44 results about "Phenylpyruvic acid" patented technology

The invention discloses a high-yield delta-tocotrienol genetically engineered bacterium and application thereof, and belongs to the technical field of gene recombination. The invention discloses a genetically engineered bacterium for high yield of delta-tocotrienols, which is characterized in that yarrowia lipolytica ATCC MYA-2613 is used as an original strain, and a ku70 gene is knocked out; the gene is used for expressing and coding 4-hydroxyphenylpyruvate dioxygenase, the gene is used for coding uromelanic acid phytate transferase and the gene is used for coding tocopherol cyclase; intensifying a shikimic acid pathway; a mevalonic acid pathway is strengthened; an isopentenol path is introduced; carrying out protein fusion on the HPD and the HPT; truncating a signal peptide of a gene encoding a tocopherol cyclase and back-filling a leucine defect. The genetically engineered bacterium constructed by the invention has industrial stability, can be amplified by more than 10 times in a 2L fermentation tank level compared with a shake flask level, can produce 616.45 mg / L of delta-tocotrienol after being cultured for 240 hours, and has industrial application prospects.

The invention provides p-hydroxymandelic acid synthetase, a gene, a mutant of the p-hydroxymandelic acid synthetase and application of the p-hydroxymandelic acid synthetase in asymmetric synthesis of (S)-mandelic acid. The p-hydroxymandelic acid synthetase disclosed by the invention is derived from actinomycetes Actinokineospora auranticola, the amino acid sequence of the p-hydroxymandelic acid synthetase is as shown in SEQ ID NO.1, and a mutant of the p-hydroxymandelic acid synthetase is obtained by performing single-point mutation or multi-point combined mutation on glutamic acid at the 187th site, isoleucine at the 189th site and threonine at the 211th site of the amino acid sequence as shown in SEQ ID NO.1. The p-hydroxymandelic acid synthetase and the mutant thereof can convert phenylpyruvic acid into (S)-mandelic acid with high optical purity, have the advantages of mild reaction conditions, simplicity and convenience in operation, safety, environment friendliness and the like, and have a very good industrial application prospect.

The invention provides application of acidophilous glycosyltransferase in salidroside production, and belongs to the technical field of biological engineering. The problem of producing salidroside under the acidic condition is solved. Comprising an application of acidophilous glycosyl transferase with an amino acid sequence as shown in SEQ ID NO.1 in salidroside production under an acidic condition and an acidophilous escherichia coli engineering strain for producing salidroside. The escherichia coli engineering strain overexpresses a mutant 3-deoxy-D-arabinoheptulose-7-phosphate (DAHP) synthetase gene aroGfbr, a cyclohexadiene dehydrogenase gene tyrC, a glucose phosphate mutant enzyme gene pgm and a UDP-glucose pyrophosphorylase galU, overexpresses a phenylpyruvate decarboxylase gene ARO10 derived from saccharomyces cerevisiae, and can be used for producing a mutant 3-deoxy-D-arabinoheptulose-7-phosphate mutant enzyme. The kit comprises an ethanol dehydrogenase gene ADH6 and a glycosyl transferase gene LrUGT85AF8. The method is mainly used for producing salidroside under an acidic condition.

The invention discloses a recombinant microorganism for producing hydroxytyrosol as well as a construction method and application of the recombinant microorganism. According to the recombinant microorganism, 3-deoxy-D-arabinoheptulose-7-phosphate synthetase aroGfbr, chorismate mutase / pre-benzoic acid dehydrogenase tyrAfbr, 4-hydroxyphenylacetic acid 3-hydroxylase HpaBC, phenylpyruvate decarboxylase ARO10 and alcohol dehydrogenase ADH6 are subjected to overexpression, and the recombinant microorganism can be used for preparing the recombinant microorganism. The genome of the gene naturally comprises a citrate synthase coding gene gltA and a tyrosine aminotransferase coding gene tyrB; the original promoter of the gltA and / or the original promoter of the tyrB are / is replaced by a time sequence promoter PrrnC-37. When the recombinant microorganism is used for producing hydroxytyrosol, the production efficiency can be improved, and the production cost of hydroxytyrosol can be reduced.

