Perfume release mechanisms, methods and uses thereof

Abstract

The present disclosure relates to release compositions comprising a protein and an active agent, wherein the active agent is released when in the presence of an electrolyte solution. Also encompassed are kits and articles of manufacture comprising the release compositions of the present subject matter.

Description

Technical Field

[0001] This disclosure relates to a mechanism of adsorption and dissociation involving fragrance molecules and an odor-binding protein (OBP-I) that is simultaneously regulated by human sweat and temperature. This system can be used in cosmetic formulations where fragrances are released at body temperature in the presence of sweat. Background Technology

[0002] Odor-binding protein (OBP) is a small, water-soluble protein belonging to the lipid transporter superfamily. 1 2 They are responsible for transporting hydrophobic odor molecules (called odor molecules) across the aqueous mucus barrier to olfactory receptors in their calyx cavity, where the cascade of brain signals that interpret the transduction signals is disrupted. 3-4 These proteins have also been described as being involved in removing odor molecules from olfactory receptors after stimulation of the olfactory receptors. 5-6

[0003] Several mammalian odor-binding proteins have been identified, some of which were isolated from nasal mucus from animals such as cattle, pigs, wild boars, pandas, mice, rats, and humans. 7-13

[0004] The DNA sequences of mammalian OBPs show low similarity: porcine OBP (OBP-I) and human OBP (hOBP) IIa Only 13.9% DNA sequence similarity was observed; OBP-I and bovine OBP showed 42.7%. 4 Despite the wide range of genetic variations among OBPs from different mammalian species, lipid transporter members exhibit few characteristic signals that allow them to be identified as having a conserved tertiary structure, exhibiting a β-barrel structure consisting of eight β-chains linked by seven loops to a short α-helix near the C-terminus and a ninth β-chain, followed by a disordered C-terminal tail. 14 16 OBP has a highly stable structure and is resistant to degradation by temperature, organic solvents, pH changes, or protein hydrolysis. 17 18 19 The FT-IR spectrum of porcine OBP revealed an unusually stable structure to thermal denaturation (up to 80 °C), especially in the presence of ligands. 20 Furthermore, vertebrate OBPs have shown the ability to reverse protein unfolding even after denaturation. 20

[0005] The human body produces unpleasant odors associated with stress, anxiety, tension, and physical exercise. 21 To prevent or reduce their occurrence, antibacterial agents and fragrances are often added to cosmetic formulations. However, drawbacks have been detected in clothing and skin, including limited effectiveness against different odors and the amount of residue left by these deodorants.22

[0006] OBP has an affinity for several molecules associated with odor perception. All of these molecules are volatile and are detected by OBP at very low concentrations, making it a highly sensitive system. The rapid response time of OBP and the high stability of these proteins create excellent biological elements as biosensors for detecting hazardous substances and pathogens, pesticides, and drugs present in food or water. 18,23 And its potential uses as a deodorant and in medical diagnostics. 24-25

[0007] Odor molecules can be associated with pleasant or unpleasant sensations. OBP has an affinity for all molecules associated with odors. 3-4 Fragrances are compositions containing odor molecules that produce a pleasant sensation.

[0008] Using 1-aminoanthracene (1-AMA) as an odor model molecule provides the ability to measure the binding capacity of odor-binding proteins via fluorescence assays. Free 1-AMA and 1-AMA bound to porcine OBP-I can be quantified by measuring fluorescence at an excitation wavelength of 295 nm. The maximum wavelength of 1-AMA bound to OBP-I shifted from 537 nm to 481 nm. 20 Non-fluorescent odorants can be measured by competitive testing or by gas chromatography-mass spectrometry.

[0009] The following work has reported the interactions between OBP and odor model molecules, as well as interactions with lipid structures such as liposomes.

[0010] Filipa Goncalves et al. (2018) “Two engineered OBPs with opposite temperature-dependent affinities for 1-aminoanthracene” mention two recombinant proteins based on porcine OBP sequences: (i) a truncated OBP (tOBP-F44A / F66A), obtained by deleting the first 16 residues of the N-terminus and replacing the two phenylalanine residues (F44A and F66A) at the binding pocket with alanine residues, and (ii) OBP::GQ. 20 ::SP-DS3 is formed by the fusion of OBP-I with a spacer region consisting of 20 repeating glycine-glutamine residues and the anchoring peptide SP-DS3. 34 Experimental and molecular modeling data show that the 1-AMA model ligand preferentially binds to OBP-F44A / F66A at 25°C, while the ligand favorably binds to OBP::GQ at 37°C. 20 ::SP-DS3. 34

[0011] Filipa Goncalves et al. (2018) reported on the fusion of porcine OBP with cell-penetrating peptides (CPPs, such as TAT, Pep-1, and pVEC) in their study "OBP fusion with cell-penetrating peptides promotes liposome transduction." This study revealed varying efficiencies in the transduction of 1-AMA into liposomes. 30

[0012] Filipa Goncalves et al. (2018) disclosed the design of two fusion proteins in “Transduction of 1-aminoanthracene into liposomes driven by odor-binding protein proximity”, which are based on porcine OBP and the anchoring peptide SP-DS3. 32 Fusion in the absence and presence of gap regions (GQ) 20 This work demonstrates that the transduction of 1-AMA into liposomes is driven by the proximity of proteins anchored to the liposome membrane (advantageously, without spacer regions). 33

[0013] Filipa Goncalves et al. (2019) disclosed the release of fragrance from cotton functionalized with carbohydrate-binding modular proteins based on porcine OBP and spacer region (GQ). 20 The design of a fusion protein combining a protein with a carbohydrate-binding module (CBM) was described. This work demonstrates the protein's affinity for a fragrance (β-citronellol) and its release from cotton in the presence of sweat. 25 Nevertheless, its release capacity is poorer in the presence of sweat compared to natural OBP.

[0014] Alessandro Capo et al. (2018) disclosed that pig odor-binding protein was used as a probe for the detection of benzene in the atmosphere by fluorescence assay. 28

[0015] Nunzio Cennamo et al. (2015) reported on the detection of butyraldehyde (20–1000 μM) by competitive assay of a porcine odor-binding protein. This aldehyde is highly toxic and poses significant risks to human health, such as cytotoxicity and cancer. The authors describe an optical biosensor for the detection of butyraldehyde in liquid samples. 27

[0016] Carla Silva et al. (2014), “Odor-binding proteins: a biotechnological tool for odor control,” disclosed the application of porcine odor-binding proteins (OBPs) for releasing fragrances from cotton fabrics to mask smoky odors. The authors demonstrated the functionalization of OBPs on fabrics. They tested the release of only one fragrance in textiles. In contrast to the work of Silva et al., this disclosure includes release mechanisms of various fragrances or other molecules in response to more efficient human perspiration. Furthermore, the subject matter of this disclosure is applicable to the textile and cosmetic fields.

