGGGCAGCAACCCGACCCCTGCTTCTTTTTCCCTGAACGGTA CTACCTGTACCGGTACCGTACCGACTACCTCCCCGACTCCGACCCCTACCCCGACCACGCC GACCCCTACCCCGACCCCGACTCCAACCCCTACGCCAACTGTCACTCCGCAACCGACCTCTG GTTTCTACGTTGATCCGACGACCCAGGGTTACCGC ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGCCA CCGGGTGGCAACCGCGGTACTACCACGACTCGTCGCCCGGCTACTACCACTGGCTCTAGCC CGGGTCCTATGCAGTACTCCGCGATCGTTGCCCTGTTCGCCACCCTGGCTGTGGCGGCTCC GGCACAGGAGGCCGCGGCAGATATTGCGATCCTGGATGGTCCATGTACGGCGGGTGTGAC TAATAACATCCCGATGTGCTGTGGCTCCGGCATTCTGGATCTCCTGTACCTGGACTGTGAAA CCCCAACTCAGGCGACCTCTGTTCTGAACCCACTGTCCGCGGTATGCGGCCGTGTGGGTCT GCAAGCTAAATGTTGCACGCTCGGTATCGCGGATCTGGGTGTACTGTGCCAGGATGCTCTG CCGGAG ATGCGGCCTGTTCGACGAGCGGTTCCGCAAGATCTGCTCGACCAGTTTGAACTCTTTTCACA ATATTCGGCGGCCGCATACTGTGCGGCAAACAATCATGCTCCAGTGGGCTCAGACGTAACG TGCTCGGAGAATGTCTGCCCTGAGGTAGATGCGGCGGACGCAACGTTTCTCTATTCTTTTGA AGATTCTGGATTAGGCGATGTTACCGGCCTTCTCGCTCTCGACAACACGAATAAACTGATCG TCCTCTCTTTCCGCGGCTCTCGCTCAGTAGAGAACTGGATCGCGAACCTCGCCGCCGACCT GACAGAAATATCTGACATCTGCTCCGGCTGCGAGGGGCATGTCGGCTTCGTTACTTCTTGGA GGTCTGTAGCCGACACTATAAGGGAGCAGGTGCAGAATGCCGTGAACGAGCATCCCGATTA CCGCGTGGTCTTTACCGGACATAGCTTGGGAGGCGCACTGGCAACTATTGCCGCAGCAGCT CTGCGAGGAAATGGATACAATATCGACGTGTTCTCATATGGCGCGCCCCGCGTCGGTAACA GGGCATTTGCAGAATTCCTGACCGCACAGACGGGCGGCACCCTGTATCGCATCACCCATAC CAATGATATCGTCCCTAGACTCCCTCCTCGAGACTGGGGTTACAGCCACTCTAGCCCGGAGT ACTGGGTCACGTCTGGTAACGACGTCCCAGTGACCGCAAACGACATCACCGTCGTGGAGGG CATCGATTCCACCGACGGGAACAACCAGGGGAATATCCCAGACATCCCTTCGCATCTATGGT ATTTCGGTCCCATTTCAGAGTGTGATGGCGCGGGCGCGGGCGCGGGCGCGGGCGCGGGC GCGGGCGCGTCCAACCCGTACCAGCGCGGTCCCAACCCCACGCGGAGCGCGCTCACGGCC GACGGGCCGTTCTCGGTGGCAACCTACACCGTTTCGCGGCTCTCGGTGAGCGGCTTCGGG GGCGGGGTGATCTACTACCCCACAGGCACCTCGCTGACCTTCGGCGGGATCGCCATGTCGC CGGGGTACACGGCCGACGCCAGTTCGCTGGCGTGGCTCGGGCGGCGGTTGGCATCGCACG GCTTCGTGGTGCTCGTCATCAACACGAACTCGCGATTCGACGGCCCTGACTCCCGCGCAAG CCAGCTATCGGCGGCGCTGAACTACCTGCGGACGAGCAGCCCCTCAGCCGTACGCGCCCG GCTCGATGCGAACCGCCTGGCCGTTGCGGGGCATTCGATGGGCGGCGGCGGGACCCTCCG CATCGCAGAGCAGAACCCGTCGCTGAAAGCGGCCGTACCGCTCACGCCGTGGCACACCGA CAAGACGTTCAACACGTCGGTACCGGTGCTCATCGTGGGAGCGGAAGCGGACACGGTCGC GCCCGTGAGCCAGCACGCCATTCCGTTCTACCAGAACTTGCCCTCGACCACGCCGAAGGTG TACGTGGAGCTCTGCAATGCGTCGCACTGGGCGCCCAACAGCAACAACGCGGCGATCTCCG TGTACACCATCTCGTGGATGAAGCTGTGGGTGGATAACGACACCCGCTACCGGCAGTTCCT CTGCAACGTGAACGATCCGGCGCTGTGCGACTTCCGGACGAACAACCGCCACTGCCAGGCT GAAGCAGCTAAAGAAGCAGCTAAAGAAGCTGCGAAAGCCTATAGCCGTTGTCAGCTGCAGG GTTTTAACTGCGTGGTACGTTCTTATGGTCTGCCTACTATTCCGTGTTGCCGTGGTCTGACG TGTCGTTCTTATTTCCCTGGTAGCACCTATGGCCGTTGCCAGCGTTAC ATGACCAACCCGTATGCGCGCGGCCCGAACCCGACCGCGGCGAGCCTGGAAGCGAGCGCG GGCCCGTTTACCGTGCGCAGCTTTACCGTGAGCCGCCCGAGCGGCTATGGCGCGGGCACC GTGTATTATCCGACCAACGCGGGCGGCACCGTGGGCGCGATTGCGATTGTGCCGGGCTATA CCGCGCGCCAGAGCAGCATTAAATGGTGGGGCCCGCGCCTGGCGAGCCATGGCTTTGTGG TGATTACCATTGATACCAACAGCACCCTGGATCAGCCGGAAAGCCGCAGCAGCCAGCAGAT GGCGGCGCTGCGCCAGGTGGCGAGCCTGAACGGCACCAGCAGCAGCCCGATTTATGGCAA AGTGGATACCGCGCGCATGGGCGTGATGGGCTGGAGCATGGGCGGCGGCGGCAGCCTGA TTAGCGCGGCGAACAACCCGAGCCTGAAAGCGGCGGCGCCGCAGGCGCCGTGGCATAGCA GCACCAACTTTAGCAGCGTGACCGTGCCGACCCTGATTTTTGCGTGCGAAAACGATAGCATT GCGCCGGTGAACAGCAGCGCGCTGCCGATTTATGATAGCATGAGCCGCAACGCGAAACAGT TTCTGGAAATTAACGGCGGCAGCCATAGCTGCGCGAACAGCGGCAACAGCAACCAGGCGCT GATTGGCAAAAAAGGCGTGGCGTGGATGAAACGCTTTATGGATAACGATACCCGCTATAGC ACCTTTGCGTGCGAAAACCCGAACAGCACCGCGGTGAGCGATTTTCGCACCGCGAACTGCA GCCCGGCGGTGCCGCCGCCGGCGGCGAACCCGTATGAACGCGGCCCGAACCCGACCAACA GCAGCATTGAAGCGCTGCGCGGCCCGTTTCGCGTGGATGAAGAACGCGTGAGCCGCCTGC AGGCGCGCGGCTTTGGCGGCGGCACCATTTATTATCCGACCGATAACAACACCTTTGGCGC GGTGGCGATTAGCCCGGGCTATACCGGCACCCAGAGCAGCATTAGCTGGCTGGGCGAACG CCTGGCGAGCCATGGCTTTGTGGTGATGACCATTGATACCAACACCACCCTGGATCAGCCG GATAGCCGCGCGAGCCAGCTGGATGCGGCGCTGGATTATATGGTGGAAGATAGCAGCTATA GCGTGCGCAACCGCATTGATAGCAGCCGCCTGGCGGCGATGGGCCATAGCATGGGCGGCG GCGGCACCCTGCGCCTGGCGGAACGCCGCCCGGATCTGCAGGCGGCGATTCCGCTGACCC CGTGGCATACCGATAAAACCTGGGGCAGCGTGCGCGTGCCGACCCTGATTATTGGCGCGGA AAACGATACCATTGCGAGCGTGCGCAGCCATAGCGAACCGTTTTATAACAGCCTGCCGGGC AGCCTGGATAAAGCGTATCTGGAACTGGATGGCGCGAGCCATTTTGCGCCGAACCTGAGCA ACACCACCATTGCGAAATATAGCATTAGCTGGCTGAAACGCTTTGTGGATGATGATACCCGC TATACCCAGTTTCTGTGCCCGGGCCCGAGCACCGGCTGGGGCAGCGATGTGGAAGAATATC GCAGCACCTGCCCGTTTGGCGGTGGCGGTTCTGGCGGTGGCGGTTCTTACTCCCGCTGCCA GCTGCAGGGTTTTAACTGTGTAGTTCGCTCCTATGGCCTCCCGACTATTCCGTGTTGCCGCG GTCTGACCTGTCGCTCCTACTTCCCTGGTTCTACGTACGGCCGTTGTCAACGCTAC The invention also provides a nucleic acid vector comprising the nucleic acid of the invention. The skilled person will understand that by nucleic acid vector we include the meaning of a plasmid, phage, artificial chromosome or other nucleic acid structure used to deliver or express at least one polypeptide or at least one domain thereof. The artificial chromosome may be any artificial chromosome and may be selected from, for example, a bacterial artificial chromosome (BAC), a yeast artificial chromosome (YAC), and a Human artificial chromosome (HAC). In one embodiment, the vector is a recombinant expression vector. The invention also provides a cell that comprises at least one fusion protein of the invention (or at least one domain thereof), at least one polynucleotide of the invention and / or at least one vector of the invention. In one embodiment, the cell is a cell that is used in the commercial, large scale manufacture of the fusion proteins of the invention, for example is a bacterial cell such as E. coli, or a fungal cell (such as a yeast cell such as P. pastoris), or a cell derived from a mammal, a plant, virus, insect or otherwise. One skilled in the art will appreciate that any cell capable of heterologously expressing a fusion protein of the invention may be suitable. In one embodiment, the cell is a bacterium, such as Escherichia coli or a bacterium of the genus bacillus. The E. coli cell may be a competent E. coli cell, such as a BL21(DE3) competent E. coli cell. Alternatively, the cell may be from a B. subtilis strain 168 or B. subtilis RIK1285 bacterium. In some embodiments, a nucleic acid or vector as disclosed herein is configures to be integrated into the genome of the host cell. In an alternative embodiment, a nucleic acid or vector as disclosed herein is configured to remain physically separated and replicate independently from the chromosomal DNA of the host cell. Methods of producing the fusion proteins of the invention The invention further provides a method of producing the fusion protein of the invention or a fragment thereof. In some embodiments, the method comprises the steps of: (i) providing one or more cells provided herein, (ii) culturing said cells in conditions suitable for the expression of the fusion protein, and (iii) obtaining a fusion protein from said culture. Methods and techniques of heterologously expressing a polypeptide, such as the fusion proteins of the invention, from a host cell, such as those provided by the invention, are well known in the art. A skilled person would thus immediately appreciate the conditions that are suitable for expression of a fusion protein and how these are dependent on the nature of the host cell. For example, in one embodiment, the one or more cells are cultured in a microbial growth medium. The growth medium may be selected from the group consisting of LB medium, TB medium, SOC medium, minimal and complex medium, or expression medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α-lactose). Additionally or alternatively, the cells may be cultured at a temperature in the range of about 5°C to about 50°C, such as about 5°C to about 30°C, 10°C to about 30°C, 10°C to about 20°C, 25°C to about 45°C, about 30°C to about 40°C, or about 35°C to about 40°C. In a preferred embodiment, the temperature is about 16°C. One skilled in the art will appreciate that the fusion protein may be secreted by the one or more cells. For example, the fusion protein may comprise a signal peptide capable of targeting the cell for translocation to the secretory pathway. Signal peptides are known in the art, and include, for example: • the signal peptide of Burkholderia ambifaria: MARSMRSRVVAGAVACAMSVAPFA (SEQ ID NO: 109); • the signal peptide from Escherichia coli: MKKLAIMAAASMVFAVSSAHA (SEQ ID NO: 110); and • the serine protease signal peptide from Escherichia coli: MNKIYSIKYSAATGGLIAVSELAKKVICKTNRKISAALLSLAVISYTNIIYA (SEQ ID NO: 111) In one embodiment, step (iii) of obtaining the fusion protein comprises lysing the cells provided in step (i). Methods and techniques of lysing the cells to release intracellular polypeptides are well known in the art, and may encompass mechanical shearing (e.g., sonication, centrifugation, snap-freezing and similar) or chemical treatment (e.g., with surfactants). Additionally or alternatively, the fusion protein is solution following secretion by the cells or release by lysing the cells can be obtained using a variety of methods known in the art. For example, Immobilized Metal Affinity Chromatography (IMAC), Ion Exchange Chromatography, Hydrophobic Interaction Chromatography (IEX), membrane filtration, thermos-precipitation, affinity precipitation, or aqueous two-phase extraction. Methods of degrading one or more plastic polymers Since the fusion proteins of the invention are able to degrade at least one plastic polymer, for example PET, it will be apparent to the skilled person that the fusion proteins of the invention have use in methods of degrading plastic polymers. For example, in one embodiment the fusion proteins of the invention are useful in degrading one or more plastic polymers and / or degrading one or more plastic polymers in mixtures containing plastic polymers (e.g., waste mixtures). Accordingly, provided is a method of degrading one or more plastic polymers comprising contacting the one or more plastic polymers with one or more of the fusion proteins of the invention. Provided is also use of one or more fusion proteins according to the invention to degrade one or more plastic polymers, the use comprising contacting the one or more plastic polymers with the one or more fusion proteins. It will be appreciated that the one or more plastic polymers may comprise or consist of any plastic polymer that a fusion protein according to the invention is capable of degrading. Particularly, in some embodiments, the one or more plastic polymers comprise or consist of PET, PTT, PBT, PEF, PLA, PCL, PBAT, blends or combinations thereof, or mixed plastic waste. In some embodiments, the polymer is formed as a foam, powder, fibre, paste, flake or pellet. In some embodiments, the plastic polymer is PET. Particularly, in some embodiments, the PET may be in amorphous, semi-crystalline or crystalline form. In one embodiment, the one or more fusion proteins and the one or more plastic polymers are contacted in a solution. Without wanting to be bound by theory, it will be appreciated that certain catalytic proteins, particularly hydrolases (such as serine hydrolases) may require or function more efficiently in the presence of an aqueous solution. Additionally, the fusion protein(s) may be present in solution or may be immobilized to a solid support. By solid support we mean any material or composition to which the fusion protein may be attached to. In some embodiments, the solid support may be immobile, such as the surface of a reaction container. In an additional or alternative embodiment, the solid support may be mobile and capable of being intermixed with the solution, such as solid beads. In an alternative embodiment, the solid support may be a biological agent capable of maintaining the fusion protein in solution, such as a vesicle or lipid nanoparticle. In some additional or alternative embodiments, the fusion protein may be coupled to a stimuli-responsive polymer. As used herein, “stimuli-responsive polymers” refers to polymers capable of changing one or more physical properties in response to the environment they are in. Particularly, the solubility (e.g., in an aqueous solution) of the stimuli-response polymer may change according to one or more of the pH, temperature and salt concentration of the environment (i.e., of the solution). As detailed above, it will be appreciated that the plastic degrading efficiency of a protein capable of degrading one or more plastic polymers, such as the fusion proteins of the invention, will be affected by the conditions in which the one or more plastic polymers are contacted with the protein. One skilled in the art will appreciate that certain conditions generally favour protein (enzyme) driven catalytic reactions. Similarly, certain conditions may favour specific plastic polymer degradation by a protein capable of catalysing said reaction, such as the fusion proteins of the invention. Accordingly, in some embodiments, the solution in which the one more plastic polymer(s) is contacted with the fusion protein(s) of the invention may have specific conditions, which are sufficient for the efficient degradation of the one or more plastic polymer(s) by the fusion protein(s). For example, in some embodiments, the solution may have a pH in the range of about 5 to about 10, such as about 6 to about 9, about 7 to about 9, about 7 to about 8 or about 8 to about 9. It will be apparent to one skilled in the art that a particular solution may provide a particular pH or may allow for a particular pH to be maintained. For example, in some embodiments, the solution may comprise a buffer solution, such as potassium phosphate buffer, Tris-HCl buffer or Bicine buffer. As detailed throughout this specification, the temperature at which said one or more plastic polymers and said fusion proteins are contacted may also affect the plastic polymer degrading efficiency of the fusion protein. This may due to the thermal stability of the fusion proteins, as described above, or due to the temperature(s) at which the catalytic reaction occurs efficiently. Accordingly, in some embodiments, said contacting is performed at a temperature in the range of about 4°C to about 90°C, such as about 10°C to about 90°C, about 20°C to about 90°C, about 30°C to about 90°C, about 40°C to about 85°C, about 50°C to about 80°C, about 55°C to about 75°C, or about 50°C to about 70°C. In an additional or alternative embodiment, said solution may be agitated, mixed or stirred during said contacting. Said agitation, mixing or stirring may ensure or improving efficient contacting between said one or more plastic polymers and said fusion protein(s). In some embodiments, said contacting is performed for about 10 hours to about 672 hours, such as about 10 hours to about 672 hours, about 14 hours to about 608 hours, about 18 hours to about 544 hours, about 22 hours to about 480 hours, about 26 hours to about 416 hours, about 30 hours to about 352 hours, about 34 hours to about 288 hours, about 38 hours to about 224 hours, about 42 hours to about 160 hours, about 46 hours to about 128 hours or about 48 hours to about 96 hours. One skilled in the art will further appreciate that the plastic degradation efficiency of the fusion proteins of the invention may be affected by the ratio of fusion protein to its substrate (i.e., one or more plastic polymer(s)). Accordingly, in some embodiments, said one or more plastic polymers are present at a concentration in the range of about 0.1 g / L to about 700 g / L, such as about 0.1 g / L to about 700 g / L, about 5 g / L to about 650 g / L, about 10 g / L to about 600 g / L, about 15 g / L to about 550 g / L, about 20 g / L to about 500 g / L, about 25 g / L to about 450 g / L, about 30 g / L to about 400 g / L, about 35 g / L to about 350 g / L, about 40 g / L to about 300 g / L, about 45 g / L to about 250 g / L or about 50 g / L to about 200 g / L. In a preferred embodiment, the said one or more plastic polymers are present at a