Various methods and compositions of treating 4-hydroxyphenylpyruvate dioxygenase-like (HPDL)-related diseases or disorders are presented herein. Also presented herein are methods of increasing CoQ10 biosynthesis, and methods of determining whether a subject will benefit from a CoQ10 or CoQ10 alternative treatment. Also presented herein are pharmaceutical compositions and dosage forms comprising 4-hydroxymandelic acid (4-HMA), and / or its metabolites. Further presented herein are compounds that inhibit 4-hydroxyphenylpyruvate dioxygenase-like (HPDL). Further presented herein are methods of identifying and / or assessing modulators of HPDL. Yet further presented herein are example methods and systems for isotopic labelling in cells by metabolizing cells in the presence of gaseous isotopic tracer.

The invention discloses application of phenylpyruvic acid in prevention and control of citrus canker, and belongs to the field of treatment of agricultural canker. The invention discloses a new application of phenylpyruvic acid in treating and / or preventing citrus canker, and the effective dosage of phenylpyruvic acid is 0.01-1.5 M. The phenylpyruvic acid is externally applied, so that the scab area of the citrus canker can be reduced to a great extent, and the attack degree of the canker is reduced. In addition, the content of phenylpyruvic acid in citrus can be increased through multiple technologies, and the phenylpyruvic acid can be used for canker-resistant molecular breeding.

The invention provides a phenylpyruvate decarboxylase mutant with multi-site mutation and application of the phenylpyruvate decarboxylase mutant in production of tyrosol, and belongs to the technical field of bioengineering. The problem of low yield of tyrosol is solved. The phenylpyruvate decarboxylase mutant comprises a phenylpyruvate decarboxylase mutant, and the phenylpyruvate decarboxylase mutant is obtained by mutating any two or three sites of the 93rd site, the 106th site, the 153rd site, the 220th site, the 242nd site, the 273rd site and the 285th site by taking amino acid as shown in SEQ ID NO.2 as a starting sequence. The method is mainly used for increasing the yield of tyrosol.

The invention discloses 2-phenethyl alcohol-beta-D-glucoside catalyzed and synthesized by a cofactor self-circulating multi-enzyme cascade system and application of the 2-phenethyl alcohol-beta-D-glucoside. The system comprises phenylalanine dehydrogenase and a mutant thereof, wherein the phenylalanine dehydrogenase is used for converting L-phenylalanine (L-Phe) into phenylpyruvic acid (PPA); pPA is converted into pyruvate decarboxylase (Aro10) of phenylacetaldehyde; the alcohol dehydrogenase is used for reducing phenylacetaldehyde into 2-phenethyl alcohol (2-PE) or a mutant of the alcohol dehydrogenase; 2-PE is converted into sucrose synthase (SuSy) of 2-phenethyl alcohol-beta-D-glucoside (2PE-Glc) or a mutant of the sucrose synthase, and UDP-glucosyltransferase (UGT) or a mutant of the UDP-glucosyltransferase. A novel multi-enzyme cascade system with cofactor self-circulation capability is realized and is used for efficiently synthesizing 2PE-Glc from L-phenylalanine. The invention not only provides an effective 2PE-Glc biosynthesis strategy, but also shows the potential of a multi-enzyme cascade system in the aspect of synthesizing biologically active complex glycoconjugates.