[0017] Paolo Pelosi et al. (2014) "Structure and Biotechnological Applications of Odor-Binding Proteins" disclosed the potential of OBP as a sensor for detecting the volatility and slow release of odor molecules.

[0018] Lei Han et al. (2014), in their paper "Operational Mechanism and Molecular Dynamics of the Pheromone-Binding Protein ASP1 Affected by pH," demonstrated that the pheromone-binding protein ASP1 binds odorants at low pH and dissociates in response to pH changes. The authors described the potential benefits of this research in biotechnology and agriculture. The results were determined by molecular docking and kinetic simulations.

[0019] Alberto Mazzini et al. (2007) disclosed the structure of bovine odor-binding protein (OBP) under neutral and acidic pH conditions through molecular simulations in their work on "dissociation and unfolding of bovine odor-binding protein at acidic pH".

[0020] Mariella Parisi et al. (2003), “Unfolding and Refolding of OBP Proteins in Guanidine Hydrochloride: An Equilibrium Study at Neutral pH,” disclosed the denaturing role of guanidine hydrochloride (a well-known dissociation agent) in protein folding / unfolding. The aim of this fundamental study was to understand the structure of OBP proteins, particularly their unfolding and refolding processes.

[0021] Document WO 0123890A1 discloses a detector array based on sensing elements within a solid support for gaseous clinical samples or cell extracts. This utilizes an immunoassay of viral peptides.

[0022] Document EP0335654A3 ​​discloses a method for gene-isolated odor-binding proteins from rats and a method for protein production.

[0023] Document WO2001012806A3 describes OBPII as a fixative for hydrophobic ligands, such as odors that can be used in personal hygiene, agri-food systems, and for nutritional and therapeutic purposes.

[0024] These facts are disclosed to illustrate the technical problem addressed by this disclosure. Summary of the Invention

[0025] This disclosure relates to natural odor-binding protein (OBP-I), particularly porcine OBP-I (SEQ.ID NO.1) and OBP fused with linker GQ20x and KP peptide (OBP::GQ). 20 The adsorption and dissociation mechanisms of ::KP (SEQ.ID NO.21) are studied. Due to the high content of aspartic acid and glutamic acid residues, these proteins have a negative charge of approximately -20 (pH 7.4). The isoelectric points of these proteins are between 4.08 and 4.65. 26

[0026] In one implementation, the scheme disclosed herein could have a significant impact on human social life related to perspiration issues. The system offers several advantages, including the use of biomimetic cosmetic bio-ingredients (a green scheme) without harming the ecosystem.

[0027] The mechanism disclosed here reveals that odor-binding proteins, particularly porcine odor-binding protein (OBP-I), exhibit high affinity (adsorption) for fragrances at 37°C in 50 μM Tris-HCl pH 7.5 buffer. The affinity constant (Ka) of OBP-I is 4.00 ± 0.03 μM. Conversely, OBP-I exhibits the opposite mechanism: even at different pH levels (range 4.0–8.5, Table 2), fragrances dissociate from their binding sacs upon exposure to sweat (perspiration), and the Ka decreases (0.20 ± 0.02 μM). Similarly, OBP::GQ... 20 ::KP exhibits a high affinity for fragrance in buffer solution at 37°C (Ka = 4.00 ± 0.04 μM), which decreases in the presence of electrolyte solutions such as sweat (Ka = 0.59 ± 0.01 μM). Therefore, OBP exhibits a decreased affinity upon contact with sweat, under which condition fragrance is released.

[0028] Surprisingly, compared to the presence of buffer, OBP::GQ 20 ::KP (SEQ ID NO. 21) showed a fragrance release of more than 6.8 times in the presence of sweat. These values ​​are superior to those reported in the prior art, particularly superior to those for OBP::GQ. 20 The value reported by ::CBM (SEQ ID NO.22) indicates that the release mechanism shows a 1.3-fold increase in fragrance release in the presence of sweat. 25

[0029] The adsorption and dissociation mechanism of swine odor-binding proteins can be repeated.

[0030] Human sweat can be used as an initiator for the release / dissociation of fragrance from OBP-I. Therefore, the subject matter of this disclosure can be used in skin care products as well as textile products, particularly clothing.

[0031] In one embodiment, this disclosure relates to a protein having an amino acid sequence similar to that of mammalian odor-binding proteins, which will be incorporated into formulations for cosmetic or textile applications.

[0032] In one implementation, the natural form of the odor-binding protein may be derived from pigs, humans, dogs, cats, rats, mice, cattle, wild boars, pandas, Chinese hamsters, Meishan pigs, guinea pigs, Tibetan pigs, horses, dolphins, and chimpanzees.

[0033] In one aspect of this disclosure, the application of the subject matter of the invention may be based on the release of odor molecules from odor-binding proteins triggered by an electrolyte solution at body temperature.

[0034] In one embodiment, the electrolyte solution refers to a solution with a NaCl concentration higher than 9.5 g / L, particularly a solution with a NaCl concentration in the range of 9.5 to 45 g / L. Preferably, the electrolyte solution is human sweat, pet sweat, saline solution, or micelle solution.

[0035] In one implementation, human sweat may contain water, lactic acid, urea, and minerals such as sodium, potassium, calcium, and magnesium.

[0036] In one implementation, cosmetic applications may be used for skin and hair care. Skin care applications may be related to OBP in specific formulations of skin creams, lipsticks, lip balms and face mask powders, face creams and body creams, skin cleansers, primers, and foundations.

[0037] In another implementation, hair care applications may be related to OBP formulated in mascara, shampoo, hair serum, hair mask, conditioner, or hair dye.