concentration of 50 g / L to about 200 g / L. In an additional or alternative embodiment, said one or more fusion proteins are present at a concentration in the range of about 0.001 µM to about 100 µM, such as about 0.001 µM to about 100 µM, about 0.025 µM to about 90 µM, about 0.05 µM to about 80 µM, about 0.075 µM to about 70 µM, about 0.1 µM to about 60 µM, about 0.125 µM to about 50 µM, about 0.15 µM to about 40 µM, about 0.175 µM to about 30 µM, about 0.2 µM to about 20 µM, about 0.225 µM to about 10 µM, about 0.25 µM to about 1 µM, about 0.25 µM to about 0.75 µM, about 1 µM to about 3 µM, or about 1.5 µM to about 2.5 µM. In a preferred embodiment, said one or more fusion proteins are present at a concentration of about 1.5 µM to about 2.5 µM. As detailed above, methods of determining the plastic polymer degradation activity of a polypeptide are known in the art. For example, plastic polymer degradation can be determined as detailed previously, by contacting the polypeptide with an exemplary plastic polymer (e.g., PET) and measuring the concentration of plastic polymer-derived monomers, for example by HPLC. One skilled in the art will appreciate that the plastic polymer degradation efficiency of the fusion proteins may be increased or improved by release, purification, or removal of non- plastic polymer components or plastic polymer(s) which cannot be degraded by the fusion protein, from a mixture comprising one or more plastic polymer components. By way of example, removal of organic material from a mixture comprising organic material and one or more plastic polymers, can improve the plastic polymer degradation efficiency of the fusion protein(s). Removal of such components may be done by physical removal (e.g., filtration or centrifugation), chemical means (i.e., pyrolysis or acid degradation) or enzymatically using one or more additional catalytically active proteins capable of degrading such components. In some embodiments, removal of such components is performed by the method further comprising a step of contacting said one or more plastic polymers with one or more additional catalytically active proteins. In some embodiments, said one or more additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulase, or a pectinase. Particularly, it may be advantageous to remove such components prior to contacting said one or more plastic polymers with said fusion protein(s). Accordingly, in some embodiments, said further step of contacting said one or more plastic polymers with one or more additional catalytically active proteins is carried prior to the step of contacting said one or more plastic polymers with said one or more fusion proteins. Kits Provided herein are also kits for use in the method of degrading one or more plastic polymers. In one embodiment, the kit comprises comprising (i) one or more fusion proteins according to the invention and (ii) a suitable buffer solution and / or one or more additional catalytically active proteins. The buffer solution may be selected from the group consisting of potassium phosphate buffer, Tris-HCl buffer or Bicine buffer. Additionally or alternatively, the optional additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulose, or a pectinase. Certain aspects and embodiments of the present invention are also provided in the following list of numbered paragraphs: 1. A fusion protein capable of degrading a plastic polymer, wherein the fusion protein comprises two or more serine hydrolase domains. 2. The fusion protein of paragraph 1, further comprising one or more polymer binding domain(s). 3. The fusion protein of paragraph 1 or 2, wherein one or more, two or more, three or more, four or more, five or more or six or more serine hydrolase domains are catalytically active. 4. The fusion protein of any of the proceeding paragraphs, wherein all serine hydrolase domains are catalytically active. 5. The fusion protein of any of the preceding paragraphs comprising two serine hydrolase domains. 6. The fusion protein of any of the preceding paragraphs, wherein at least one serine hydrolase domain is an esterase, a lipase or a protease, or a catalytically active portion thereof. 7. The fusion protein of paragraph 6, wherein at least one esterase is selected from the group consisting of a PETase, a MHETase, and a cutinase, or a catalytically active portion thereof. 8. The fusion protein of any of the preceding paragraphs, wherein at least one serine hydrolase domain comprises a cutinase or a PETase, or a catalytically active portion thereof. 9. The fusion protein of paragraph 6, wherein at least one protease is proteinase K, or a catalytically active portion thereof. 10. The fusion protein of any one of paragraphs 6 or 7, wherein at least one cutinase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11. 11. The fusion protein of paragraphs 7 or 8, wherein at least one PETase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 12, 13 or 14, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 12, 13 or 14. 12. The fusion protein of paragraph 6, wherein at least one lipase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 9 or 10, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 9 or 10. 13. The fusion protein of any of the preceding paragraphs, wherein the amino acid sequence of two or more serine hydrolase domains is the same. 14. The fusion protein of the preceding paragraphs, wherein the amino acid sequences of at least two serine hydrolase domains comprise no more than about 95% sequence identity, such as no more than about 90%, 85%, 80%, 75%, 70%, 65%, 60%, 55% or 50% sequence identity. 15. The fusion protein of paragraph 2-14, wherein the one or more polymer binding domains are selected from the group consisting of a hydrophobin, a cellulose binding domain, a carbohydrate binding module, an anchor peptide, an anchor linker peptide, PET binding domain and PHA binding domains. 16. The fusion protein of any one of paragraphs 2-15, wherein the one or more polymer binding domains are capable of binding one or more plastic polymer(s), optionally wherein the one or more plastic polymer(s) are selected from the group consisting of PET, PTT, PBT, PEF, PLA, PCL, PBAT and MHET. 17. The fusion protein of any one of paragraphs 2-16, wherein the one or more polymer binding domain comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 85-96 and / or SEQ ID NO: 112-121, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: SEQ ID NO: 85-96 and / or SEQ ID NO: 112-121. 18. The fusion protein of any of the preceding paragraphs, wherein two or more serine hydrolase domains or at least one serine hydrolase domain and at least one polymer binding domain are coupled by a linker. 19. The fusion protein of paragraph 18, wherein the linker is a polypeptide linker. 20. The fusion protein of paragraph 19, wherein the linker is selected from the group consisting of a polyglycine linker, a polyalanine linker, an alanine-glycine linker, a glycine-serine linker, a histidine linker, threonine-serine linker, a glutamine linker, an asparagine linker. 21. The fusion protein of paragraph 19, wherein the linker comprises the polypeptide sequence of any one of SEQ ID NO: 57-70. 22. The fusion protein of any one of paragraphs 18-21, wherein the fusion protein has increased or improved stability and / or expression capabilities. 23. The fusion protein of paragraph 22, wherein the improved stability and / or expression capabilities are improved compared to a fusion protein without a linker and / or comprising a flexible linker. 24. The fusion protein of any one of paragraphs 19-23, wherein the linker comprises between about 4 to about 20 amino acids, such as between about 5 to about 18 amino acids, about 6 to about 16 amino acids, about 7 to about 16 amino acids, about 8 to about 14 amino acids or about 10 to about 12 amino acids. 25. The fusion protein of any one of paragraphs 18-24, wherein the linker is coupled to the C-terminal end of the first serine hydrolase domain and to the N-terminal end of the second serine hydrolase domain. 26. The fusion protein of any of the preceding paragraphs, comprising an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149 or 150. 27. The fusion protein of paragraph 26, comprising or consisting of the amino acid sequence of any of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149 or 150, or a variant, fragment or derivative thereof. 28. The fusion protein of any of the preceding paragraphs, wherein the fusion protein has increased or improved thermal stability. 29. The fusion protein of paragraph 28, wherein the fusion protein has increased or improved thermal stability compared to each constituent serine hydrolase domain separately. 30. The fusion protein of any of the preceding paragraphs, wherein the fusion protein has increased or improved plastic polymer degradation activity. 31. The fusion protein of paragraph 30, wherein the fusion protein has increased or improved degradation activity of at least one plastic polymer selected from the group consisting of PET, PTT, PBT, PEF, PLA, PCL, PBAT, MHET, blends or combinations thereof, and mixed plastic waste. 32. The fusion protein of paragraphs 30 or 31, wherein the fusion protein has increased or improved plastic polymer degradation compared to each constituent serine hydrolase domain separately. 33. The fusion protein of any one of paragraphs 30–32, wherein the fusion protein has similar, equal, increased or improved plastic polymer degradation compared to LCC, or a variant or derivative thereof. 34. The fusion protein of any one of paragraph 30-33, wherein the fusion protein has increased or improved plastic polymer degradation activity when one or more of the plastic polymers has not been subject to pre-treatment. 35. The fusion protein of paragraph 34, wherein the pre-treatment comprises at least one step selected from the group consisting of an enzymatic treatment, a mechanical treatment, a chemical treatment and heat treatment. 36. The fusion protein of paragraph 35, wherein the mechanical treatment comprises one or more of grinding, milling, extrusion and / or spinning. 37. The fusion protein of paragraph 35, wherein the chemical treatment comprises one or more of pyrolysis, gasification and / or hydro-cracking. 38. The fusion protein of any of the preceding paragraphs, wherein the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 37°C. 39. The fusion protein of paragraph 38, wherein the temperature is at least 40°C, such as at least 45°C, at least 50°C, at least 55°C, at least 60°C, at least 65°C, at least 70°C, at least 75°C, at least 80°C, or at least 90°C. 40. A polynucleotide encoding the fusion protein of any of paragraphs 1-39. 41. The polynucleotide of paragraph 40, comprising a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168 or 169. 42. A vector comprising at least one polynucleotide according to paragraph 40 or 41. 43. The vector according to paragraph 43, wherein said vector is a recombinant expression vector. 44. A cell comprising the fusion protein according to any one of paragraphs 1-39, the polynucleotide according to paragraph 40 or 41 or the vector according to paragraph 42 or 43. 45. The cell of paragraph 44, wherein the cell is a mammalian cell, a fungal cell or a bacterial cell. 46. The cell of paragraph 45, wherein the cell is a bacterium, optionally wherein the bacterium is Escherichia coli or a bacterium of the genus bacillus. 47. The cell of paragraph 45 or 46, wherein the cell is a competent E. coli cell, optionally a BL21(DE3) competent E. coli cell. 48. The cell of paragraph 45 or 46, wherein the cell is a cell from a B. subtilis strain 168 or B. subtilis RIK1285 bacterium. 49. A method of producing a fusion protein according to any one of paragraphs 1-39 comprising the steps of: (i) providing one or more cells of any one of paragraphs 44-48, (ii) culturing said cells in conditions suitable for the expression of the fusion protein, and (iii) obtaining a fusion protein from said culture. 50. The method of paragraph 49, wherein the one or more cells are cultured in a microbial growth medium. 51. The method of paragraph 50, wherein the growth medium is selected from the group consisting of LB medium, TB medium, SOC medium, minimal and complex medium, or expression medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α-lactose). 52. The method of any one of paragraphs 49-51, wherein the cells are cultured at a temperature in the range of about 5°C to about 50°C, such as about 5°C to about 30°C, 10°C to about 30°C, 10°C to about 20°C, 25°C to about 45°C, about 30°C to about 40°C, or about 35°C to about 40°C, optionally wherein the temperature is about 16°C. 53. The method of any one of paragraphs 49-52, wherein the fusion protein is secreted by the one or more cells. 54. The method of any one of paragraphs 49-53, wherein step (iii) of obtaining the fusion protein comprises one or more of: (a) lysing the cells provided in step (i), (b) Immobilized Metal Affinity Chromatography (IMAC), Ion Exchange Chromatography, Hydrophobic Interaction Chromatography (IEX), membrane filtration, thermos-precipitation, affinity precipitation, or aqueous two-phase extraction. 55. A method of degrading one or more plastic polymers comprising contacting the one or more plastic polymers with one or more of the fusion proteins of any one of paragraphs 1-39. 56. Use of one or more fusion protein according to any one of paragraphs 1-39 to degrade one or more plastic polymers, the use comprising contacting the one or more plastic polymers with the one or more fusion proteins. 57. The method or use according to paragraphs 55 or 56, wherein the one or more plastic polymers comprise or consist of PET, PTT, PBT, PBS, PEF, PLA, PCL, PBAT, PHA, blends or combinations thereof, or mixed plastic waste. 58. The method or use of any one of paragraphs 55-57, wherein the one or more fusion proteins and the one or more plastic polymers are contacted in a solution. 59. The method of paragraph 58, wherein at least one fusion is in solution. 60. The method of paragraph 58, wherein at least one fusion protein is immobilized to a solid support. 61. The method of paragraph 60, wherein said solid support is a surface or a bead. 62. The method or use of any one of paragraphs 58-61, wherein said solution has a pH in the range of about 5 to about 10, such as about 6 to about 9, about 7 to about 9, about 7 to about 8 or about 8 to about 9. 63. The method or use of any one of paragraphs 58-62, wherein said solution comprises a buffer solution, optionally wherein said buffer solution is selected from the group consisting of potassium phosphate buffer, Tris-HCl buffer or Bicine buffer. 64. The method or use of any one of paragraphs 55-63, wherein said one or more plastic polymers are present at a concentration in the range of about 0.1 g / L to about 700 g / L, such as about 0.1 g / L to about 700 g / L, about 5 g / L to about 650 g / L, about 10 g / L to about 600 g / L, about 15 g / L to about 550 g / L, about 20 g / L to about 500 g / L, about 25 g / L to about 450 g / L, about 30 g / L to about 400 g / L, about 35 g / L to about 350 g / L, about 40 g / L to about 300 g / L, about 45 g / L to about 250 g / L or about 50 g / L to about 200 g / L. 65. The method or use of any one of paragraphs 55-64, wherein said one or more fusion proteins are present at a concentration in the range of about 0.001 µM to about 100 µM, such as about 0.001 µM to about 100 µM, about 0.025 µM to about 90 µM, about 0.05 µM to about 80 µM, about 0.075 µM to about 70 µM, about 0.1 µM to about 60 µM, about 0.125 µM to about 50 µM, about 0.15 µM to about 40 µM, about 0.175 µM to about 30 µM, about 0.2 µM to about 20 µM, about 0.225 µM to about 10 µM, about 0.25 µM to about 1 µM, about 0.25 µM to about 0.75 µM, about 1 µM to about 3 µM, or about 1.5 µM to about 2.5 µM. 66. The method or use of any one of paragraphs 55-65, wherein said contacting is performed at a temperature in the range of about 4°C to about 90°C, such as about 10°C to about 90°C, about 20°C to about 90°C, about 30°C to about 90°C, about 40°C to about 85°C, about 50°C to about 80°C, about 55°C to about 75°C, or about 50°C to about 70°C. 67. The method or use of any one of paragraphs 55-66, wherein said solution is agitated, mixed or stirred during said contacting. 