Maotai-flavor round-based liquor polypeptide and its application in influencing liquor body flavor

CN117924413BActive Publication Date: 2025-07-08SHAOYANG UNIV
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Patent Information

Application Number
CN202410177805.7
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2024-02-08
Publication Date
2025-07-08
Estimated Expiration
2044-02-08

AI Technical Summary

Technical Problem

目前,对于白酒中内源性肽的生物活性报道也逐渐增多,但对多肽与风味物质的相互作用研究较少

Benefits of technology

[0007] The polypeptide SDAE can inhibit the volatilization of pyrazine substances, and the effects reach 10.44% respectively;

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Abstract

The present invention discloses polypeptide of sauce-flavor round base liquor and its application in influencing the flavor of liquor body, belonging to the field of liquor brewing. The present invention provides a preparation method of endogenous polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH in the first-round base liquor of sauce-flavor liquor. After synthesizing the polypeptides, gas chromatography was used to explore the interaction between the polypeptides and flavor substances (acids, esters, pyrazines) in sauce-flavor liquor, and it was found that the addition of polypeptide TRLF would significantly affect the volatility of alcohol, acid, and pyrazine flavor substances in sauce-flavor liquor, which will provide a direction for future research and further exploration of the binding mechanism between peptides and flavor substances in liquor.
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Description

Technical Field

[0001] The present invention relates to polypeptide of Maotai-flavor round base liquor and its application in influencing the flavor of liquor body, belonging to the field of liquor brewing. Background Art

[0002] The non-volatile components in liquor mainly include amino acids, reducing sugars, higher fatty acids, polyols, minerals, polypeptides, etc. Compared with the reports on volatile components, for a long time, the research on Chinese liquor has mainly focused on the types of microorganisms and the formation of flavor compounds during the fermentation process, and emphasized the qualitative and quantitative analysis of the final products. The research on non-volatile components in liquor is relatively less, and the reasons may be that the content of non-volatile components is very low, the extraction and separation efficiency is not high, and the detection limit of detection instruments is high, etc. However, liquor contains a large number of non-volatile trace components beneficial to human health, and active oligopeptides, as a class of endogenous health factors generated during the liquor brewing process, have received the favor of scientific researchers and liquor enterprises in recent years.

[0003] In addition to containing a large amount of starch, the grains used for liquor brewing are also rich in protein. In the micro-ecological pit environment, due to the degradation of protein in the brewing raw materials, the action of microorganisms in the fermented grains during the fermentation process, and the autolysis of microbial cells after the fermentation ends, the protein is decomposed to produce oligopeptides and even degraded into free amino acids. These non-volatile components such as endogenous oligopeptides and amino acids are dissolved in the ethanol-water system and distilled out during the subsequent distillation process of fermented grains. Therefore, the characterized trace components such as active oligopeptides and amino acids in liquor initially originate from the fermented grains in the micro-ecological pit. At present, the reports on the biological activities of endogenous peptides in liquor are also gradually increasing, but the research on the interaction between polypeptides and flavor substances is less. Summary of the Invention

[0004] The present invention provides a novel polypeptide Ser-Asp-Ala-Glu (SDAE), Thr-Arg-Leu-Phe (TRLF), Phe-Asp-His-Gly-Phe-Ala-Glu-Gln (FDHGFAEQ), Trp-Ala-Lys (WAK), Asn-Val-Leu-His (NVLH). This polypeptide interacts with flavor substances in Maotai-flavor liquor, and adding it to liquor can increase the content of flavor substances in the liquor.

[0005] The first object of the present invention is to provide a polypeptide, the amino acid sequence of which is Ser-Asp-Ala-Glu (SEQ ID NO.1: SDAE) or Thr-Arg-Leu-Phe (SEQ ID NO.2: TRLF) or Phe-Asp-His-Gly-Phe-Ala-Glu-Gln (SEQ ID NO.3: FDHGFAEQ) or Trp-Ala-Lys (WAK) or Asn-Val-Leu-His (SEQID NO.4: NVLH).