[0038] This disclosure relates to a release composition comprising an isolated or artificial protein having at least 90% identity with an amino acid sequence selected from the following list: SEQ.ID NO.1, SEQ.ID NO.2, SEQ.ID NO.3, SEQ.ID NO.4, SEQ.ID NO.5, SEQ.ID NO.6, SEQ.ID NO.7, SEQ.ID NO.8, SEQ.ID NO.9, SEQ.ID NO.10, SEQ.ID NO.11, SEQ.ID NO.12, SEQ.ID NO.13, SEQ.ID NO.14, SEQ.ID NO.15, SEQ.ID NO.16, SEQ.ID NO.17, SEQ.ID NO.18, SEQ.ID NO.19, SEQ.ID... NO.20, SEQ.ID NO.21, or mixtures thereof, preferably 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or identical; the active agent is selected from a list including: deodorants, natural fragrances, perfumes, humectants, or mixtures thereof; wherein the active agent is bound to the protein; and wherein the protein releases the active agent in the presence of an electrolyte solution at a temperature between 10 and 60°C.

[0039] In one embodiment, the releasing composition comprises an isolated or artificial unmodified protein having at least 90% identity with an amino acid sequence selected from the following list: SEQ.ID NO.1, SEQ.ID NO.2, SEQ.ID NO.3, SEQ.ID NO.4, SEQ.ID NO.5, SEQ.ID NO.6, SEQ.ID NO.7, SEQ.ID NO.8, SEQ.ID NO.9, SEQ.ID NO.10, SEQ.ID NO.11, SEQ.ID NO.12, SEQ.ID NO.13, SEQ.ID NO.14, SEQ.ID NO.15, SEQ.ID NO.16, SEQ.ID NO.17, SEQ.ID NO.18, SEQ.ID NO.19, SEQ.ID NO.20, SEQ.ID NO.21, or mixtures thereof, preferably 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or identical.

[0040] Sequence alignment methods used for comparison are well known in the art, including GAP, BESTFIT, BLAST, FASTA, and TFASTA. GAP uses the algorithm of Needleman and Wunsch ((1970) J Mol Biol 48:443-453) to find global (overall) alignments between two sequences, maximizing the number of matches and minimizing the number of gaps. The BLAST algorithm (Altschul et al. (1990) J Mol Biol 215:403-10) calculates the percentage of sequence identity and performs statistical analysis on the similarity between two sequences. Software for performing BLAST analysis is publicly available from the National Center for Biotechnology Information (NCBI). The global percentage of similarity and identity can also be determined using one of the methods available in the MatGAT software package (Campanella et al., BMC Bioinformatics. July 10, 2003; 4:29. MatGAT: Applications for generating similarity / identity matrices from protein or DNA sequences). Minor manual editing can be performed to optimize alignments between conserved motifs, as will be apparent to those skilled in the art. Sequence identity values ​​expressed as a percentage in the subject matter of this invention were determined using BLAST and default parameters across the entire amino acid sequence.

[0041] In one embodiment, the composition of the subject matter of the present invention comprises 0.01 to 5000 μM of unmodified protein.

[0042] In one embodiment, the composition of the subject matter of the present invention comprises 0.01 to 5000 μM of protein.

[0043] In another embodiment, the releasing composition comprises 0.1 μM to 2 M of an active agent, preferably 0.2 μM to 1 M.

[0044] In one embodiment, in water or a buffer solution, preferably Tris-HCl, phosphate solution, and / or phosphate-buffered saline, the protein has an affinity constant of 1-4.5 μM for the active agent. In another embodiment, in an electrolyte solution, preferably in sweat, the protein has an affinity constant for the active agent in the range of 0.1-0.99 μM.

[0045] This disclosure relates to a fragrance-releasing composition comprising 0.01 to 5000 μM of an isolated or artificial protein, the isolated or artificial protein having at least 90% identity with an amino acid sequence selected from the following list: SEQ.ID NO.1, SEQ.ID NO.2, SEQ.ID NO.3, SEQ.ID NO.4, SEQ.ID NO.5, SEQ.ID NO.6, SEQ.ID NO.7, SEQ.ID NO.8, SEQ.ID NO.9, SEQ.ID NO.10, SEQ.ID NO.11, SEQ.ID NO.12, SEQ.ID NO.13, SEQ.ID NO.14, SEQ.ID NO.15, SEQ.ID NO.16, SEQ.ID NO.17, SEQ.ID NO.18, SEQ.ID NO.19, SEQ.ID NO.20, SEQ.ID... NO. 21 or mixtures thereof; 0.1 μM to 2 M of an active agent selected from a list including: deodorants, natural fragrances, perfumes, humectants or mixtures thereof; wherein the active agent is bound to and / or embedded in a protein; and wherein the protein releases the active agent in the presence of an electrolyte solution at a temperature between 10-70°C, preferably between 10-60°C; wherein the affinity constant of the protein for the active agent in water is in the range of 1-4.5 μM; wherein the molecular weight of the active agent is 20 to 1000 g / mol; wherein the electrolyte solution is sweat, saline or micelle water.

[0046] In one embodiment, the molecular weight of the active agent is between 20 and 1000 g / mol, preferably between 75 and 300 g / mol. In another embodiment, the active agent is a fragrance molecule. In yet another embodiment, the bioactive agent comprises a functional group selected from aromatics, aldehydes, or alcohols. In still another embodiment, the active agent is a fragrance molecule selected from the list of molecules included in Table 1.

[0047] Table 1 - List of spices and their properties.

[0048]

[0049]

[0050] In one implementation, the release of the active agent occurs between 30 seconds and 24 hours.

[0051] In one embodiment, the pH of the electrolyte solution is between 4.0 and 8.5. In another embodiment, the electrolyte solution is sweat, saline, or micelle water, preferably human sweat or pet sweat.

[0052] In one embodiment, the unmodified protein is stable in polar and nonpolar solvents (including methanol, butanol, benzene, ethanol, and undecanool) and buffer solutions (preferably Tris-HCl, phosphate, or phosphate-buffered saline (PBS)). In another embodiment, the unmodified protein is also stable at temperatures between 18 and 70°C, preferably between 18 and 60°C, and at a pH range of 4.0 to 10.0.

[0053] In one embodiment, the protein is stable in polar and nonpolar solvents (including methanol, butanol, benzene, and undecyl alcohol) and buffer solutions (Tris-HCl, phosphate, PBS). In another embodiment, the protein is also stable at temperatures between 18 and 70°C, preferably between 18 and 60°C, and at a pH range of 4.0 to 10.0.

[0054] In one implementation, the release of the active agent from the protein occurs at 20-40°C.