The present invention discloses a phenylpyruvate reductase mutant with high enzyme activity and its application. Lactobacillus The wild-type phenylpyruvate reductase of sp. CGMCC 9967 is molecularly modified, and the 193rd position of the amino acid sequence shown in SEQ ID NO.1 is mutated from asparagine to aspartic acid, and the 203rd position is mutated from histidine to arginine, so as to obtain a phenylpyruvate reductase mutant with high enzyme activity. The 193rd and 203rd positions are located on the enzyme surface and are related to NADH and substrate binding activity. The present invention proposes for the first time to carry out site-directed mutation of these two positions, and obtains a mutant with significantly improved enzyme activity, which provides more possibilities for the mutation design of phenylpyruvate reductase with improved enzyme activity. The present invention has important practical significance for the industrial catalysis of phenylpyruvate to produce phenyllactic acid and the industrial application of phenylpyruvate reductase.

The invention relates to the technical field of gene engineering, and discloses a recombinant Escherichia coli engineering strain for producing phenethyl alcohol by using L-phenylalanine as a substrate, the recombinant Escherichia coli engineering strain comprises a recombinant Escherichia coli engineering strain for producing phenethyl alcohol by using L-phenylalanine as a substrate, and the recombinant Escherichia coli contains a key gene capable of synthesizing phenethyl alcohol. Proteins coded by the key gene are a transaminase gene, a phenylpyruvate decarboxylase gene and an ethanol dehydrogenase gene. According to the invention, a recombinant plasmid containing a phenethyl alcohol biosynthetic pathway is constructed, the recombinant plasmid is transformed into Escherichia coli, and a recombinant engineering strain for improving the yield of phenethyl alcohol is screened out. The recombinant escherichia coli engineering strain contains transaminase KmARO8 derived from kluyveromyces marxianus, phenylpyruvate decarboxylase VvPDC1 derived from wine grapes and ethanol dehydrogenase AtADH1 derived from arabidopsis thaliana, the yield of phenethyl alcohol can be 7.29 g / L after fermentation culture of the recombinant strain, and the recombinant escherichia coli engineering strain has a good industrial prospect.

This invention discloses a recombinant *E. coli* strain for producing phenyllactic acid, a lactate dehydrogenase mutant, a whole-cell catalytic method for preparing phenyllactic acid, and the application of the aforementioned recombinant *E. coli* strain or lactate dehydrogenase mutant in the catalytic preparation of phenylpyruvic acid from phenyllactic acid. This invention significantly improves catalytic efficiency by modifying the 52nd amino acid of lactate dehydrogenase through site-directed mutagenesis. After mutating glutamine (Q) to valine (V) at position 52 of the *Lactobacillus mucosa* lactate dehydrogenase, the catalytic efficiency is significantly improved even at low cell density (OD). 600 =15) and substrate 15 g / L conditions, almost complete conversion was achieved; and combined with high-density catalysis and surface display optimization, the yield of phenyl lactic acid was increased while the downstream separation and purification costs were significantly reduced, greatly enhancing the potential for industrial production.

In a method for preparing a keto acid, an enzymatic reaction is carried out by using glycine and an alcoholic organic substance as substrates; the alcoholic organic substance is converted into an aldehyde organic substance, glycine and the aldehyde organic substance are converted into a β-hydroxy-α-amino acid, and then the β-hydroxy-α-amino acid is converted into a keto acid. The preparation method for a keto acid can also be used in the preparation of amino acids. The number of enzymes used is much less than that of enzymes used in a natural synthesis route, so that the production cost is low. An artificial metabolism platform for keto acids is established and can produce multiple important keto acids, such as phenylpyruvic acid, 4-methyl-2-oxopentanoic acid, pyruvic acid and 2-oxo-butyric acid.

Provided herein are compositions and methods for increasing the amount aryl-lactates in fermented foods. The methods can comprise delivering alpha-ketoglutarate (AKG), trisodium citrate dehydrate (CIT), or both AKG and CIT; and / or phenylpyruvic acid (PPyA), 4-hydroxyphenylpyruvic acid (4HPPyA), indole-3-pyruvic acid (IPyA) or combinations thereof; and / or phenylalanine (Phe), tyrosine (Tyr), and / or tryptophan or combinations thereof to fermented foods and fermented food matrices. Optionally, bacteria with aromatic amino transferase (ArAT) and / or phenyllactate dehydrogenase activity can also be added to the fermented foods and fermented food matrices. Also provided are methods to increase the bioactivity of fermented foods towards an immune receptor (aryl hydrocarbon receptor—AhR). Also provided are methods to more effectively maintain food matrix AhR bioactivity across food storage times of up to 4 weeks. Also provided are methods of inducing weight loss, reducing fat mass, and / or reducing glucose intolerance in mammals.