68. The method or use of any one of paragraphs 55-67, wherein said contacting is performed for about 10 hours to about 672 hours, such as about 10 hours to about 672 hours, about 14 hours to about 608 hours, about 18 hours to about 544 hours, about 22 hours to about 480 hours, about 26 hours to about 416 hours, about 30 hours to about 352 hours, about 34 hours to about 288 hours, about 38 hours to about 224 hours, about 42 hours to about 160 hours, about 46 hours to about 128 hours or about 48 hours to about 96 hours. 69. The method or use of any one of paragraphs 55-68, further comprising a step of contacting said one or more plastic polymers with one or more additional catalytically active proteins. 70. The method or use of paragraph 69, wherein said one or more additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulase, or a pectinase. 71. The method or use of paragraph 69 or 70, wherein said further step of contacting said one or more plastic polymers with one or more additional catalytically active proteins is carried prior to the step of contacting said one or more plastic polymers with said one or more fusion proteins. 72. A kit comprising (i) one or more fusion proteins according to any one of paragraphs 1-39 and (ii) a suitable buffer solution and / or one or more additional catalytically active proteins. 73. The kit of paragraph 72, wherein the buffer solution is selected from the group consisting of potassium phosphate buffer, Tris-HCl buffer or Bicine buffer. 74. The kit of paragraph 72 or 73, wherein the additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulose, or a pectinase. FIGURE LEGENDS Unless specified otherwise, or clearly contradicted by context, the reference to a single number in the figure legends or axis labels (e.g., 16) refers to the fusion proteins of SEQ ID NO corresponding to said number (e.g., SEQ ID NO: 16). Throughout the figures the fusion proteins are also referred to as “fusion enzymes” or “enzyme variants”. Figure 1: Total released monomers (µg / ml) from PET for screening of fusion proteins in 96 well plate. PET microparticles (semi-crystalline PET powder, Goodfellow Cambridge Ltd, Cat. No. ES306000) 10 mg / ml resuspended in 50 mM Bicine buffer (pH 9.0). 200 µl of the resuspended PET microparticles were mixed with 100 µl of the clarified cell lysate and incubated at 50oC, 450 rpm for 7 hours. The supernatant was further analyzed for PET degradation, for negative control, pET28a(+) empty vector transformed into E. coli BL 21(DE3) grown, lysed and analyzed under the same conditions. For positive control, the LCCWCCG variant was cloned and expressed and tested under the same conditions and tested under the same conditions (well no. H12). A1-H11 represents the positions of different fusion enzymes within a 96-well plate. Figure 2: SDS-PAGE of the soluble fractions of the expressed singlets as well as fusion proteins. Lanes 1, 4, 6, 8,10,12 and 14 are the soluble fractions representative for some singlet / monomeric enzymes. Lanes 2, 5, 7, 9, 11, 13 and 15 are the soluble fractions representative for some fusion proteins. Lane 3 is the Precision Plus Protein™ unstained protein ladder (Bio-Rad). Figure 3: Fusion enzymes screening for the optimum pH and buffers. Fusion proteins screened in 100 mM Tris-HCl buffer pH 7 and 8, Potassium phosphate buffer pH 8 and Bicine buffer pH 9. 0.5 µM of purified fusion proteins as well as LCCWCCGvariant were mixed Goodfellow semicrystalline PET microparticle (5 mg / ml) in 1 ml reaction volume at 60oC for 24 hours, 500 rpm. Screening was done in triplicates for each buffer with corresponding controls, the released monomers were quantified by HPLC. Figure 4: Screening for the optimum temperature of the most active fusion proteins as well as LCCWCCG variant. 0.5 µM enzymes were incubated with Goodfellow semicrystalline PET microparticle (5 mg / ml) in 1 ml reaction volume for 24 hours, 500 rpm at 37, 50, 60 and 70°C in 100 mM potassium phosphate buffer pH 8, reactions were performed in triplicates for each temperature with corresponding controls, the released monomers were analyzed by HPLC. Figure 5: Calculated protein melting temperature for the selected fusion proteins with SEQ ID NO 16, 18, 22, 23, and 24, as well as for LCCWCCG. The purified fusion enzymes were mixed with SYPRO Orange dye, in a final concentration of 5 µM and 2X, respectively. The mixture was incubated in CFX96 touch system (Bio-Rad) run with already established thermal shift assay protocol. Data were analyzed with Bio-Rad CFX maestro to derivatize the melting curves and calculate the melting temperature (Tm) of the fusion enzymes. The experiment was done in triplicate for each fusion enzyme and LCCWCCG. Figure 6: Total released monomers (µg / ml) of the amorphous PET particles after treatment with fusion enzymes. Amorphous PET microparticles (750 µm) particles were resuspended in 100 mM Phosphate buffer (pH 8) to 10 mg / ml. One milliliter of PET particlessuspension was mixed with 0.5 µM fusion enzyme variants as well as LCCWCCG andincubated at 60oC, 500 rpm, for 48 h, samples were taken at different time intervals for HPLC analysis. Amorphous PET particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 7: Total released monomers (µg / ml) of the semicrystalline PET particles after treatment with fusion proteins. Goodfellow semicrystalline PET microparticle resuspended in 100 mM Phosphate buffer (pH 8) to 10 mg / ml. One milliliter of semicrystalline PET particles suspension was mixed with 0.5 µM fusion protein variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were taken at different time intervals for HPLC analysis. Particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 8: Total released monomers (µg / ml) of the crystalline PET particles after treatment with fusion proteins. One milliliter of crystalline PET microparticles in 100 mM Phosphate buffer (pH 8) 10 mg / ml was mixed with 0.5 µM fusion protein variants as well as LCCWCCG and incubated at 60oC, 500 rpm, for 48 h, samples were taken at different time intervals for HPLC analysis. Crystalline PET particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 9: Screening for hydrolysis of polybutylene adipate terephthalate (PBAT) polymer with fusion proteins. One milliliter of PBAT particles (10mg / ml) in 100 mM Phosphate buffer (pH 8) was treated with 0.5 µM fusion enzymes variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were analyzed by HPLC. PBAT particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 10: Screening for hydrolysis of polybutylene terephthalate (PBT) polymer with fusion proteins. One milliliter of PBT particles (10mg / ml) in 100 mM Phosphate buffer (pH 8) was treated with 0.5 µM fusion enzymes variants as well as LCCWCCG and incubated at 60oC, 500 rpm, for 48 h, samples were analyzed by HPLC. PBT particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 11: Screening for hydrolysis of polytrimethylene terephthalate (PTT) polymer with fusion proteins. One milliliter of PTT particles (10mg / ml) in 100 mM Phosphate buffer (pH8) was treated with 0.5 µM fusion protein variants as well as LCCWCCG and incubated at60oC, 500 rpm, for 48 h, samples were analyzed by HPLC. PTT particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 12: Screening for hydrolysis of polycaprolactone (PCL) polymer with fusion proteins. One milliliter of PCL particles (10mg / ml) in 100 mM Phosphate buffer (pH 8) was treated with 0.5 µM fusion protein variants as well as LCCWCCG and incubated at 60oC, 500 rpm, for 48 h, samples were analyzed by HPLC. PCL particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 13: Screening for hydrolysis of polyethylene furan-2,5-dicarboxylate (PEF) polymer with fusion proteins. One milliliter of PEF particles (10mg / ml) in 100 mM Phosphate buffer (pH 8) was treated with 0.5 µM fusion protein variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were analyzed by HPLC for FDCA release. PEF particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Figure 14: Screening the activity of the fusion proteins against mixed plastic waste samples with different composition (MPW 1 – 3, shown in figure legend as 1, 2 and 3). One milliliter of the polymer particle suspension (10 mg / ml) in 100 mM Potassium phosphate buffer pH 8 was mixed with 0.5 µM fusion proteins variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were collected at different time intervals for HPLC analysis. The reactions were run in triplicates. Figure 15: Depolymerization profile of mixed plastic waste-3 by fusion proteins. Reactions were run in 10 ml of 100 mM Potassium phosphate buffer pH 8 with the MPW-3 (10 mg / ml) . Reactions started by adding 0.5 µM fusion proteins variants as well as LCCWCCGand incubated at 60°C, 500 rpm, for 96 h, samples were collected at different time intervals for HPLC analysis. The reactions were run in triplicates. Figure 16: Scaled enzymatic depolymerization of mixed plastic-3 waste using fusion protein indicating the released monomers, i.e., terephthalic acid (TPA), monohydroxyethyl terephthalate (MHET), Bis(2-Hydroxyethyl) terephthalate (BHET), throughout the reaction time. Reaction was done in INFORS HT bioreactor with 50 g / L of MPW-3 in 100 mM potassium phosphate buffer at pH 8. The reaction was initiated with the addition of 10 mg of the purified fusion protein of SEQ ID NO 18 and incubated at 60 °C and 200 rpm. Samples were collected at different time intervals and analysed with HPLC, based on the results batches of the fusion protein was added. Figure 17: Scaled up enzymatic depolymerization of MPW-3 using fusion protein with SEQ ID NO 22 showing the released monomer (TPA) and short oligomers (MHET, BHET) throughout the reaction time. Reaction was run in the same pattern as in Figure 16. Figure 18: Depolymerization of different polyesters using fusion proteins. Monomers detected by HPLC analysis using C18 or organic acid column from (A) polycaprolactone (monomer detected: 6,hydroxyhexanoic acid), B) polybutylene adipate terephthalate (PBAT) (monomer detected: terephthalic acid), (C) polytrimethylene terephthalate (PTT) (monomer detected: terephthalic acid), (D) polyethylene furan-2,5-dicarboxylate (PEF) (monomer detected: 2,5-furandicarboxylic acid), and (E) polybutylene terephthalate (PBT) (monomer detected: terephthalic acid). Figure 19: HPLC chromatogram for different time intervals from for the scaled up depolymerization reaction of MPW-3 showing TPA, (MHET, and BHET). Figure 20:1H-NMR spectrum of the recovered and purified TPA obtained from the scaled depolymerization of the mixed plastic waste-3. Figure 21: Total released monomers (µg / ml) from PET for screening of fusion proteins further comprising polymer binding domains in 96 well plate. PET microparticles (semi- crystalline PET powder, Goodfellow Cambridge Ltd, Cat. No. ES306000) 10 mg / ml were resuspended in 100 mM potassium phosphate buffer (pH 8). 200 µl of the resuspended PET microparticles were mixed with 100 µl of clarified cell lysate and incubated at 60 °C, 450 rpm for 7 hours. The supernatant was then analyzed for PET degradation. As a negative control, pET28a(+) empty vector transformed into E. coli BL 21(DE3) was grown, lysed and analyzed under the same conditions. For positive control, the LCCWCCGvariant was cloned and expressed and tested under the same conditions (well no. H12). A1-H11 represents the positions of different fusion proteins within a 96-well plate. Figure 22: Released TPA and MHET (mg / ml) from the screening of different fusion protein variants comprising polymer binding domains in equimolar concentrations (0.5 µM) against Goodfellow semicrystalline PET microparticles. Reactions were performed on the 96 deep- well plate at 60 °C and 300 rpm for 24 hours. Samples were collected and analyzed by HPLC for quantification of the released monomers. Figure 23: SDS-PAGE image of selected purified fusion proteins comprising polymer binding domains. Clarified cell lysates of the corresponding variants were purified with IMAC purification method and the eluted fractions were run on 12 % SDS-PAGE gel. Figure 24: Total released monomers from the refined selection of the fusion proteins comprising polymer binding domains after initial screening. Fusion protein variants (0.5 µM) were incubated with 10 mg / ml semicrystalline PET microparticles from GoodFellow (300 µm) at 60 °C, samples were taken at different time points (24 and 48 hours) and the released monomers were analyzed by HPLC. Figure 25: Total released monomers from the refined selection of the fusion proteins comprising polymer binding domain variants against polycotton samples. Fusion protein variants (0.5 µM) were incubated with polycotton samples at 60 °C, samples were taken at different time points (24, 48, and 168 hours), and the released monomers were analyzed by HPLC. Figure 26: TPA, MHET and BHET (mg / ml) released from post-industrial and post- consumer PET samples after treatment with; (A) fusion protein of SEQ ID NO: 18 and (B) fusion protein of SEQ ID NO: 134. Depolymerization reactions were performed with 1 mM chimeric enzymes against 10-15 mg / ml of plastic samples without prior treatment in 100 mM potassium phosphate buffer pH 8, 60 °C, 500 rpm. Samples were collected at different time intervals (24, 48 and 96 h) and analyzed by HPLC. Figure 27: Released monomers (mg / ml) from PET for screening of fusion proteins comprising the serine hydrolases of SEQ ID NO: 14 and 2 with different linkers and swapped serine hydrolases. PET microparticles (Amorphous) 5 mg / ml were resuspended in 50 mM Bicine buffer (pH 9). 0.5 µM enzymes were incubated with amorphous PET microparticle (5 mg / ml) in 1 ml reaction volume for 24 hours, 500 rpm at 50 °C. The supernatant was then analyzed for PET degradation. As a negative control, pET28a(+) empty vector transformed into E. coli BL 21(DE3) was grown, lysed and analyzed under the same conditions. Figure 28: Released monomers (mg / ml) from PET for screening of fusion proteins comprising the serine hydrolases of SEQ ID NO: 12 and 11 with different linkers and swapped serine hydrolases. PET microparticles (Amorphous) 5 mg / ml were resuspended in 50 mM Bicine buffer (pH 9). 0.5 µM enzymes were incubated with amorphous PET microparticle (5 mg / ml) in 1 ml reaction volume for 24 hours, 500 rpm at 60 °C. The supernatant was then analyzed for PET degradation. As a negative control, pET28a(+) empty vector transformed into E. coli BL 21(DE3) was grown, lysed and analysed under the same conditions. For positive control, fusion enzyme with SEQ ID NO. 22 was cloned and expressed and tested under the same conditions. (A) Aligned HPLC chromatograms showing only fusion enzyme with SEQ ID NO 22 having peaks corresponding to TPA, MHET, and BHET. (B) and (C) analysis of HPLC runs where a drastic effect was noticed with changing the linker or swapping the position of the enzyme singlet units.