[0055] In one embodiment, the composition further comprises glycerol, erythritol, arabinitol, sorbitol, mannitol, xylitol, mannitol, glyceryl glucoside, glucose, fructose, sucrose, trehalose, isofluoroside, dextran, fructan, polyethylene glycol, chloride, citrate, sulfate, acetate, or phosphate, or mixtures thereof.

[0056] One aspect of this disclosure includes kits or articles comprising the compositions described in the subject matter of this invention. In one embodiment, the articles comprising the compositions may be selected from a list including: fabrics, textiles, fibers, clothing, scarves, hats, gloves, socks and headscarves, shoes, insoles, bags, handbags, detergents, creams, lotions, foams, perfumes, softeners, aerosols, deodorants, lipsticks, lip balms, face mask powders, face creams and body creams, skin cleansers, primers, foundations, shampoos, hair serums, hair masks, conditioners, or hair dyes.

[0057] This disclosure also relates to the use of the fragrance-releasing compositions described in the subject matter of this invention in cosmetics, preferably as cosmetic agents / compositions, more preferably as skin care or hair care; and the use of said compositions in the textile industry.

[0058] This disclosure also relates to the use of fragrance-releasing compositions as deodorants / compositions. Attached Figure Description

[0059] The following figures provide preferred embodiments for illustrating this disclosure and should not be construed as limiting the scope of the invention.

[0060] Figure 1Schematic diagram of SDS-PAGE gel electrophoresis (A) under reducing conditions and circular dichroism (CD) spectrum (B) of natural porcine odor-binding protein. Mw: Precision Plus Protein™ standard (BioRad). Detailed Implementation

[0061] This disclosure relates to a method for manufacturing a flavor / protein complex and natural flavor-binding protein (OBP-I), particularly porcine OBP-I, and its connection with GQ. 20 The adsorption and dissociation mechanism of natural proteins fused with KP peptides. This mechanism involves the release of active agents, preferably odor molecules (or fragrances), in response to human sweat.

[0062] This disclosure has a significant impact on the textile and cosmetic fields, particularly on the release of fragrances from lotion and cream-based products and textile fabrics, and provides a green solution.

[0063] In one embodiment, the resulting odor-binding proteins and fragrance / protein complexes are completely soluble and stable in different solvents (such as methanol, butanol, benzene, and undecyl alcohol), different temperature ranges (18-60°C), and different pH ranges (4.0-10.0). 12,27-29

[0064] In another embodiment, the odor molecule and OBP-I or OBP::GQ 20 The mixture of ::KP proteins showed improved results in terms of affinity constants in buffered solutions and sweat (Table 2). In particular, the lower Ka in sweat forced the use of OBP proteins when a sweat-induced response was expected. Notably, the protein adsorption and dissociation mechanisms were reversible. Compared to other fusion proteins based on pig odor-binding proteins, the disclosed protein release in response to human sweat at different pH ranges (pH 4.0–8.5) was more than 20-fold to 6.8-fold (for OBP-1 and OBP::GQ, respectively). 20 The odor molecules of ::KP (Table 2). Therefore, fragrance release occurs in response to sweat and is independent of the pH of sweat in each individual. Furthermore, fragrance release occurs over a period of at least 0.5–24 hours.

[0065] In one embodiment, a variety of active agents, including deodorants, natural fragrances, perfumes, moisturizers, or mixtures thereof, can be used in the formation of the complex, thereby allowing for a wide range of cosmetic applications. In particular, pleasant odor molecules (of different sizes and shapes) exhibit a strong affinity for odor-binding proteins, especially porcine odor-binding proteins.

[0066] In one embodiment, the odor molecules used in this disclosure belong to different functional groups (aromatic, aldehyde, or alcohol). In another embodiment, the odor molecules include molecules with molecular weights ranging from 20,00 to 1,000,000 g / mol and concentrations varying from 0.2 to 2,000 μM.

[0067] In one embodiment, the molecular weight of the odor molecule is between 75 and 300 g / mol.

[0068] In one embodiment, the system effectively responds to human sweat, releasing fragrance over time. Importantly, the system does not respond to the presence of water in the body, thus giving the subject matter presented in this disclosure specificity and robustness. Without this selectivity, if the system were responsive to water, the OBP protein would immediately release odor molecules upon contact with the skin.

[0069] Example:

[0070] In one implementation, natural pig odor-binding protein (OBP-I) and glycine-glutamine in the spacer region are repeated 20 times (GQ). 20 ) and fused with the carbohydrate binding module OBP-I (OBP::GQ) 20 The protein (::CBM) was cloned into plasmid pET28a and transformed into *E. coli* BL21(DE3). The protein was expressed and purified using nickel magnetic beads, which are specific for the His tag present at the N-terminus of the protein. Under reducing conditions, 10 μM of the protein was loaded onto a sodium dodecyl sulfate and polyacrylamide (SDS-PAGE) gel electrophoresis. The same concentration was used to determine the protein structure by circular dichroism (CD) spectroscopy.

[0071] The protein purified in the laboratory revealed a high level of purity (observed by SDS-PAGE gel). Figure 1 -A) and the secondary structure in the barrel, which was determined by circular dichroism spectroscopy analysis ( Figure 1 This is a result of the presence of a large number of β-sheets in -B).

[0072] In one embodiment, the pure odor-binding protein is lyophilized and used in further procedures. To determine the affinity of the odor-binding protein for odor molecules, 1-aminoanthracene (1-AMA) is used as an odor model molecule. An increased concentration of the fluorescent ligand model 1-aminoanthracene (1-AMA) is added to 1 μM of the protein, and after 1 hour at 37°C, the formation of the ligand / protein complex is quantified by fluorescence emission at 481 nm (excited at 295 nm). 30 The dissociation constant (Kd) was determined from a graph of fluorescence intensity versus ligand concentration, obtained using a standard nonlinear regression method, as described by Malpeli et al. (1998).31 The affinity behavior of the protein in the presence of sweat solution was determined by competitive fluorescence assay. Here, 1 μM of the protein was mixed with 2 μM 1-AMA and incubated at 37 °C for 1 hour. After this time, a larger volume of sweat solution was added to the complex and incubated under the same conditions.

[0073] In one embodiment, the sweat solution is prepared according to AATCC Method 15-2009, "Colorfastness to Perspiration". The pH of the prepared solution varies between 4.0 and 8.5. Based on its composition, the sweat solution is also considered an electrolyte solution.