The invention relates to the technical field of biology, in particular to a phenylpyruvate decarboxylase ARO10 protein mutant and application of the phenylpyruvate decarboxylase ARO10 protein mutant in preparation of phenethyl alcohol. The invention discloses an ARO10 mutant. The phenylpyruvate decarboxylase mutant is obtained by mutating one or more of the 335th amino acid, the 339th amino acid and the 628th amino acid of phenylpyruvate decarboxylase ARO10 (the amino acid sequence shown as SEQ ID NO.1) from yeast. Experiments prove that the mutated phenylpyruvate decarboxylase protein can improve the specific reaction on phenylpyruvic acid, so that the phenethyl alcohol generation capability of saccharomyces cerevisiae is improved. Glycosyl transferase ARO10 mutant protein is expressed in microorganisms, the phenethyl alcohol conversion capacity of the microorganisms is obviously enhanced, and the industrial application prospect is good.

The application discloses a kind of functionalized graphene materials, preparation method and its application in phenylpyruvic acid preparation, belong to graphene catalytic organic drug synthesis technical field, 4-dimethylaminopyridine is added to the prepared graphene solution, ultrasonic treatment is then carried out under the condition of 120~180 DEG C for 12~36h, the product is filtered, washed and dried after reaction is finished and naturally cooled to room temperature, and black solid is obtained as functionalized graphene material DMAP-rGO, which is used as catalyst to prepare phenylpyruvic acid, has better stability and reusability, and can be widely used in industrial production.

The invention relates to the field of bioengineering, in particular to recombinant yarrowia lipolytica with high yield of denosine as well as a construction method and application of the recombinant yarrowia lipolytica. According to the invention, Yarrowia lipolytica is taken as a chassis cell, a phenylalanine ammonialyase gene PtrPAL3, a coumaroyl-coenzyme A ligase gene Pc4CL1 and a stilbene synthetase gene PtSTS are inserted into a genome, and 3-deoxy-D-arabinohepturonate-7-phosphate synthetase gene ARO3 and an acetyl-coenzyme A carboxylase gene ACC1 are overexpressed, so that the Yarrowia lipolytica is obtained. The 4-hydroxyphenylpyruvate dioxygenase gene HPD and the phenylpyruvate decarboxylase gene ARO10 are knocked out, and the recombinant yarrowia lipolytica is constructed and obtained. After genetic modification, the strain has the capability of synthesizing the pinosine from the beginning, the fermentation yield reaches 260mg / L by using a glucose shake flask, and the yield of the pinosine fermented in a 5L fermentation tank reaches 1200mg / L. According to the method, high-efficiency production of the pinosine is realized by utilizing the yarrowia lipolytica for the first time, and the pinosine yield of the constructed recombinant yarrowia lipolytica is the highest level of microbial fermentation production at present.

The present invention relates to a mutant of Rhodococcus opaqueus L-amino acid oxidase and its application, belonging to the field of bioengineering technology. The present invention overcomes the limitation of poor catalytic performance of wild-type RoLAAO and designs a mutant RoLAAO through maltoprotein engineering and combined mutation. Y226H / D227H / Y371L / A466C / W467A Its catalytic efficiency for five selected substrates is 9.2-82.8 times that of the wild type. It can use L-amino acids (L-Leu, L-Ile, L-Met, L-Val and L-Phe) as substrates to prepare a series of α-keto acids (α-ketoleucine, α-ketoisoleucine, α-ketomethionine, α-ketovaline and α-phenylpyruvate) on a large scale, with a corresponding yield of >101g / L and a conversion rate of >95%. The unit cell capacity for producing α-keto acids is 5.1-5.5g / g, laying the foundation for the industrial production of a variety of α-keto acids.