[0002] REFERENCES 1. Tiseo I. Global plastic production 1950–2020. Statista, September. 2021;20. 2. Britt PF, Coates GW, Winey KI, Byers J, Chen E, Coughlin B, et al. Report of the Basic Energy Sciences Roundtable on Chemical Upcycling of Polymers. USDOE Office of Science (SC)(United States); 2019. 3. Agenda I, editor The new plastics economy rethinking the future of plastics. The World Economic Forum: Geneva, Switzerland; 2016. 4. Schiffer H-W. WEC energy policy scenarios to 2050. Energy policy. 2008;36(7):2464-70. 5. Geyer R, Jambeck JR, Law KL. Production, use, and fate of all plastics ever made. Sci Adv. 2017;3(7). 6. Zurier HS, Goddard JM. A high-throughput expression and screening platform for applications-driven PETase engineering. Biotechnol Bioeng. 2023;120(4):1000-14. 7. Seeley ME, Song B, Passie R, Hale RC. Microplastics affect sedimentary microbial communities and nitrogen cycling. Nat Commun. 2020;11(1). 8. MacLeo M, Arp HPH, Tekman MB, Jahnke A. 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Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, et al. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020;580(7802):216. EXAMPLES Example 1 Materials and methods DNA manipulation Nucleotide sequence of different PETases, cutinases, esterases and lipases were codon optimized for expression in E. coli host, synthesized and cloned as reported earlier in Tournier et al. (15). The nucleotide sequences were inserted between NcoI and XhoI restriction sites of the expression vector pET28a(+) and ligated with T4 DNA ligase. The ligation mixture was transformed into E. coli BL21(DE3) and these were plated on LB agar plates supplemented with 50 µg / mL kanamycin and grown overnight at 37 °C. Small scale parallel expression and lysate preparation Colonies were picked form the agar plates and used to inoculate 500 µl of LB medium supplemented with 50 µg / mL kanamycin and incubated at 37oC, 1000 rpm on a thermoplate shaker for 6 hrs. 50 microliters of the deep well plate inoculate were used to inoculate 500µl of the expression medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α- lactose) supplemented with 100 µg / mL kanamycin, in deep well plates. The expression plates were incubated 37oC, 1000 rpm for 5 hours, and then the temperature was decreased to 16oC for 48 hours. The expression was terminated by harvesting the plate (3200g, 30 min, 20°C, Sigma 3-16PK, Sigma Laborzentrifugen GmbH, Osterode am Harz, Germany). Cells were lysed by BugBuster® protein extraction reagent (Millipore Sigma, Burlington, MA, USA), soluble proteins were then clarified (3200g, 60 min, 4°C, Sigma 3-16PK, Germany) and stored at 4oC for PET degradation activity screening. Enzyme (fusion proteins) variants Various fusion proteins consisting of two serine hydrolase domains as presented in Table A and at least one polypeptide linker as presented in Table D(i) were generated and further screened for PET degradation activity (Example 2). Screening for PET degradation activity PET microparticles (semi-crystalline PET powder, Goodfellow Cambridge Ltd, Cat. No. ES306000) 10 mg / ml were washed twice with 30 ml of 50 mM Bicine buffer (pH 9.0) and resuspended in the same buffer. 200 µl of the resuspended PET microparticles were mixed with 100 µl of the clarified cell lysate in 96 deep well plate covered with adhesive aluminium foil and incubated at 50oC, 450 rpm for 7 hours. The plate was centrifuged (3200g, 30 min, 20°C) and the supernatant was further analyzed for PET degradation. For negative control, pET28a (+) empty vector transformed into E. coli BL 21 (DE3) grown, lysed and analyzed under the same conditions. For positive control, LCCWCCG variant was cloned and expressed and tested under the same conditions. PET degradation was measured by determining the concentration of the PET degradation monomers (Terephthalic acid (TPA), Ethylene glycol, Mono-(2-hydroxyethyl)terephthalic acid (MHET) and Bis(2-Hydroxyethyl) terephthalate (BHET)). Specifically, the monomers released from the hydrolysis of plastic polymers (including PET, PBAT, PLA, PCL, and PEF) were quantified using HPLC (JASCO, Tokyo, Japan) equipped with refractive index detector (ERC, Kawaguchi, Japan), JASCO UV detector at 260 and 280 nm, and a JASCO intelligent autosampler. TPA, MHET and BHET were analyzed on a C18 column using 20 % acetonitrile with 0.02 % formic acid as mobile phase at 0.6 mL / min. Aminex HPX-87H column connected to a guard column (BioRad, Richmond, CA, USA) was employed for the separation of adipic acid (AA), lactic acid (LA), 6-hydroxyhexanoic acid (6-HHA), ethylene glycol (EG), 2,5-furandicarboxylic acid (FDCA), and 1,4-butanediol (1,4-BDO) using 0.05 % H2SO4as mobile phase at flow rate of 0.6 mL / min. The column temperature was maintained at 40 °C (C18) and 65 °C (Aminex) in a chromatographic oven (Shimadzu, Tokyo, Japan). Samples were prepared by diluting in DMSO for TPA, BHET and MHET, or acidified milliQ for other monomers analysis. The structure of TPA separated from the depolymerization was confirmed by1H-NMR (DMSO-d6) using 400 MHz NMR (Bruker, UltraShield Plus 400, Germany). Results The fusion proteins were screened for PET degradation by measuring the release of TPA, MHET and BHET monomers after the 7 hours reaction as described above (Figure 1). Fusion proteins that released monomers higher or comparable to those released by LCCWCCG (40 µg / ml) were considered as positive hits and selected for further characterization. Of the 95 fusion proteins in the library, 20 fusion proteins were considered as hits and studied further. 7 of the hits were removed for lack of reproducibility or efficient heterologous expression in E.coli. The remaining 13 hit fusion proteins are described in Table D(i). Example 2 Materials and methods Scaled production and purification fusion proteins For scaled enzyme production, glycerol stock of the recombinant E. coli BL21(DE3) cells harbouring the active fusion protein plasmids were first inoculated into 25 mL of LB medium supplemented with 50 µg / mL kanamycin in 250 mL sterile Erlenmeyer flask and grown overnight at 37°C, 200 rpm. The cultures were then inoculated into 300 mL of auto- induction medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α-lactose) supplemented with 100 µg / mL kanamycin, in 1 L Erlenmeyer flask to an OD600nm of 0.1. The cultures were incubated at 37 °C, 200 rpm for 5 h, and then at 16 °C for 24 h prior to harvesting by centrifugation at 6000 rpm, 4 °C for 20 min (Sorvall Lynx 4000 centrifuge, Thermo Scientific, Waltham, MA, USA). Active fusion proteins were purified from cell lysates by immobilized metal ion chromatography. The clarified lysate was subjected to immobilized metal ion affinity chromatography (IMAC) for purification using 5 mL HisTrap FFTMnickel column (GE Healthcare Bio-Sciences AB, Uppsala, Sweden). The clarified lysate was applied to the column pre-equilibrated with the binding buffer (50 mM Tris-HCl, 0.5 M NaCl, 20 mM imidazole, pH 8), the unbound proteins were washed out and finally the bound proteins were eluted with the elution buffer (50 mM Tris-HCl, 0.5 M NaCl, 0.5 M imidazole, pH 8). The eluted fractions were pooled together and dialyzed against dialysis buffer (100mM Potassium phosphate, 0.5 M NaCl, pH 8) overnight at 4oC. Protein concentration wasmeasured by nanodrop, and samples were kept at 4oC. Results Protein production and purification Unlike the expression and purification of monomeric / singlet enzymes, the fusion proteins showed better expression and activity compared to their constituent subunit enzymes under the mentioned method for protein production and purification (Figure 2). This allowed the scaling up of the fusion protein for testing under controlled conditions for mixed plastic waste depolymerization. A yield of 25-30 mg of pure fusion proteins can be obtained from a liter of E. coli cultivation representing 2.5-3 % yield of protein. Example 3 Screening and optimization of reaction conditions Materials and methods Screening for the optimum buffer and pH Fusion proteins with the highest PETase activity were screened for the optimum pH and buffers in 100 mM of Tris-HCl buffer pH 7 and 8, Potassium phosphate buffer pH 8 and Bicine buffer pH 9. Screening was performed by mixing 0.5 µM of fusion protein variants as well LCCWCCG variant with the semicrystalline Goodfellow PET microparticle (5 mg / ml) in 1 ml reaction volume at 60oC for 24 hours, 500 rpm (Hettich Benelux Digital Heating Thermomixer MHR) with corresponding controls. Screening was done in triplicates for each buffer with corresponding controls, the released monomers were quantified by HPLC. Screening for the optimum temperature The most active fusion proteins as well as LCCWCCGvariant were screened for the optimum reaction temperature 37, 50, 60 and 70oC in 100 mM potassium phosphate buffer pH 8, using the semicrystalline Goodfellow PET microparticle (5 mg / ml) in 1 ml reaction volume at for 24 hours, 500 rpm (Hettich Benelux Digital Heating Thermomixer MHR) with corresponding controls. Reactions were performed in triplicates for each temperature with corresponding controls, the degradation products were analysed by HPLC. Results Screening for optimal buffer and pH indicated that the fusion proteins are more active in phosphate buffer pH 8. Therefore, all the subsequent experiments were conducted in phosphate buffer pH 8 (Figure 3). The thermal stability of the fusion proteins was also examined and compared to LCCWCCG, where the reactions were run at 37, 50, 60, and 70 °C. The fusion proteins were found active at elevated temperatures in some cases such as fusion protein with SEQ ID NO 23, the activity was even increased at 70 °C, whereas the other fusion proteins were most active at 60 °C (Figure 4). While LCCWCCG enzyme lost more than 50% of its PETase activity at 70oC, most of the fusion proteins retained more than 60% of their PETase activity and even the fusion protein with SEQ ID NO 23 showed higher catalytic activity at 70oC. This finding shed the light on the enhanced thermal operational stability of the fusion proteins. Example 4 Materials and methods Determination of protein melting temperature (Tm) through thermal shift assay The melting temperature of the purified fusion proteins was determined as previously described. Briefly, the purified fusion proteins were mixed with SYPRO Orange dye, the final concentrations of protein and dye in the mixture were 5 µM and 2X, respectively. The protein-dye mixture was mixed thoroughly and incubated in CFX96 touch system (Bio-Rad) run with already established thermal shift assay protocol. Data were retrieved and analyzed with Bio-Rad CFX maestro to derivatize the melting curves and calculate the melting temperature (Tm) of the fusion proteins. The experiment was done in triplicate for each fusion protein. Results The melting curves for the purified fusion proteins indicated melting temperature (Tm) of 71.5 – 87 °C for the refined enzymes (Figure 5). Noteworthy, fusion protein with SEQ ID NO 22 is composed of two enzymes with a maximum Tm of 50 and 55 °C, yet the calculated Tm for this fusion protein increased to 76.5 °C (Figure 5). Moreover, the fusion protein was still active at 70 °C (Example 3, Figure 4). These results indicate that the combination and fusion of enzymes in a specific pattern can enhance their thermal stability and hence their operational activity. Example 5 Materials and methods Hydrolysis of PET particles with different degrees of crystallinities Crystalline PET microparticles (750 µm) and amorphous PET microparticles (750 µm) were obtained from AIMPLAS (Carrer de Valencia, Spain), while semicrystalline PET microparticles were ordered from Goodfellow (Goodfellow Cambridge Limited, LS548735 J O, ES306031 / 1, particle size 300 micron, semi-crystalline, crystallinity > 40 %). PET particles were washed twice with 100 mM Phosphate buffer (pH 8) and collected by centrifugation (3,392 x g, 4 °C for 10 min Sigma 3-16PK,) and resuspended in the same buffer at a concentration of 10 mg / ml. One millilitre of PET particles suspension (10 mg / ml) was mixed with 0.5 µM fusion proteins as well as LCCWCCG and incubated at 60oC, 500 rpm, for 48 h, samples were taken at different time intervals for HPLC analysis. PET particles resuspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Results Polyethylene terephthalate with different degrees of crystallinity (amorphous, semicrystalline, and crystalline) were tested against the fusion proteins and compared to LCCWCCG. The fusion proteins showed higher activities in All cases (amorphous, semicrystalline, and crystalline) compared to LCCWCCG. In the case of amorphous PET, LCCWCCG was inhibited after 24 hours of the reaction due to product inhibition whereas the fusion proteins were still active till 48 hours with no inhibition specially with fusion proteins of SEQ ID NO: 18 and 22 (Figure 6). With semicrystalline and crystalline material, the effect of inhibition