[0006] The polypeptide of the present invention has the following advantages:

[0007] The polypeptide SDAE can inhibit the volatilization of pyrazine substances, and the effects reach 10.44% respectively;

[0008] The polypeptide TRLF can inhibit the volatilization of acids, esters and pyrazine substances, and the effects reach 21.45%, 15% and 65.66% respectively;

[0009] The polypeptide FDHGFAEQ can inhibit the volatilization of esters and pyrazine substances, and the effects reach 4.16% and 1.35% respectively;

[0010] The polypeptide WAK can inhibit the volatilization of pyrazine substances, and the effects reach 16.49% respectively;

[0011] The polypeptide NVLH can inhibit the volatilization of acids and pyrazine substances, and the effects reach 9.24% and 35.35% respectively;

[0012] The interaction between the polypeptide TRLF and volatile flavor substances is the most obvious. There are interactions with the mixtures of acids, esters and pyrazines, and most of them show inhibition of their volatility.

[0013] This polypeptide has strong solubility and stability;

[0014] This polypeptide is derived from liquor. As an additive added to liquor products, it is safer while improving the flavor.

[0015] Based on the effects of the above polypeptides, the second object of the present invention is to provide a polypeptide composition, which includes one or more of the polypeptides Ser-Asp-Ala-Glu (SDAE) or Thr-Arg-Leu-Phe (TRLF) or Phe-Asp-His-Gly-Phe-Ala-Glu-Gln (FDHGFAEQ) or Trp-Ala-Lys (WAK) or Asn-Val-Leu-His (NVLH).

[0016] The third object of the present invention is to provide a method for improving the flavor of wine products, by adding any of the above polypeptides or the above polypeptide composition to wine.

[0017] In one embodiment, the wine products include fermented wines, distilled spirits, and blended wines.

[0018] In one embodiment, the fermented wines include: wine, beer, rice wine, fruit wine, etc.; the distilled spirits include: Chinese liquor, brandy, whisky, vodka, etc.; the blended wines include: cocktail, liqueur, medicinal liquor.

[0019] The present invention also provides a method for reducing the volatilization of flavor substances during the storage of wine products, by adding any of the above polypeptides or the above polypeptide composition to wine before storage.

[0020] In one embodiment, the flavor substances are acids, esters, and pyrazine substances.

[0021] In one embodiment, the ester substances include: ethyl formate, ethyl acetate, isoamyl acetate, ethyl propionate, ethyl butyrate, ethyl valerate, ethyl caproate, ethyl heptanoate, ethyl octanoate, ethyl decanoate, ethyl laurate, ethyl lactate, etc., among which ethyl acetate, ethyl caproate, ethyl lactate, ethyl butyrate, etc.; the acid substances include: acetic acid, butyric acid, caproic acid, lactic acid, etc.; the pyrazine substances include: pyrazine, 2-methylpyrazine, 2-ethylpyrazine, 2,3-methylpyrazine, 2,5-methylpyrazine, 2,6-methylpyrazine, 2,3,5-trimethylpyrazine, tetra-O-methylpyrazine, 2-ethyl-5-methylpyrazine, etc.

[0022] In one embodiment, the preparation method includes:

[0023] (1) Take the first-round base liquor of Maotai-flavor Chinese liquor, adsorb it with macroporous adsorption resin, and store it frozen.

[0024] (2) Freeze-dry to obtain a crude peptide powder, dissolve it in water to obtain a crude peptide solution.

[0025] (3) Ultrafilter the crude peptide solution with an ultrafiltration membrane, separate and purify it by liquid chromatography, remove acetonitrile and dry it to obtain a polypeptide powder.

[0026] (4) Identify the amino acid sequence of the polypeptide powder and synthesize the polypeptide according to the sequence.

[0027] In one embodiment, in step (1), the pore size of the macroporous resin is 0.4 - 0.45 μm.

[0028] In one embodiment, in step (2), the freeze-drying conditions are -75 to -80 °C for 24 to 36 h.

[0029] In one embodiment, the pore size of the ultrafiltration membrane in step (3) is 5-10 kDa.

[0030] In one embodiment, the method for synthesizing the polypeptide in step (4) includes separating from baijiu, synthesizing by genetically engineered bacteria, or synthesizing artificially.