The present invention discloses a recombinant Escherichia coli for efficiently producing D-salvianic acid and its construction method and application. By changing the plasmid copy number and the strength of RBS, the present invention finely regulates the expression levels of the pathway enzymes L-amino acid deaminase LAAD, phenylpyruvate reductase LaPPR and glucose dehydrogenase GDH of D-salvianic acid, achieving the balance of the cascade pathway reaction. The optimal recombinant strain E. coli 13 (containing plasmids pRSF-LAAD-LaPPR, PCDF-GDH) adopts a fed-batch strategy (a total of 60 g / L L-DOPA is fed) in a 5 L fermenter and is transformed for 16 h, and the yield of D-salvianic acid reaches 58.86 g / L, and the conversion rate is 97.6%. The method of the present invention has great potential and wide value for increasing the yield of D-salvianic acid industrially.

The application discloses a genetically engineered bacterium with high yield of gallic acid and application thereof, and belongs to the technical field of gene recombination.The genetically engineered bacterium with high yield of gallic acid is prepared from Yarrowia lipolytica ATCC MYA-2613 as a starting strain, and the ku70 gene is knocked out; the gene coding 4-hydroxyphenylpyruvate dioxygenase is expressed; the shikimic acid pathway is strengthened; and three copies of tHMGR and the lysine defect are integrated.In 2L fermenter fed-batch fermentation, the yield of gallic acid is 33.71g / L, which is more than 10 times higher than the highest yield of gallic acid of 2.8g / L of the genetically engineered Yarrowia lipolytica reported at present in 2L fermenter fed-batch fermentation, and the application lays a solid foundation for industrialization of Yarrowia lipolytica for producing gallic acid, and has an industrial application prospect.

The invention discloses lactobacillus plantarum with phenyllactic acid biosynthesis performance and application of the lactobacillus plantarum, and belongs to the technical field of biology. The invention provides lactobacillus plantarum CJEL01, which is preserved in the China General Microbiological Culture Collection Center (CGMCC), the preservation number of the lactobacillus plantarum CJEL01 is CGMCC No.30204, and the preservation date of the lactobacillus plantarum CJEL01 is March 29, 2024. The lactobacillus plantarum CJEL01 provided by the invention can be used for synthesizing phenyllactic acid by using kumquat pulp, phenylalanine and phenylpyruvic acid, and has the characteristics of simple steps, environmental protection, no pollution and the like, and the obtained fermentation liquor has great application potential in the aspect of food preservation, and lays a foundation for research and development of natural bacteriostatic agent products of citrus flavones, polyphenols and phenyllactic acid in the later period.

Provided are a genetically engineered bacterium, a preparation method therefor and a use thereof in de novo synthesis of salidroside. The genetically engineered bacterium comprises an exogenously introduced phenylpyruvate decarboxylase gene ARO10 and a glycosyltransferase gene OfT8GT1, wherein the phenylpyruvate decarboxylase gene ARO10 has a nucleotide sequence as shown in SEQ ID NO: 3, and the glycosyltransferase gene OfT8GT1 has a nucleotide sequence as shown in SEQ ID NO: 4. The method for synthesizing salidroside from the genetically engineered bacterium by catalysis greatly reduces synthesis costs, simplifies subsequent separation and purification steps, and exhibits high efficiency of salidroside synthesis, thereby laying a foundation for industrial production of salidroside by using a microbial fermentation method.