[0074] In another implementation, fluorescence emission at 481 nm (excitation at 295 nm) is recorded and the dissociation constant (Kd) is calculated. The binding constant (Ka) is calculated using the formula Kd = 1 / Ka.

[0075] In one embodiment, fragrance release is quantified by gas chromatography-mass spectrometry (GC-MS). Increasing concentrations of fragrance are used in different vials, and the fragrance in the headspace is quantified by performing a calibration curve (peak area versus fragrance concentration). The fragrance is incubated with odor-binding proteins at 37°C. A sweat solution is added, and fragrance release is measured after several time periods of sweat exposure (0.5–24 hours).

[0076] In one implementation scheme, as comparative data, porcine odor-binding protein and spacer region GQ 20 It is fused with a carbohydrate binding module (CBM), as previously reported. 25 CBM via endoglucanase C from Cellulomonas fimi N1 The fusion of (PDB ID 1ULP) and OBP exhibits specific affinity for cotton. When added to a sweat solution, the modified protein showed a high binding constant (Ka = 4.17 ± 0.05 μM), which decreased for Ka = 3.16 ± 0.02 μM. Natural OBP-I (SEQ ID No. 1) and OBP::GQ... 20 ::KP (SEQ ID NO.21) shows a match with OBP::GQ 20 The binding constants obtained for ::CBM (SEQ ID NO.22, Ka = 4.17 ± 0.05) were very similar (Ka = 4.00 ± 0.03 μM). However, the affinity constants for natural proteins obtained with the addition of sweat solution (Ka = 0.20 ± 0.02 μM) and OBP::GQ were significantly different. 20::KP (Ka = 0.59 ± 0.01 μM) had a significant effect. Compared with the quantification of the protein fused with CBM (SEQ ID NO 22), only a 1.3-fold reduction was confirmed (Ka = 3.16 ± 0.02, Table 2), and a significant decrease in affinity was observed, which was 20-fold when using native OBP (SEQ ID NO. 1) and when using OBP::GQ. 20 The concentration of KP (SEQ ID NO. 21) was 6.8 times higher. Therefore, the fragrance release of OBP-1 and OBP fused with KP is clearly a response to sweat.

[0077] Table 2. Affinity constants (Ka) of natural OBP-I (SEQ ID NO.1) and fusion proteins based on OBP, SEQ ID NO.21, and SEQ ID NO.22. SEQ ID NO.22 was used as comparative data. Values ​​are the average of two independent experiments at 37°C.

[0078]

[0079] In one implementation, to release fragrance in the presence of sweat, the following protein sequences can be incorporated into different substrates. In this regard, substrates can be selected from a list including: textiles, fabrics, skin care products, hair care products, etc.

[0080] protein sequence list

[0081] Protein sequences are described by single-letter codes for amino acids. The codes are as follows:

[0082]

[0083]

[0084] Pig OBP (PDB ID 1DZK) - SEQ ID NO.1

[0085] QEPQPEQDPFELSGKWITSYIGSSDLEKIGENAPFQVFMRSIEFDDKESKVYLNFFSKENGICEEFSLIGTKQEGNTYDVNYAGNNKFVVSYASETALIISNINVDEEGDKTIMTGLLGKGTDIEDQDLEKFKEVTRENGIPEENIVNIIERDDCPA

[0086] Human OBP IIa (UniProt ID Q9NY56)-SEQ ID NO.2

[0087] MKTLFLGVTLGLAAALSFTLEEEDITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGNLEATFTFMREDRCIQKKILMRKTEEPGKFSAYGGRKLIYLQELPGTDDYVFYCKDQRRGGLRYMGKLVGRNPNTNLEALEEFKKLVQHKGLSEEDIFMPLQTGSCVLEH

[0088] Human OBPIIb (UniProt ID Q9NPH6) - SEQ ID NO.3

[0089] MKTLFLGVTLGLAAALSFTLEEEDITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGKLEATFTFMREDRCIQKKILMRKTEEPGKYSAYGGRKLMYLQELPRRDHYIFYCKDQHHGGLLHMGKLVGRNSDTNREALEEFKKLVQRKGLSEEDIFTPLQTGSCVPEH

[0090] Mouse OBP (UniProt ID OBP1A) - SEQ ID NO.4

[0091] MAKFLLLALTFGLAHAAMEGPWKTVAIAADRVDKIERGGELRIYCRSLTCEKECKEMKVTFYVNENGQCSLTTITGYLQEDGKTYKTQFQGNNRYKLVDESPENLTFYSENVDRADRKTKLLFILGHGPLTSEQKEKFAELAEEKGIPAGNIREVLITDYCPE

[0092] Mouse OBP2A (UniProt ID Q8K1H9) - SEQ ID NO.5

[0093] MKSLLLTILLLGLVAVLKAQEAPPDDLVDYSGIWYAKAMVHNGTLPSHKIPSIVFPVRIIALEEGDLETTVVFWNNGHCREFKFVMKKTEEPGKYTAFHNTKVIHVEKTSVNEHYIFYCEGRHNGTSSFGMGKLMGRDSGENPEAMEEFKNFIKRMNLRLENMFVPEIGDKCVESD

[0094] Mouse OBP1B (UniProt ID A2AEP0) - SEQ ID NO.6

[0095] MMVKFLLLALVFGLAHVHAHDHPELQGQWKTTAIMADNIDKIETSGPLELFVREITCDEGCQKMKVTFYVKQNGQCSLTTVTGYKQEDGKTFKNQYEGENNYKLLKATSENLVFYDENVDRASRKTKLLYILGKGEALTHEQKERLTELATQKGIPAGNLRELAHEDTCPE

[0096] Rat OBP (PDB ID 3FIQ) - SEQ ID NO.7

[0097] HHENLDISPSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYFHVLKKTDDIIFFHNVNVDESGKETNVILVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTCNQ

[0098] Rat OBP (PDB ID 3ZQ3) - SEQ ID NO.8

[0099] MRGSHHHHHHTDPEEASFERGNLDVDKLNGDWFSIVVASDKREKIEENGSMRVFVQHIDVLENSLGFTFRIKENGVCTEFSLVADKTAKDGEYFVEYDGENTFTILKTDYDNYVMFHLVNVNNGETFQLMELYGRTKDLSSDIKEKFAKLCVAHGITRDNIIDLTKTDRCLQA