[0031] In one embodiment, the method for preparing the polypeptide includes:

[0032] (1) Take the first-round Maotai-flavor baijiu, pass it through a macroporous adsorption resin with a pore size of 0.45 μm, put it into a petri dish and seal it with a film, and store it frozen at -75 to -80 °C for 24 to 36 h;

[0033] (2) Put it into a freeze dryer, fully freeze-dry it to obtain a crude peptide powder, re-dissolve it with a small amount of water, and store it at 4 °C;

[0034] (3) Ultrafilter the crude peptide powder using a 5-10 kDa ultrafiltration membrane, separate and purify it using liquid chromatography, remove acetonitrile in a rotary evaporator, and further freeze-dry it using a freeze dryer;

[0035] (4) The collected components are re-dissolved in 40 μL of 0.1% v / v (hereinafter omitted, all are volume fractions) trifluoroacetic acid solution, and the endogenous polypeptide sequence in baijiu is further identified by LC-MS / MS. The most abundant precursor ions are selected for HCD fragmentation in the dynamic scan (300 - 1800 m / z). The determination of the target value is based on predicted automatic gain control (PAGC). The dynamic exclusion time is 20 s. When m / z is 200, the measured scan resolution is 70000, and the HCD spectral resolution is set to 17500. The normalized collision energy is 27 eV, and the bottom fill rate is defined as 0.1%. This ratio specifies the minimum percentage that can reach the target value at the maximum fill time. According to the results of polypeptide identification and quantitative analysis, the peptide sequences SDAE, TRLF, FDHGFAEQ, WAK, and NVLH are determined. The corresponding polypeptide powder is obtained by Fmoc solid-phase synthesis method, dissolved in water to form a mother liquor, and stored at 4 °C.

[0036] In one embodiment, the production of Maotai-flavor baijiu: uses sorghum, wheat, and water as raw materials, does not add edible alcohol or flavor substances produced by non-alcoholic fermentation, and is made through high-temperature fermentation and distillation; it has the technological characteristics of "12987". "1" represents a one-year production cycle, "2" represents two feedings, "9" represents nine cookings, "8" represents eight fermentations, and "7" represents seven distillations.

[0037] In one embodiment, the first-round base liquor of Maotai-flavor baijiu in step (1) is the base liquor collected by distilling the first-round fermented grains according to the Maotai-flavor baijiu fermentation process in the Maotai-flavor baijiu workshop of the winery. Two parallel samples are taken, and the taken wine samples are placed in a 4 °C refrigerator for testing.

[0038] In one embodiment, in step (1), 10-15 mL of the first round of Maotai-flavor liquor should be taken for testing.

[0039] In one embodiment, in step (3), the liquid chromatography conditions are: on a SPE Cartridge C18 column (7 mm ID, 3 mL, Sigma-Aldrich, St. Louis, MO, USA), pre-equilibrated with 40 mL of 10% acetonitrile at normal pressure, washed with 5 mL of 10% acetonitrile, and then eluted with 5 mL of 70% acetonitrile.

[0040] In one embodiment, in step (4), the concentration of the polypeptide stock solution is 5.0-50 mg / mL.

[0041] Beneficial Effects

[0042] The various endogenous polypeptides separated from the Maotai-flavor liquor of the present invention have the following effects:

[0043] (1) The present invention obtains endogenous polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH from the first round of base wine of Maotai-flavor liquor. The polypeptides have intermolecular interactions with the flavor substances in Maotai-flavor liquor. Adding them to the raw liquor can reduce the volatilization of the flavor substances during the aging process and maintain the rich aroma of the liquor. In addition, adding them to the finished liquor can reduce the expression of irritating odors and coordinate the flavor of the liquor. Specifically, an appropriate amount of acid in Maotai-flavor liquor manifests as a fruity aroma, but when the acid is excessive, it manifests as a pungent odor. TRLF and NVLH can inhibit the volatility of excessive acid and play a positive role in blending the flavor of the finished liquor. Secondly, SDAE, FDHGFAEQ, and WAK can inhibit the volatility of pyrazine and ester aroma substances, which can reduce the loss of aroma of the raw liquor during the aging process and retain the fragrance for a long time.

[0044] (2) The method of the present invention is low-cost, energy-saving and environmentally friendly; Maotai-flavor liquor contains a large amount of unutilized polypeptides. The scheme of the present invention can realize the high-value recycling of Maotai-flavor liquor by-products, thereby promoting the concept of ecological winemaking to be implemented in all aspects of winemaking production;

[0045] (3) The process of the present invention is simple and does not require complicated equipment investment, but only requires very simple equipment;

[0046] (4) The polypeptide of the present invention is derived from liquor, and is added to alcoholic beverages as an additive to improve the flavor while being safer. BRIEF DESCRIPTION OF THE DRAWINGS

[0047] To more clearly illustrate the technical solutions in the embodiments of the present invention, the following will briefly introduce the attached drawings required for the description of the embodiments. Obviously, the attached drawings in the following description are only some embodiments of the present invention. For those of ordinary skill in the art, without creative efforts, other attached drawings can be obtained based on these attached drawings.