A herbicidal composition and a method for controlling weeds, including one or more uracil compounds of formula (I) and a compound of formula (II), and a herbicide compound of group B and a safener of group C. A weight ratio of the uracil compounds to the herbicide compound group B and the safener group C is 1:0.02 to 1:50, and the herbicide compound of group B is one or more of compounds B-1 to B-12: B-1, acetolactate synthase inhibitors; B-2, acetyl CoA carboxylase inhibitors; B-3, protoporphyrinogen IX oxidase inhibitors; B-4, 4-hydrophenylpyrubic acid dioxygenase inhibitors; B-5, phytoene desaturase inhibitors; B-6, photosystem II inhibitors; B-7, very-long-chain fatty acid synthesis inhibitors; B-8, microtubule formation inhibitors; B-9, auxin-type herbicides; B-10, enolpyruvylshikimate-3-phosphate synthase inhibitors; B-11, glutamine synthase inhibitors; and B-12, other herbicides; or agriculturally acceptable salts or derivatives thereof

The present application belongs to the technical field of genetic engineering, and relates to a recombinant Yarrowia lipolytica for synthesizing homogentisic acid as well as a construction method and application thereof. The recombinant strain is obtained by genetic modification of a starting strain. Compared with the starting strain, the activity of phenylpyruvate decarboxylase ARO10 of the recombinant strain is weakened or inactivated. The construction method comprises: genetic modification of the starting strain to weaken or inactivate the activity of phenylpyruvate decarboxylase of the starting strain. The method for fermenting and synthesizing homogentisic acid comprises: inoculating the aforementioned recombinant strain into a fermentation medium added with L-tyrosine to perform fermentation; or, constructing the recombinant strain according to the aforementioned method, and inoculating the obtained recombinant strain into a fermentation medium added with L-tyrosine to perform fermentation. More phenylpyruvic acid in the recombinant strain flows to the homogentisic acid synthesis pathway, and the yield of homogentisic acid can be effectively improved.

This invention relates to a phenylpyruvate decarboxylase mutant for the synthesis of phenylethanol and its applications, belonging to the fields of enzyme engineering and genetic engineering. To address the technical problems of low catalytic efficiency, poor substrate affinity, and insufficient stability of existing phenylpyruvate decarboxylases, which lead to low biosynthetic efficiency and limited yield of phenylethanol, making it difficult to meet the needs of industrial production, this invention provides a phenylpyruvate decarboxylase mutant for the synthesis of phenylethanol. This mutant offers a new and highly efficient synthetic element for the biosynthesis of phenylethanol, with broad application prospects and market potential in the field of higher alcohol synthesis.

The invention discloses a genetically engineered bacterium for high yield of uromelanoic acid and application thereof, and belongs to the technical field of gene recombination. The invention discloses a genetically engineered bacterium for high yield of uromelanoic acid, which is characterized in that yarrowia lipolytica ATCC MYA-2613 is used as an original strain, and a ku70 gene is knocked out; the method comprises the following steps: expressing a gene for coding 4-hydroxyphenylpyruvate dioxygenase; intensifying a shikimic acid pathway; and the tHMGR of three copies is integrated, and leucine defects are supplemented. The Yarrowia lipolytica genetically engineered bacterium has the advantages that the Yarrowia lipolytica genetically engineered bacterium has the advantages that the Yarrowia lipolytica genetically engineered bacterium is high in yield, the yield of the uromelanic acid is 33.71 g / L when the Yarrowia lipolytica genetically engineered bacterium is subjected to fed-batch fermentation in 2L fermentation tanks and is increased by more than 10 times as compared with the highest yield 2.8 g / L of the uromelanic acid when the Yarrowia lipolytica genetically engineered bacterium is subjected to fed-batch fermentation in the 2L fermentation tanks, and solid foundations are laid for industrialization of Yarrowia lipolytica

The invention relates to a construction method of high-yield rosmarinic acid engineering saccharomycetes, which comprises the following steps of: introducing synthetic route related enzymes of rosmarinic acid into starting saccharomycetes, knocking out endogenous phenylpyruvate synthetase of a strain, and introducing pre-benzoic acid transaminase and longroot acid dehydratase into the starting saccharomycetes. According to the invention, a pre-benzoate transaminase expression cassette is introduced into yeast cells, so that the yeast can synthesize the longroot acid, synthesis routes of phenylalanine, tyrosine and derivatives thereof can be reconstructed by taking the longroot acid as a center, and meanwhile, endogenous synthesis routes of phenylalanine and tyrosine in the yeast cells are knocked out; some by-products in an endogenous way are eliminated, and the yield of the rosmarinic acid is increased. On the basis, the related enzyme combination of the rosmarinic acid synthesis route is further optimized, the content of the rosmarinic acid is increased to nearly 1g / L at most, and a road is tamped for the biosynthesis industrialization of the rosmarinic acid.