[0100] Rat OBP (UniProt ID P08937) - SEQ ID NO.9

[0101] MVKFLLIVLALGVSCAHHENLDISPSEVNGDWRTLYIVADNVEKVAEGGSLRAYFQHMECGDECQELKIIFNVKLDSECQTHTVVGQKHEDGRYTTDYSGRNYFHVLKKTDDIIFFHNVNVDESGRRQCDLVAGKREDLNKAQKQELRKLAEEYNIPNENTQHLVPTDTCNQ

[0102] Bovine OBP (PDB ID 10BP) - SEQ ID NO.10

[0103] AQEEEAEQNLSELSGPWRTVYIGSTNPEKIQENGPFRTYFRELVFDDEKGTVDFYFSVKRDGKWKNVHVKATKQDDGTYVADYEGQNVFKIVSLSRTHLVAHNINVDKHGQTTELTGLFVKLNVEDEDLEKFWKLTEDKGIDKKNVVNFLENEDHPHPE

[0104] Wild boar OBP (PDB ID 1GM6) - SEQ ID NO.11

[0105] HKEAGQDVVTSNFDASKIAGEWYSILLASDAKENIEENGSMRVFVEHIRVLDNSSLAFKFQRKVNGECTDFYAVCDKVGDGVYTVAYYGENKFRLLEVNYSDYVILHLVDVNGDKTFQLMEFYGRKPDVEPKLKDKFVEICQQYGIIKENIIDLTKIDRCFQLRGSGGVQESSAE

[0106] Panda OBP (PDB ID 5NGH) - SEQ ID NO.12

[0107] HEEGNDVRRNFDVSKISGYWYSVLLASDVREKTEENSSMRVFVNHIEVLSNSSLLFNMHIKVDGKCTEIALVSDKTEKDGEYSVEYDGYNVFRIVETDYTDYIIFHLVNFKEKDSFQMMELSAREPDTSEEVRKRFVEYCQKHGIVKENIFDLTEVDRCLQARGSEKA

[0108] Chinese hamster OBP (Ensembl ID ENSCGRP00015014591.1) - SEQ ID NO.13

[0109] MVKFLLLAFALSVSCAHHKIPEISPSEVDGKWRTLYIGADNTEKVIQGGPLRAYFRHMECSDECQTLTITFNTKEEGKCQTHTVVGRKDEDGQYKTGFSGNNDFHVVEKADGIIIFHNVNVDSSGKKTNVILVAGKGKSLSKEQKERLENIAKEFDISKENIQHLVPTDTCDQ

[0110] Meishan pig OBP (Ensembl ID ENSSSCP00040041163.1) - SEQ ID NO.14

[0111] MKSLLLSLVLGLVCAQEPQPEQDPFVLSGKWITSYIGSSDLEKIGENAPFQVFMRSIEFDDKESKVYLNFFSKENGICEEFSLIGTKQEGNTYDVNYAGNNKFVVSYASETALIISNINVDEEGDKTIMTGLLGKGTDIEDQDLEKFKEVTRENGIPEENIVNIIERDDCPAK

[0112] Horse OBP (Ensembl ID ENSECAP00000000103.2) - SEQ ID NO.15

[0113] MQILLLSLVLGVVCAVQEPQSETDYSLFSGEWNTIYIGSSNIEKISENGPFRILLRRLDLDSAGDRIIYTFFLKVNGQCTKISSLAIKTEENTYVCHYAGKNKFEILHLSKTAIIIDIVNEDEGGLVTKMVALVGMLGDIQKEDIEKFKEVAKEKEIPEENIVNIINIDDCPTSE

[0114] Guinea pig OBP ((Ensembl ID ENSCPOP00000016393.2) - SEQ ID NO.16

[0115] MQILLLALTIGLAYAHQTLDPSEINGQWHTISIAADNVEKIGEGGPLRGYFHNLHCYDGCKNIGLTFYVKLDGNCQRFDVLGAKQEDSDVYVAQYSGTNHFEVIGKKEDAIAFYNHNTDETGKETKMIVVVARRDSLTEEEQQKLQEVAGEKGIPKDNIRYFRERDTCAQ

[0116] Dog OBP ((Ensembl ID ENSCAFP00040020992.1) - SEQ ID NO.17

[0117] MKILLLCLILVLACDAHLPLPNVLTQVSGPWKTLYVSSNNLDKIAENGPFRIYIRRINVDIPRLKILFSFFVKVDGECVEKSVEASIGQDNLINAHYAGGNYHQILDVTPNALIGYIVNVDDKGRITKLASLVGRGAHVNEEDIAKFKKLSREKGIPEENIIYLGDTDNCPNHE

[0118] Tibetan pig OBP (Ensembl ID ENSSSCP00015013912.1) - SEQ ID NO.18

[0119] MKSLLLSLVLGLVCAQEPQPEQDPFELSGKWITSYIGSSDLEKIGENAPFQVFMRSIEFDDKESKVYLNFFSKENGICEEFSLTGTKQEGNTYDVNYAGNNKFVVSYASETALIIANINVDEEGDKTIMTGLLGKGTDIEDQDLEKFKEVTRENGIPEENIVNIIERDDCPAK

[0120] Domestic cat OBP (Ensembl ID ENSFCAP00000053707.1) - SEQ ID NO.19

[0121] RSCVIHLQCLPTGCLFSALHNGLPDGRLPLPDGRLPLPDGRLPLPDSRLPLPDGRLPLPDGRLPLPDGRLPLPDGRLPLPDGRLPLPDGRLPLPDGRLPLPDGRLPLPEGRLPLPDSHPPLQDNLTQLSGEWNTLLVAATNVDKISNGPFHGYICKVDVDVTNGTVVFNFSVMMNGRCTEKSAVGTIGRDKFINIGSMNQNLFNLFSVTSNTIAINVNTRRNTTKAFALLDTNGNIFNIGYDSLGSLIIHTANVDTAGQTTQVFALLGKRLHPDDNDFAKFRELMRENNIpEENLIDMSKTEKCPKKEKGTNPS

[0122] Chimpanzee OBP (Ensembl ID ENSPTRP00000048681.3) - SEQ ID NO.20

[0123] MALLLLSLGLSLITAQEFDPRNVMQRNYNMARVSGVWYSIFMADDLNRIKENGDLRVFVQNIEHLKNGSLKFDFEYMVQGECVAVVVVCEKTEKNGEYSINYEGQNTVAVSETDYRLFITFHLQNFRNGTETHTLALYETCKKYGLGSQNIINLTNKDPCYSKHYRSPPRPPMRE