was lower due to lower product release (LCCWCCG continued to function), however, in both cases fusion proteins of SEQ ID NO 18 and 22 (semicrystalline PET, Figure 7) and 22 (crystalline PET, Figure 8) showed higher activity compared to LCCWCCG. Example 6 Materials and methods Depolymerization of different polyesters Depolymerization of PCL, PBAT, PTT, PEF and PBT by a set of fusion proteins, the released monomers were analysed by HPLC using a C18 or organic acid column, as detailed above under Example 1. The concentration of the fusion proteins was constant (0.5 µM) in all reactions run in 100 mM potassium phosphate buffer at pH 8 at 60 °C, 200 rpm in 1 ml reaction volume. Hydrolysis of different polymers with different composition Polybutylene adipate terephthalate (PBAT), polybutylene terephthalate (PBT), polytrimethylene terephthalate (PTT), polycaprolactone (PCL) and polyethylene furan-2,5- dicarboxylate (PEF) were tested for depolymerization by the fusion proteins. The polymers particles were washed twice with 100 mM Phosphate buffer (pH 8) and collected by centrifugation (3,392 x g, 4 °C for 10 min Sigma 3-16PK,) and resuspended in the same buffer at a concentration of 10 mg / ml. One milliliter of the polymers´ particles suspension (10 mg / ml) was mixed with 0.5 µM fusion proteins variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were analyzed by HPLC. Polymer particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Results The refined active hits of the fusion proteins were found to be active on other polymers; however, with variant degree of activity. Polybutylene adipate terephthalate (PBAT), a biodegradable polyester used in mulch films and packaging with monomers of 1,4- butanediol, adipic acid, and terephthalic acid, was depolymerized by all tested fusion proteins, however, their activity was lower than LCCWCCG(Figure 9). Polybutylene terephthalate (PBT), a polymer with high mechanical strength and heat resistance of 150 °C, difficult to degrade, with a composition of 1,4-butanediol and terephthalic acid, only three fusion proteins (SEQ ID NO 16, 22, and 23) showed activity that is comparable to LCCWCCG, but the activity was low in all cases. (Figure 10). Polytrimethylene terephthalate (PTT), composed of 1,3-propanediol and terephthalic acid, currently used in carpets, showed low levels of depolymerization, nevertheless, two of the fusion proteins, (SEQ ID NO 22 and 16) showed higher or similar activity compared to LCCWCCG (Figure 11). Polycaprolactone (PCL), composed of 6-hydroxyhexanoic acid, a semicrystalline biodegradable polyester was hydrolyzed more efficiently by the fusion proteins compared to LCCWCCG, particularly enzymes with SEQ ID NO 16, 23, and 22 (Figure 12). Polyethylene Furanoate (PEF), a biobased substituent of PET, composed of ethylene glycol and 2,5- furandicarboxylic acid, was easily depolymerized by the fusion proteins and particularly SEQ ID NO 16 higher than that of LCCWCCG(Figure 13). Figure 18 shows the HPLC chromatogram for the detected monomer from each tested polyesters using the fusion proteins. Example 7 Materials and methods Hydrolysis of mixed plastic waste with different compositions Mixed plastic waste (MPW) materials with various compositions were tested for hydrolysis with fusion proteins. MPW particles were washed twice with 100 mM Phosphate buffer (pH 8) and collected by centrifugation (3,392 x g, 4 °C for 10 min Sigma 3-16PK,) and resuspended in the same buffer at a concentration of 10 mg / ml. One milliliter of the polymer particle suspension was mixed with 0.5 µM fusion protein variants as well as LCCWCCGand incubated at 60oC, 500 rpm, for 48 h, samples were collected at different time intervals for HPLC analysis. MPW particles suspended in the same buffer without enzymes served as a negative control, the experiment was done in triplicates. Code Composition MPW-1 29.62 % PET, 41.19 % PE, 9.37 % PP, 2.61 % PS MPW-2 90.8 % Hollow body [PET], 2.29 % Rings, 5.09 % Caps, 2.54 % labels MPW-3 87 % trays [PET], 12.56 film [PET, PE], <0.1 labels [PE, PET, PP, PA] Results Different MPW with different compositions of PET were tested for hydrolysis with the fusion protein variants and compared with LCCWCCG. In all cases the fusion proteins were able to degrade MPW samples with different ratios based on the percentage of PET and its properties (crystallinity percentage). MPW-3 was the most hydrolyzed sample, especially of SEQ ID 18 fusion protein at 1.5 times more depolymerization compared to LCCWCCG, followed by fusion protein variants of SEQ ID 24, 16, and 22 which all exceeded LCCWCCG. Similar pattern was observed for MPW-2, especially for fusion proteins SEQ ID NO 18 and 22. As expected, MPW-1 with lower PET composition showed lower depolymerization efficiency with all tested enzymes (Figure 14). Monitoring the depolymerization of MPW-3 by running the reaction for longer period (96 hours) showed an inhibition for LCCWCCG, whereas all the fusion proteins were still active. Fusion proteins of SEQ ID NO 18, 22, and 24 showed the highest activity against MPW-3 compared to LCCWCCGthroughout the reaction duration (Figure 15). Example 8 Materials and methods Stability and activity of fusion proteins for prolonged time As described in Example 1, the depolymerization of amorphous PET was tested for the active fusion proteins hits and compared to LCCWCCGat equimolar ratio. The reactions were followed at intervals by sampling and running HPLC on C18 column to detect TPA, MHET, and BHET. Results The results align with the previous reports on LCC variants, where the enzyme is inhibited after certain time due to the accumulation of the released products. With amorphous PET being easily depolymerized, the effect of product inhibition can be easily observed (Figure 6). After 24 hours of the reaction, LCCWCCG was completely inhibited and no depolymerization of amorphous PET could be detected. In contrast, all the fusion proteins continued catalyzing the depolymerization reaction without any noticeable product inhibition. The same observation was noted when running the reaction on MPW-3 (Example 7) where the reaction intervals over 96 hours indicated inhibition to LCCWCCGwhich was not the case for the fusion proteins that continued to function throughout the reaction time (SEQ ID NO 18, 22, and 24; Figure 15). Neither exchanging the buffer nor adding new batches of fresh enzymes were needed, which has been required previously to mitigate the inhibitory effect of the released products. Example 9 Materials and methods Large scale Depolymerization of mixed plastic waste Fifty grams of mixed plastic waste-3 were resuspended in 500 ml of 100 mM potassium phosphate buffer at pH 8 in INFORS HT bioreactor. The reaction was initiated by adding 10 mg of the purified fusion protein variants and incubated at 60°C and 200 rpm. Samples were collected intermittently at different time points to monitor the depolymerization process and release of the monomers. Concomitantly, fresh patches of pure enzyme were added. The reaction pH was maintained at 8 using 5 N NaOH and 2 M H3PO4. The reaction was allowed to continue till complete degradation was achieved. The reaction was monitored visually through disintegration of the waste flakes, and by HPLC to determine the concentration of the released monomers. Samples were analysed by HPLC using a C18 column. The hydrolysate containing TPA and EG obtained from MPW-3 depolymerization was used for TPA separation. First, the solution pH was increased to pH 11 to completely solubilize all monomers, followed by centrifugation to separate the solubilized monomers from the unhydrolyzed waste. Later, the supernatant was subjected to gradual acidification to pH 3.4-2.5 with concentrated acid solutions, TPA was completely precipitated out from the solution and filtered. The entire purification process was monitored by HPLC. TPA pelletwas dried, and its purity was analyzed and confirmed by 1H-NMR.Results The depolymerization of mixed plastic waste was conducted as previously described. The macro-shredded waste (1-2 cm) was resuspended in 100 mM potassium phosphate buffer pH 8 with a concentration of 100 g / L in INFORS 2L bioreactor with a pH and temperature control units. The pH was adjusted using 2 M NaOH and the reaction was initiated by the addition of the fusion protein. Figure 16 shows the depolymerization reaction using fusion protein (SEQ ID NO 18). Another reaction was also performed following the same procedure using LCCWCCGto compare with our developed fusion proteins. In case of LCCWCCG and fusion proteins SEQ ID NO 18, a weight loss of 73.5 % and 78 % was achieved, respectively. Moreover, the concentration of the fusion protein used in the reaction was 1.3 times lower than LCCWCCG. The final recovered yield of TPA from the depolymerized mixed plastic waste using the fusion protein was 1.24 times higher thanthat from LCCWCCG.Another fusion protein with lower activity but improved thermal stability (SEQ ID NO 22) compared to its monomeric constituents was used for the degradation of MPW-3. The same degradation pattern was attained using 1.3 times lower enzyme concentration and a final weight loss of 75.6 % was achieved with a recovered TPA of 73.6 g / L representing 1,015 time increase over that achieved by LCCWCCG (Figure 17). An example showing the HPLC chromatogram (Figure 19) for the different times taken throughout the reaction, indicating the type of compounds that can be separated by C18 column and detected by HPLC. The chromatogram indicates the increase in TPA with the decrease in the MHET and BHET. The reactions were finally processed for the separation and purification of the constituent monomers from the depolymerization of MPW-3. Figure 20 indicate the proton NMR for the recovered TPA with high purity. Example 10 Materials and Methods Preparation of fusion proteins comprising polymer binding domains (PBD-fusion chimeric proteins) Fusion proteins as described above under Example 1 were further engineered to comprise a polymer binding domain selected from Table B. Nucleotide sequences of different polymer binding domains were codon optimized for expression in E. coli host, synthesized and cloned as reported earlier. The nucleotide sequences were inserted downstream of the hydrolase domains and ligated with T4 DNA ligase. The ligation mixture was transformed into E. coli BL21(DE3) expression host, and were plated on LB agar plates supplemented with 50 µg / mL kanamycin as a selection marker and grown overnight at 37 °C. Screening Small-scale parallel expressions, lysate preparation, and screening for PET degradation activity were performed as described in Example 1 with slight modifications. PET microparticles (semi-crystalline PET powder, Goodfellow Cambridge Ltd, Cat. No. ES306000) 10 mg / ml were resuspended in 100 mM potassium phosphate buffer (pH 8.0). 200 µl of the resuspended PET microparticles were mixed with 100 µl of the clarified cell lysate of PBD-fusion chimeric proteins in 96 deep well plate covered with adhesive aluminium foil and incubated at 60 °C, 450 rpm for 24 hours. The plate was centrifuged (3200 g, 30 min, 20°C) and the supernatant was further analyzed for PET degradation. For negative control, pET28a (+) empty vector transformed into E. coli BL 21 (DE3) was grown, lysed and analyzed under the same conditions. For positive control, LCCWCCG variant was cloned, expressed and tested under the same conditions. Results Fusion proteins comprising a polymer binding domain (PBD-fusion chimeric proteins) were screened for PET degradation by measuring the release of TPA, MHET, and BHET monomers after a 24-hour reaction, as described above (Figure 21). PBD-Fusion chimeric proteins that released monomers equivalent to or higher than LCCWCCG (40 µg / mL) were considered positive hits and selected for further characterization (Figure 22). From a library of 768 PBD-fusion chimeric protein variants, 53 were identified as potential hits. Of these, 16 clones were retrieved after secondary screening to ensure reproducibility and efficient heterologous expression in E. coli. The selected PBD-fusion chimeric protein hits are listed in Table D(ii). Example 11 Materials and Methods Lab scale production and purification of selected most active PBD-fusion chimeric proteins As detailed in Example 2, glycerol stocks of the recombinant E. coli BL21(DE3) cells harbouring plasmids expressing active PBD-fusion chimeric proteins were first inoculated into 25 mL of LB medium supplemented with 50 µg / mL kanamycin in 250 mL sterile Erlenmeyer flask and grown overnight at 37 °C, 200 rpm. The cultures were then inoculated into 300 mL of auto-induction medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α-lactose) supplemented with 100 µg / mL kanamycin, in 1 L Erlenmeyer flask to an OD600nmof 0.1. The cultures were incubated at 37 °C, 200 rpm for 5 h, and then at 16 °C for 24 h prior to harvesting by centrifugation at 6000 rpm, 4 °C