The invention relates to the technical field of biological engineering, and discloses a method for synthesizing chiral phenylalaninol by multi-enzyme cascade catalysis of L-phenylalanine. L-amino acid deaminase, phenylpyruvate decarboxylase, benzaldehyde lyase and transaminase are used for catalyzing the reaction of L-phenylalaninol in a cascade manner to generate chiral phenylalaninol. The method is carried out in a one-pot two-stage reaction manner; in the first stage, L-amino acid deaminase, phenylpyruvate decarboxylase and benzaldehyde lyase are used for carrying out cascade catalysis on natural L-phenylalanine to synthesize 1-hydroxy-3-phenylpropane-2-ketone; in the first stage, 1-hydroxyl-3-phenylpropane-2-ketone is used as a raw material, and in the second stage, transaminase is used for catalyzing 1-hydroxyl-3-phenylpropane-2-ketone to synthesize chiral phenylalaninol, the method is simple and convenient in step operation, low in cost, high in product synthesis efficiency and high in selectivity, a new way is provided for green and sustainable synthesis of chiral phenylalaninol, and the method has a good industrial application prospect.

The present disclosure concerns a recombinant yeast host cell for making a flavored solution obtainable or obtained by fermentation of a fermentation medium. The recombinant yeast host cell comprises an upregulated alcohol acetyltransferase 2 (ATF2) and / or an upregulated phenylpyruvate decarboxylase (ARO10); and at least one downregulated native transferase when compared to a wild-type yeast host cell. The at least one downregulated transferase is a native alcohol acetyltransferase 1 (ATF1) and / or a native ethanol acetyl-CoA transferase (EAT1). The present disclosure also concerns process for making a flavored solution which could be used to generate new flavored beverages such as beer, distilled spirits, and wines.

The invention relates to the technical field of biology, in particular to a phenylpyruvate decarboxylase ARO10 protein mutant and application of the phenylpyruvate decarboxylase ARO10 protein mutant in preparation of tyrosol. The invention discloses an ARO10 mutant. The phenylpyruvate decarboxylase mutant is obtained by mutating one or more of the 335th site of phenylpyruvate decarboxylase ARO10 (an amino acid sequence shown as SEQ ID NO1) from yeast. Experiments prove that the mutated phenylpyruvate decarboxylase protein can improve the specific reaction on 4-hydroxyphenylpyruvic acid, so that the tyrosol generation capability of saccharomyces cerevisiae is improved. Glycosyl transferase ARO10 mutant protein is expressed in microorganisms, the capacity of the microorganisms for converting tyrosol is obviously enhanced, and the industrial application prospect is good.

The invention discloses a phenylpyruvate decarboxylase mutant and application of the phenylpyruvate decarboxylase mutant in production of tyrosol, and belongs to the technical field of bioengineering. The purpose of the present invention is to increase the yield of tyrosol. The phenylpyruvate decarboxylase mutant provided by the invention is obtained by mutating any one of the 56th site, the 92th site, the 93th site, the 106th site, the 115th site, the 153th site, the 178th site, the 188th site, the 214th site, the 220th site, the 234th site, the 242th site, the 273th site, the 285th site, the 371th site, the 416th site, the 581th site and the 621th site by taking amino acid as shown in SEQ ID NO.2 as a starting sequence. The phenylpyruvate decarboxylase is mainly used for high-efficiency phenylpyruvate decarboxylase and application thereof in de novo synthesis of tyrosol.