[0124] OBP::GQ 20 ::KP (Recombinant Protein) - SEQ ID NO.21

[0125] QEPQPEQDPFELSGKWITSYIG5SDLEKIGENAPFQVFMRSIEFDDKESKVYLNFFSKENGICEEFSLIGTKQEGNTYDVNYAGNNKFVVSYASETALIISNINVDEEGDKTIMTGLLGKGTDIEDQDLEKFKEVTRENGIPEENIVNIIERDDCPAGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGGVCGPSPPCITT

[0126] OBP::GQ 20 ::CBM (Recombinant Protein) - SEQ ID NO.22

[0127] QEPQPEQDPFELSGKWITSYIGSSDLEKIGENAPFQVFMRSIEFDDKESKVYLNFFSKENGICEEFSLIGTKQEGNTYDVNYAGNNKFVVSYASETALIISNINVDEEGDKTIMTGLLGKGTDIEDQDLEKFKEVTRENGIPEENIVNIIERDDCPAGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQGQASPIGEGTFDDGPEGWVAYGTDGPLDTSTGALCVAVPAGSAQYGVGVVLNGVAIEEGTTYTLRYTATASTDVTVRALVGQNGAPYGTVLDTSPALTSEPRQVTETFTASATYPATPAADDPEGQIAFQLGGFSADAWTLCLDDVALDSEVEL

[0128] References

[0129] (1) Flower, D.R. The lipocalin protein family: structure and function. Biochem. J. 1996, 318, 1 - 14.

[0130] (2) Flower, D.R. Beyond the superfamily: the lipocalin receptors. Biochimica et biophysica acta 2000, 1482, 327 - 336.

[0131] (3) Breer, H. Olfactory receptors: molecular basis for recognition and discrimination of odors. Analytical and bioanalytical chemistry 2003, 377(3), 427 - 33, DOI: 10.1007 / s00216 - 003 - 2113 - 9.

[0132] (4)Tegoni,M.;Pelosi,P.;Vincent,F.;Spinelli,S.;Campanacci,V.;Grolli,S.;Ramoni,R.;Cambillau,C.Mammalian odorant binding proteins.Biochimica etbiophysica acta 2000,1482,229-240.

[0133] (5)Bignetti,E.;Cattaneo,P.;Cavaggioni,A.;Damiani,G.The pyrazine-binding protein and olfaction.Comp.Biochem.Physiol.1988,90B,1-5.

[0134] (6)Pevsner,J.;Hou,V.;Snowman,A.M.;Snyder,S.H.Odorant-binding protein:characterization of ligand binding.The Journal of biologicaI chemistry 1990,265(11),6118-6125.

[0135] (7)Bignetti,E.;Cavaggioni,A.;Pelosi,P.;Persaud,K.C.;Sorbi,R.T.;Tirindelli,R.Purification and characterisation of an odorant-binding proteinfrom cow nasal tissue.Eur.J.Biochem.1985,149,227-231.

[0136] (8)Dal Monte,M.;Andreini,l.;Revoltella,R.;Pelosi,P.Purification andcharacterizationof two odorant-binding proteins from nasal tisue of rabbitand pig.Comp Biochem Physiol 1991,99B(2),445-451.

[0137] (9)Garibotti,M.;Navarrini,A.;Pisanelli,A.M.;Pelosi,P.Three Odorant-binding Proteins from Rabbit NasaI Mucosa.Chemical senses 1997,22(4),383-390.

[0138] (10)Laza r,J.;Greenwood,D.R.;Rasmussen,L.E.L.;Prestwich,G.D.Molecularand Functional Characterization of an Odorant Binding Protein of the AsianElephant,Elephas maximus:Implications for the Role of Lipocalins in MammalianOlfaction.Biochemistry 2002,41,11786-11794.

[0139] (11)Pes,D.;Dal Monte,M.;Ganni,M.;Pelosi,P.Isolation of two odorant-binding proteins from mouse nasal tissue.Comp.Biochem.Physiol.1992,103B(4),1011-1017.

[0140] (12)Lobel,,D.;Jacob,M.;Volkner,M.;Breer,H.Odorant of differentchemica classes interact with distinct odorant binding proteinSubtypes.Chemical senses 2002,27,39-44.

[0141] (13)Briand,L.;Eloit,C.;Nespoulous,C.;Bezirard,V.;Huet,J.-C.;Henry,C.;Blon,F.;Trotier,D,;Permollet,J.-C.Evidence of an Odorant-Binding Protein inthe Human Olfactory Mucus:Location,Structural Characterization,and Odorant-Binding Properties.Biochemistry 2002,41,7241-7252.

[0142] (14)Pelosi,P.Odorant-Binding Proteins:Structural Aspects.In AnnalsNew York academy of sciences;Olfaction and Taste XII:an internationalsymposium,1998;pp 281-293.

[0143] (15)spinelli,S.;Ramoni,R.;Grolli,S.;Bonicel,J.;Cambillau,C.;Tegoni,M.The structure of the Monomeric Porcine Odorant Binding Protein Sheds Lighton the Domain Swapping Mechanism.Biochemistry 1998,37,7913-7918.

[0144] (16)Perduca,M.;Mancia,F.;DeI Giorgio,R.;Monaco,H.L.Crystal Structureof a Truncated Formof Porcine Odorant-Binding Protein.Proteins:Structure,Function,and Genetics 2001,42,201-209.

[0145] (17)Cave,J.W.;Wickiser,J.K.;Mitropoulos,A.N.Progress in thedevelopment of olfactory-based bioelectronic chemosensors.Biosensors&bioelectronics 2019,123,211-222,DOI:10.1016 / j.bios.2018.08.063.

[0146] (18)Pelosi,P.;Mastrogiacomo,R.;lovinella,l.;Tuccori,E.; Persaud,K.C.Structure and biotechnological applications of odorant-bindingproteins.Applied microbiology and biotechnology 2014,98(1),61-70,DOI:10.1007 / s00253-013-5383-y.

[0147] (19)Mulla,M.Y.;Tuccori,E.;Magliulo,M.;Lattanzi,G.;Palazzo,G.;Persaud,K.;Torsi,L.Capacitance-modulated transistor detects odorant binding proteinchiral interactions.Nature communications 2015,6,6010,DOI:10.1038 / ncomms7010.