for 20 min (Sorvall Lynx 4000 centrifuge, Thermo Scientific, Waltham, MA, USA). The cell pellets were sonicated and the clarified lysate was subjected to immobilized metal ion affinity chromatography (IMAC) for purification using 5 mL HisTrap FFTMnickel column (GE Healthcare Bio-Sciences AB, Uppsala, Sweden). The clarified lysate was applied to the column pre-equilibrated with the binding buffer (50 mM Tris-HCl, 0.5 M NaCl, 20 mM imidazole, pH 8), the unbound proteins were washed out and finally the bound proteins were eluted with the elution buffer (50 mM Tris-HCl, 0.5 M NaCl, 0.5 M imidazole, pH 8). The eluted fractions were pooled together and dialyzed against dialysis buffer (100 mM Potassium phosphate, 0.5 M NaCl, pH 8) overnight at 4oC. Protein concentration was measured by nanodrop, and samples were kept at 4oC. Results The PBD-fusion proteins showed good expression similar to the previously described chimeric enzymes in Example 2 under the mentioned method for protein production and purification (Figure 23). A yield of 25-30 mg of pure PBD-fusion proteins can be obtained from a litre of E. coli cultivation representing 2.5-3 % yield of protein. The high yield of soluble pure PBD-fusion proteins allowed for screening of hydrolysis of different PET samples. Example 12 Materials and Methods Hydrolysis of different forms of PET PET degradation reactions were performed as described in Example 5, using semicrystalline PET microparticles (300 µm) and polycotton fabric samples containing 50% PET. Reactions were sampled at different time intervals, and the released monomers were quantified by HPLC analysis. Results PET samples in different forms and degrees of crystallinity (semicrystalline microparticles, and polycotton fibers mixtures) were tested against the refined PBD-fusion chimeric proteins and compared to LCCWCCG. PBD-fusion chimeric proteins, in particular those of SEQ ID NO: 134 exhibited higher activity against semicrystalline PET samples, while those of SEQ ID NO: 133, and 134 exhibited higher activity against polycotton samples under the specified reaction conditions after 48 and 168 hours (Figures 24 and 25). The fusion protein of SEQ ID NO: 134 showed almost 3-fold activity after 48 hours (total released monomers ~ 0.6 mg / ml), compared to LCCWCCG which showed only one-fold increase in the activity after the same period of time (total released monomers ~ 0.3 mg / ml) against semicrystalline PET. Similar results were obtained for polycotton. Example 13 Materials and Methods Activity of selected purified fusion proteins against post-industrial and post-consumer PET fractions Reactions were conducted as described in Example 5, with post-industrial and post- consumer PET obtained from plastic sorting facilities and manufacturers. The PET samples included PET-G, PET / PE-colored blends, and PET originated from trays were supplied by Vanden Recycling UK, recycled PET-milky and clear were supplied by Scanfill Sweden, PET / PE-clear from Remondis Sweden AB, and post-industrial PET-packaging from INP Packaging AB. Reactions were performed with 10-15 mg / mL of plastic materials without pretreatment and initiated by the addition of 0.5 µM of the fusion proteins of SEQ ID NO: 18 and SEQ ID NO: 134, (Figure 26 A and B, respectively). Enzymatic activity was monitored over a 96-hour period by HPLC, quantifying the release of TPA, MHET, and BHET. Results Among the tested substrates, PET / PE blends, particularly the colored samples, showed the highest depolymerization rates (Figure 26 A, B). Both chimeric enzymes retained activity throughout the 96-hour reaction period across all PET fractions, with no evidence of product inhibition, despite the accumulation of 2.5–5.5 mg / mL of released monomers. Consistent with earlier observations in Example 5, where the reference enzyme LCCWCCGexhibited the pattern of product inhibition under the same conditions against amorphous PET, where such elevated monomer concentrations resulted in loss of activity, in contrast to the chimeric enzymes (with and without PBD) which retained robust performance. Example 14 Materials and methods Construct generation Nucleotide sequence encoding the PETase of SEQ ID NO: 14 and cutinase of SEQ ID NO: 2, (which are also comprised in the fusion protein of SEQ ID NO: 26) were engineered to be linked through one of the polypeptide linkers of SEQ ID NO: 60, 62, 69, 70, or 66. Additionally, the position of the individual serine hydrolases was swapped from that present in SEQ ID NO: 26 and linked using the linker of SEQ ID NO: 69. The resulting fusion proteins are shown in the Table below (linkers are highlighted in bold): SEQ Clone Sequence ID NO: MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHY PTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQI EAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAP WNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCA 26- NGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYAGAG 171 L60 AGNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAIS PGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVR SRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGA DLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDN DTRYTQFLCPGPRDGLFGEVEEYRSTCPFGS MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHY PTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQI EAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAP WNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCA 26- NGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYGAGA 172 L62 GAGAGAGAGANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPREN NTYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHM INRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSV TVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAW LKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPFGS 26- MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHY 173 L69 PTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQI EAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAP WNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCA NGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYVFNQR KEHKGYMLANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENN TYGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMI NRASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSV TVPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAW LKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPFGS MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHY PTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQI EAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAP WNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCA 26- NGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYPAVPP 174 L70 PANPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNTYGAVAIS PGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMINRASSTVR SRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVTVPTLIIGA DLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDN DTRYTQFLCPGPRDGLFGEVEEYRSTCPFGS MNPPGGDPDPGCQTDCNYQRGPDPTDAYLEAASGPYTVSTIRVSSLVPGFGGGTIHY PTNAGGGKMAGIVVIPGYLSFESSIEWWGPRLASHGFVVMTIDTNTIYDQPSQRRDQI EAALQYLVNQSNSSSSPISGMVDSSRLAAVGWSMGGGGTLQLAADGGIKAAIALAP WNSSINDFNRIQVPTLIFACQLDAIAPVALHASPFYNRIPNTTPKAFFEMTGGDHWCA 26- NGGNIYSALLGKYGVSWMKLHLDQDTRYAPFLCGPNHAAQTLISEYRGNCPYEAAAK 175 L66 EAAKEAAKNPYERGPNPTDALLEASSGPFSVSEENVSRLSASGFGGGTIYYPRENNT YGAVAISPGYTGTEASIAWLGERIASHGFVVITIDTITTLDQPDSRAEQLNAALNHMIN RASSTVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVT VPTLIIGADLDTIAPVATHAKPFYNSLPSSISKAYLELDGATHFAPNIPNKIIGKYSVAWL KRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPFGS Similarly, the nucleotide sequence encoding the PETase of SEQ ID NO: 12 and esterase / cutinase of SEQ ID NO: 11 (which are also comprised in the fusion protein of SEQ ID NO: 22) were engineered to be linked through one of the polypeptide linkers of SEQ ID NO: 60, 62, 69, 70, or 66. Additionally, the position of the individual serine hydrolases was swapped from that present in SEQ ID NO: 22 and linked using the linker of SEQ ID NO: 70. The resulting fusion proteins are shown in the Table below (linkers are highlighted in bold): SEQ Clone Sequence ID NO: MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVP GYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSS SPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPT LIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVA 22- WMKRFMDNDTRYSTFACENPNSTAVSDFRTANCSPAVPPPANPYERGPNPTNSSIE 176 L70 ALRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTGTQSSISWLGERL ASHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSSRLAAMGHS MGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIASVRSHSEPF YNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYTQFLCPGPSTG WGSDVEEYRSTCPF MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVP GYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSS SPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPT LIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVA 22- WMKRFMDNDTRYSTFACENPNSTAVSDFRTANCSAGAGAGNPYERGPNPTNSSIEA 177 L60 LRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTGTQSSISWLGERLA SHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSSRLAAMGHSM GGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIASVRSHSEPFY NSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYTQFLCPGPSTG WGSDVEEYRSTCPF MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVP GYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSS SPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPT LIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVA 22- WMKRFMDNDTRYSTFACENPNSTAVSDFRTANCSGAGAGAGAGAGAGANPYERG 178 L62 PNPTNSSIEALRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTGTQS SISWLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSS RLAAMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIA SVRSHSEPFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYT QFLCPGPSTGWGSDVEEYRSTCPF MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVP 22- GYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSS 179 L69 SPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPT LIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVA WMKRFMDNDTRYSTFACENPNSTAVSDFRTANCSVFNQRKEHKGYMLANPYERG PNPTNSSIEALRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTGTQS SISWLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSS RLAAMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIA SVRSHSEPFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYT QFLCPGPSTGWGSDVEEYRSTCPF MTNPYARGPNPTAASLEASAGPFTVRSFTVSRPSGYGAGTVYYPTNAGGTVGAIAIVP GYTARQSSIKWWGPRLASHGFVVITIDTNSTLDQPESRSSQQMAALRQVASLNGTSS SPIYGKVDTARMGVMGWSMGGGGSLISAANNPSLKAAAPQAPWHSSTNFSSVTVPT LIFACENDSIAPVNSSALPIYDSMSRNAKQFLEINGGSHSCANSGNSNQALIGKKGVA 22- WMKRFMDNDTRYSTFACENPNSTAVSDFRTANCSEAAAKEAAKEAAKNPYERGPN 180 L66 PTNSSIEALRGPFRVDEERVSRLQARGFGGGTIYYPTDNNTFGAVAISPGYTGTQSSIS WLGERLASHGFVVMTIDTNTTLDQPDSRASQLDAALDYMVEDSSYSVRNRIDSSRLA AMGHSMGGGGTLRLAERRPDLQAAIPLTPWHTDKTWGSVRVPTLIIGAENDTIASVR SHSEPFYNSLPGSLDKAYLELDGASHFAPNLSNTTIAKYSISWLKRFVDDDTRYTQFLC PGPSTGWGSDVEEYRSTCPF The respective clones were transformed into E. coli BL21(DE3), expressed, purified as described in Examples 1 and 2. Screening for PET degradation activity Amorphous PET microparticles 5 mg / ml were washed twice with 30 ml of 50 mM Bicine buffer (pH 9.0) and resuspended in the same buffer. One ml of the resuspended PET microparticles were mixed with 0.5 µM of the purified enzymes at 50°C, 450 rpm for 24 hours. For negative control, pET28a (+) empty vector transformed into E. coli BL 21 (DE3) grown, lysed and analyzed under the same conditions. For positive control, the fusion of SEQ ID NO: 26 was tested under the same conditions. PET degradation was measured by determining the concentration of the PET degradation monomers (Terephthalic acid (TPA), Ethylene glycol, Mono-(2-hydroxyethyl)terephthalic acid (MHET) and Bis(2-Hydroxyethyl) terephthalate (BHET)) after 24h. The monomers released from the hydrolysis of PET polymer were quantified using HPLC (JASCO, Tokyo, Japan) equipped with refractive index detector (ERC, Kawaguchi, Japan), JASCO UV detector at 260 and 280 nm, and a JASCO intelligent autosampler same as in Example 1. Results The fusion proteins with different linkers and swapped position were screened for PET degradation by measuring the release of TPA, MHET and BHET monomers after the 24 hours reaction. From the screening of the different fusion proteins, the sequence with linker SEQ ID NO: 69 (L-69; SEQ ID NO: 173) showed the highest activity compared to the fusion enzymes with other linkers. Furthermore, when swapping the position of the individual serine hydrolase, i.e., PETase in position 3 and cutinase in position 1 maintaining the linker of SEQ ID NO: 69, the activity of the fusion enzyme dropped by 4 folds (Figure 27). The corresponding experiment using the serine hydrolases of fusion enzyme of SEQ ID NO: 12 and 11 showed similar results (Figure 28).