[0148] (20)Paolini,S.;Tanfani,F.;Fini,C.;Bertoli,E.;Pelosi,P.Porcineodorant-binding protein:structural stability and ligand afinities measured byFourier-transform infrared spectroscopy and fluorescencespectroscopy.Biochimica et biophysica acta 1999,1431,179-188.

[0149] (21)Sorokowska,A.;Sorokowski,P.;Szmajke,A.Does Personality Smell?Accuracy of Personality Assessments Based on Body Odour.European Journal ofPersonality 2012,26(5),496-503,DOI:10.1002 / per.848.

[0150] (22)Ozeki,C.;Moro,O.A study of the suppression of body odourinelderly subjects by anti-fungal agents.lnternational journal of cosmeticscience 2016,38(3),312-8,DOI:10.1111 / ics.12295.

[0151] (23)Di Pietrantonio,F.;Cannata,D.;Benetti,M.;Verona,E.;Varriale,A.;Staiano,M.;D′Auria,S.Detection of odorant molecules via surface acoustic wavebiosensor array based on odorant-binding proteins.Biosensors&bioelectronics2013,41,328-34,DOI:10.1016 / j.bios.2012.08.046.

[0152] (24)Sankaran,S.;Khot,L.R.;Panigrahi,S.Biology and applications ofolfactory sensing system:A review.Sensors and Actuators B:Chemical 2012,171-172,1-17,DOI:10.1016 / j.snb.2012.03.029.

[0153] (25)Goncalves,F.;Ribeiro,A.;Silva,C.;Cavaco-Paulo,A.Release ofFragrances from Cotton Functionalized with Carbohydrate-Binding ModuleProteins.ACS Appl Mater lnterfaces 2019,DOI:10.1021 / acsami.9b08191.

[0154] (26)Kozlowski,L.P.IPc-lsoelectric Point caIcuIator.Biology direct2016,11(1),55,DOI:10.1186 / s13062-016-0159-9.

[0155] (27)Cennamo,N.;Di Giovanni,S.; Varriale,A.;Staiano,M.;DiPietrantonio,F.;Notargiacomo,A.;Zeni,L.;D′Auria,S.Easy to Use Plastic OpticalFiber-Based Biosensor for Detection of Butanal.PloS one 2015,10(3),e0116770,DOI:10.1371 / journal.pone.0116770.

[0156] (28)Capo,A.;Pennacchio,A.;Varriale,A.;D′Auria,S.;Staiano,M.Theporcine odorant-binding protein as molecular probe for benzene detection.PloSone 2018,13(9),e0202630,DOI:10.1371 / journal.pone.0202630.

[0157] (29)Vincent,F.;Ramoni,R.;Spinelli,S.;Grolli,S.;Tegoni,M.;Cambillau,C.Crystal structures of bovine odorant-binding protein in complex withodorant molecules.European journal of biochemistry 2004,271(19),3832-42,DOI:10.1111 / j.1432-1033.2004.04315.x.

[0158] (30)Goncalves,F.;Castro,T.G.;Nogueira,E.;Pires,R.;Silva,C.;Ribeiro,A.;Cavaco-Paulo,A.OBP fused with cell-penetrating peptides promotes liposomaltransduction.Colloids and surfaces.B,Biointerfaces 2018,161,645-653,DOI:10.1016 / j.colsurfb.2017.11.026.

[0159] (31)Malpeli,G.;Folli,C.;Cavazzini,D.;Sartori,G.;Berti,R.Purificationand Fluorescent Titration of Cellular Retinol-Binding Protein.In Methods inMolecular Biology;Redfern,C.P.F.,Ed.;1998;pp 111-122.

[0160] (32) Nogueira, E.; Mangialavori, IC; Loureiro, A.; Azoia, NG; Sárria, MP; Nogueira, P.; Freitas, J.; Harmark, J.; Shimanovich, U.; Rollet, Lacroix, G., Bernardes, G.J.L., Guebitz, G., Hebert, H., Moreira, A., Carmo, A.M., Rossi, JPFC, Gomes, A.C., Preto, A., Cavaco-Paulo, A. Peptide anchor for folate-targetedliposomal delivery. BiomacromoIecules 2015, 16(9), 2904-2910, DOI: 10.1021 / acs.biomac.5b00823.

[0161] (33) Goncalves, F.; Silva, C.; Ribeiro, A.; Cavaco-Paulo, A.1-AminoanthraceneTransduction into Liposomes Driven by Odorant-Binding Protein Proximity. ACSApplied Materials&lnterfaces 2018, DOI: 10.1021 / acsami.8b10158.

[0162] (34) Goncalves, F.; Castro, TG; Azoia, NG; Ribeiro, A.; Silva, C.; Cavaco-Paulo, A. Two Engineered OBPs with opposite temperature-dependent affinitiestowards 1-aminoanthracene. Scientific reports 2018, 8(1), 14844, DOI: 10.1038 / s41598-018-33085-8

[0163] The term “comprising” as used in this document is intended to indicate the presence of the stated feature, integer, step, or component, but does not exclude the presence or addition of one or more other features, integers, steps, components, or combinations thereof.

[0164] This disclosure should not be construed as a limitation on the described implementations in any way, and those skilled in the art will foresee a variety of possibilities for modifications thereto.

[0165] The above implementation methods are combinable.

[0166] The following claims further illustrate specific embodiments of this disclosure.

Claims

1. A fragrance-releasing composition comprising: 0.01-5000 μM of isolated or artificial proteins with the same amino acid sequence as SEQ. ID NO. 21; Surfactants of 0.1 μM to 2 M, wherein the surfactants are selected from a list including: deodorants, natural fragrances, perfumes, humectants or mixtures thereof; The active agent is bound to and / or embedded in the protein; and The protein releases the active agent in the presence of an electrolyte solution at a temperature of 10-70°C. The active agent has a molecular weight of 20 to 1000 g / mol; The electrolyte solution is sweat, saline, or micelle water; The electrolyte solution has a NaCl concentration of more than 9.5 g / L.

2. The composition according to claim 1, further comprising glycerol, erythritol, arabinitol, sorbitol, xylitol, mannitol, glycerol glucoside, glucose, fructose, sucrose, trehalose, isoflurane, dextran, fructan, polyethylene glycol, chloride, citrate, sulfate, acetate, or phosphate, or mixtures thereof.

3. Use of the composition according to any one of claims 1-2 as a hair care agent / composition.

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