Claims

CLAIMS 1. A fusion protein capable of degrading a plastic polymer, wherein the fusion protein comprises two or more serine hydrolase domains coupled by a linker comprising: (i) an (EAAAK)n motif wherein n is an integer greater than or equal to 2; or (ii) an amino acid sequence according to any one of SEQ ID NO: 69, 59, 60, 62, 66, or 70.

2. The fusion protein of claim 1, wherein the fusion protein is catalytically active after at least 72 hours at a temperature of at least 60°C, optionally wherein the fusion protein is catalytically active after at least 96 hours at a temperature of at least 60°C 3. The fusion protein of claim 1 or 2, further comprising one or more polymer binding domain(s).

4. The fusion protein of any of the preceding claims, wherein all serine hydrolase domains are catalytically active.

5. The fusion protein of any of the preceding claims comprising two serine hydrolase domains.

6. The fusion protein of any of the preceding claims, wherein at least one serine hydrolase domain is an esterase, a lipase or a protease, or a catalytically active portion thereof.

7. The fusion protein of claim 6, wherein at least one esterase is selected from the group consisting of a PETase, a MHETase, and a cutinase, or a catalytically active portion thereof.

8. The fusion protein of any of the preceding claims, wherein at least one serine hydrolase domain comprises a cutinase or a PETase, or a catalytically active portion thereof.

9. The fusion protein of claim 6, wherein at least one protease is proteinase K, or a catalytically active portion thereof.

10. The fusion protein of any one of claims 6 or 7, wherein at least one cutinase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 1, 2, 3, 4, 5, 6, 7, 8 or 11.

11. The fusion protein of claims 7 or 8, wherein at least one PETase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 12, 13 or 14, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 12, 13 or 14.

12. The fusion protein of claim 6, wherein at least one lipase comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 9 or 10, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 9 or 10.

13. The fusion protein of any of the preceding claims, wherein the amino acid sequence of two or more serine hydrolase domains is the same.

14. The fusion protein of the preceding claims, wherein the amino acid sequences of at least two serine hydrolase domains comprise no more than about 95% sequence identity, such as no more than about 90%, 85%, 80%, 75%, 70%, 65%, 60%, 55% or 50% sequence identity.

15. The fusion protein of claim 2-14, wherein the one or more polymer binding domains are selected from the group consisting of a hydrophobin, a cellulose binding domain, a carbohydrate binding module, an anchor peptide, an anchor linker peptide, PET binding domain and PHA binding domains.

16. The fusion protein of any one of claims 2-15, wherein the one or more polymer binding domains are capable of binding one or more plastic polymer(s), optionally wherein the one or more plastic polymer(s) are selected from the group consisting of PET, PTT, PBT, PEF, PLA, PCL, PBAT and MHET.

17. The fusion protein of any one of claims 2-16, wherein the one or more polymer binding domain comprises or consists of an amino acid sequence selected from any one of SEQ ID NO: 85-96 and / or SEQ ID NO: 112-121, a variant, fragment or derivative thereof, or an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: SEQ ID NO: 85-96 and / or SEQ ID NO: 112-121.

18. The fusion protein of any of the preceding claims, wherein at least one serine hydrolase domain and at least one polymer binding domain are coupled by a linker.

19. The fusion protein of any of the preceding claims, wherein at least one linker is a polypeptide linker.

20. The fusion protein of claim 19, wherein the linker is selected from the group consisting of a polyglycine linker, a polyalanine linker, an alanine-glycine linker, a glycine-serine linker, a histidine linker, threonine-serine linker, a glutamine linker, an asparagine linker.

21. The fusion protein of claim 19, wherein the linker comprises the polypeptide sequence of any one of SEQ ID NO: 57-70.

22. The fusion protein of any one of claims 18-21, wherein the fusion protein has increased or improved stability and / or expression capabilities.

23. The fusion protein of claim 22, wherein the improved stability and / or expression capabilities are improved compared to a fusion protein without a linker and / or comprising a flexible linker.

24. The fusion protein of any one of claims 19-23, wherein the linker comprises between about 4 to about 20 amino acids, such as between about 5 to about 18 amino acids, about 6 to about 16 amino acids, about 7 to about 16 amino acids, about 8 to about 14 amino acids or about 10 to about 12 amino acids.

25. The fusion protein of any one of claims 18-24, wherein the linker is coupled to the C-terminal end of the first serine hydrolase domain and to the N-terminal end of the second serine hydrolase domain.

26. The fusion protein of any of the preceding claims, comprising an amino acid having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149 or 150.

27. The fusion protein of claim 26, comprising or consisting of the amino acid sequence of any of SEQ ID NO: 173, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 132, 133, 134, 135, 136, 137, 138, 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149 or 150, or a variant, fragment or derivative thereof.

28. The fusion protein of any of the preceding claims, wherein the fusion protein has increased or improved thermal stability.

29. The fusion protein of claim 28, wherein the fusion protein has increased or improved thermal stability compared to each constituent serine hydrolase domain separately.

30. The fusion protein of any of the preceding claims, wherein the fusion protein has increased or improved plastic polymer degradation activity.

31. The fusion protein of claim 30, wherein the fusion protein has increased or improved degradation activity of at least one plastic polymer selected from the group consisting of PET, PTT, PBT, PEF, PLA, PCL, PBAT, MHET, blends or combinations thereof, and mixed plastic waste.

32. The fusion protein of claims 30 or 31, wherein the fusion protein has increased or improved plastic polymer degradation compared to each constituent serine hydrolase domain separately.

33. The fusion protein of any one of claims 30–32, wherein the fusion protein has similar, equal, increased or improved plastic polymer degradation compared to LCC, or a variant or derivative thereof.

34. The fusion protein of any one of claim 30-33, wherein the fusion protein has increased or improved plastic polymer degradation activity when one or more of the plastic polymers has not been subject to pre-treatment.

35. The fusion protein of claim 34, wherein the pre-treatment comprises at least one step selected from the group consisting of an enzymatic treatment, a mechanical treatment, a chemical treatment and heat treatment.

36. The fusion protein of claim 35, wherein the mechanical treatment comprises one or more of grinding, milling, extrusion and / or spinning.

37. The fusion protein of claim 35, wherein the chemical treatment comprises one or more of pyrolysis, gasification and / or hydro-cracking.

38. The fusion protein of any of the preceding claims, wherein the fusion protein is catalytically active after at least 12 hours, such as after at least 16 hours, at least 20 hours, at least 24 hours, at least 28 hours, at least 32 hours, at least 36 hours, at least 40 hours, at least 44 hours, at least 48 hours, at least 54 hours, at least 60 hours, at least 66 hours, at least 72 hours, at least 78 hours, at least 84 hours, at least 90 hours, at least 96 hours, at least 120 hours, at least 144 hours, at least 168 hours, at least 192 hours, at least 216 hours, at least 240 hours, at least 264 hours, at least 288 hours, at least 312 hours, at least 336 hours, at least 360 hours, at least 384 hours, at least 408 hours, at least 432 hours, at least 456 hours, at least 480 hours, at least 504 hours, at least 528 hours, at least 552 hours, at least 576 hours, at least 600 hours, at least 624 hours, at least 648 hours, or at least 672 hours at a temperature of at least 37°C.

39. The fusion protein of claim 38, wherein the temperature is at least 40°C, such as at least 45°C, at least 50°C, at least 55°C, at least 60°C, at least 65°C, at least 70°C, at least 75°C, at least 80°C, or at least 90°C.

40. A polynucleotide encoding the fusion protein of any of claims 1-39.

41. The polynucleotide of claim 40, comprising a nucleotide sequence having at least 75%, 80%, 85%, 90%, 95%, 96%, 98% or 99% sequence identity to any one of SEQ ID NO: 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 151, 152, 153, 154, 155, 156, 157, 158, 159, 160, 161, 162, 163, 164, 165, 166, 167, 168 or 169.

42. A vector comprising at least one polynucleotide according to claim 40 or 41.

43. The vector according to claim 43, wherein said vector is a recombinant expression vector.

44. A cell comprising the fusion protein according to any one of claims 1-39, the polynucleotide according to claim 40 or 41 or the vector according to claim 42 or 43.

45. The cell of claim 44, wherein the cell is a mammalian cell, a fungal cell or a bacterial cell.

46. The cell of claim 45, wherein the cell is a bacterium, optionally wherein the bacterium is Escherichia coli or a bacterium of the genus bacillus.

47. The cell of claim 45 or 46, wherein the cell is a competent E. coli cell, optionally a BL21(DE3) competent E. coli cell.

48. The cell of claim 45 or 46, wherein the cell is a cell from a B. subtilis strain 168 or B. subtilis RIK1285 bacterium.

49. A method of producing a fusion protein according to any one of claims 1-39 comprising the steps of: (i) providing one or more cells of any one of claims 44-48, (ii) culturing said cells in conditions suitable for the expression of the fusion protein, and (iii) obtaining a fusion protein from said culture.

50. The method of claim 49, wherein the one or more cells are cultured in a microbial growth medium.

51. The method of claim 50, wherein the growth medium is selected from the group consisting of LB medium, TB medium, SOC medium, minimal and complex medium, or expression medium (1% tryptone, 0.5%, yeast extract, 25 mM Na2HPO4, 25 mM KH2PO4, 25 mM (NH4)2SO4, 2 mM MgSO4, 0.05% glucose and 0.2% α-lactose).

52. The method of any one of claims 49-51, wherein the cells are cultured at a temperature in the range of about 5°C to about 50°C, such as about 5°C to about 30°C, 10°C to about 30°C, 10°C to about 20°C, 25°C to about 45°C, about 30°C to about 40°C, or about 35°C to about 40°C, optionally wherein the temperature is about 16°C.

53. The method of any one of claims 49-52, wherein the fusion protein is secreted by the one or more cells.

54. The method of any one of claims 49-53, wherein step (iii) of obtaining the fusion protein comprises one or more of: (a) lysing the cells provided in step (i), (b) Immobilized Metal Affinity Chromatography (IMAC), Ion Exchange Chromatography, Hydrophobic Interaction Chromatography (IEX), membrane filtration, thermos-precipitation, affinity precipitation, or aqueous two-phase extraction.

55. A method of degrading one or more plastic polymers comprising contacting the one or more plastic polymers with one or more of the fusion proteins of any one of claims 1-39.

56. Use of one or more fusion protein according to any one of claims 1-39 to degrade one or more plastic polymers, the use comprising contacting the one or more plastic polymers with the one or more fusion proteins.

57. The method or use according to claims 55 or 56, wherein the one or more plastic polymers comprise or consist of PET, PTT, PBT, PBS, PEF, PLA, PCL, PBAT, PHA, blends or combinations thereof, or mixed plastic waste.

58. The method or use of any one of claims 55-57, wherein the one or more fusion proteins and the one or more plastic polymers are contacted in a solution.

59. The method of claim 58, wherein at least one fusion is in solution.

60. The method of claim 58, wherein at least one fusion protein is immobilized to a solid support.

61. The method of claim 60, wherein said solid support is a surface or a bead.

62. The method or use of any one of claims 58-61, wherein said solution has a pH in the range of about 5 to about 10, such as about 6 to about 9, about 7 to about 9, about 7 to about 8 or about 8 to about 9.

63. The method or use of any one of claims 58-62, wherein said solution comprises a buffer solution, optionally wherein said buffer solution is selected from the group consisting of potassium phosphate buffer, Tris-HCl buffer or Bicine buffer.

64. The method or use of any one of claims 55-63, wherein said one or more plastic polymers are present at a concentration in the range of about 0.1 g / L to about 700 g / L, such as about 0.1 g / L to about 700 g / L, about 5 g / L to about 650 g / L, about 10 g / L to about 600 g / L, about 15 g / L to about 550 g / L, about 20 g / L to about 500 g / L, about 25 g / L to about 450 g / L, about 30 g / L to about 400 g / L, about 35 g / L to about 350 g / L, about 40 g / L to about 300 g / L, about 45 g / L to about 250 g / L or about 50 g / L to about 200 g / L.

65. The method or use of any one of claims 55-64, wherein said one or more fusion proteins are present at a concentration in the range of about 0.001 µM to about 100 µM, such as about 0.001 µM to about 100 µM, about 0.025 µM to about 90 µM, about 0.05 µM to about 80 µM, about 0.075 µM to about 70 µM, about 0.1 µM to about 60 µM, about 0.125 µM to about 50 µM, about 0.15 µM to about 40 µM, about 0.175 µM to about 30 µM, about 0.2 µM to about 20 µM, about 0.225 µM to about 10 µM, about 0.25 µM to about 1 µM, about 0.25 µM to about 0.75 µM, about 1 µM to about 3 µM, or about 1.5 µM to about 2.5 µM.

66. The method or use of any one of claims 55-65, wherein said contacting is performed at a temperature in the range of about 4°C to about 90°C, such as about 10°C to about 90°C, about 20°C to about 90°C, about 30°C to about 90°C, about 40°C to about 85°C, about 50°C to about 80°C, about 55°C to about 75°C, or about 50°C to about 70°C.

67. The method or use of any one of claims 55-66, wherein said solution is agitated, mixed or stirred during said contacting.

68. The method or use of any one of claims 55-67, wherein said contacting is performed for about 10 hours to about 672 hours, such as about 10 hours to about 672 hours, about 14 hours to about 608 hours, about 18 hours to about 544 hours, about 22 hours to about 480 hours, about 26 hours to about 416 hours, about 30 hours to about 352 hours, about 34 hours to about 288 hours, about 38 hours to about 224hours, about 42 hours to about 160 hours, about 46 hours to about 128 hours or about 48 hours to about 96 hours.

69. The method or use of any one of claims 55-68, further comprising a step of contacting said one or more plastic polymers with one or more additional catalytically active proteins.

70. The method or use of claim 69, wherein said one or more additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulase, or a pectinase.

71. The method or use of claim 69 or 70, wherein said further step of contacting said one or more plastic polymers with one or more additional catalytically active proteins is carried prior to the step of contacting said one or more plastic polymers with said one or more fusion proteins.

72. A kit comprising (i) one or more fusion proteins according to any one of claims 1- 39 and (ii) a suitable buffer solution and / or one or more additional catalytically active proteins.

73. The kit of claim 72, wherein the buffer solution is selected from the group consisting of potassium phosphate buffer, Tris-HCl buffer or Bicine buffer.

74. The kit of claim 72 or 73, wherein the additional catalytically active proteins comprise one or more of an esterase, a PETase, a lipase, a laccase, a peroxidase, a monooxygenase, a tyrosinase, a protease, a cellulase, a hemicellulose, or a pectinase.

Images