[0048] Figure 1 is a process schematic diagram of the present invention;

[0049] Figure 2 is the mass spectrometry identification of endogenous polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH obtained by the method of the present invention. (A) Mass spectrometry diagram of SDAE; (B) Mass spectrometry diagram of TRLF; (C) Mass spectrometry diagram of FDHGFAEQ; (D) Mass spectrometry diagram of WAK; (E) Mass spectrometry diagram of NVLH;

[0050] Figure 3 is the quantitative analysis of the inhibition of flavor substance volatilization by endogenous polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH obtained by the method of the present invention. (A) Esters and polypeptides; (B) Pyrazines and polypeptides; (C) Acids and polypeptides. Specific Embodiments

[0051] 1. Material Sources

[0052] The first-round base liquor: In the strong-flavor Baijiu workshop of the winery, the first-round fermented grains are distilled according to the strong-flavor Baijiu fermentation process, and the base liquor is collected, taking two parallel groups.

[0053] 2. Experimental Methods

[0054] The process schematic diagram of the present invention is as Figure 1 shown.

[0055] GC Analysis of the Interaction between Polypeptides and Flavor Substances: The components in the mixture of acid components (caproic acid, acetic acid, butyric acid, lactic acid), the mixture of ester components (ethyl caproate, ethyl acetate, ethyl butyrate, ethyl lactate), and the mixture of pyrazine components (tetramethylpyrazine, 2,3-dimethylpyrazine, diethylpyrazine, acetylpyrazine) were mixed at a mass ratio of 1:1:1:1 respectively, and dissolved in a 53% ethanol / water (v / v) solution to prepare model wines of different flavor component mixtures with a final concentration of 0.01 mg / mL. A certain amount of polypeptide powders SDAE, TRLF, FDHGFAEQ, WAK, and NVLH were added to the model wines of different flavor component mixtures, and the final polypeptide concentration was 0.01 mg / mL. The above samples were used as the experimental groups, and the mixtures of each flavor component without adding polypeptides were taken as the control groups (0.01 mg / mL). All groups were stored at 4°C for analysis. The samples of the experimental groups and the control groups were stirred at 30°C until equilibrium (10 min), and then a gas chromatograph injection (1 mL) was immediately inserted into the GC injection port for analysis.

[0056] GC Conditions: Chromatographic column: DB-5MS elastic quartz capillary column (30 m * 250 μm * 0.25 μm); Carrier gas: High-purity (99.999%) helium gas, flow rate 1.0 mL / min; Injection port temperature 250°C; Splitless injection. Programmed temperature rise: Column temperature 45°C, held for 2 min. Heated to 150°C at a rate of 5°C / min and held for 23 min, then heated to 290°C at a rate of 15°C / min and held for 37.333 min.

[0057] Example 1: Preparation of Polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH

[0058] 1. Isolate Polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH from Maotai-flavor Baijiu Round Wines

[0059] The specific steps are as follows:

[0060] (1) In the Maotai-flavor Baijiu workshop of the winery, distill the fermented grains of the first-round fermentation according to the Maotai-flavor Baijiu fermentation process, collect the base wine, take two parallels, and place the collected wine samples in a 4°C refrigerator for later measurement. Take 10 - 15 mL of the base wine of the first round of Maotai-flavor Baijiu, pass it through a macroporous adsorption resin with a pore size of 0.45 μm, put it into a petri dish and seal it with a film, and store it at -80°C for 24 h;

[0061] (2) Put it into a freeze dryer and thoroughly freeze-dry to obtain a crude peptide powder. Re-dissolve it with a small amount of water and store it at 4°C;

[0062] (3) Ultrafiltration of the crude peptide powder was carried out using a 10 kDa ultrafiltration membrane, and the filtrate was separated and purified by liquid chromatography. Liquid chromatography conditions: On a SPE Cartridge C18 column (7 mm I.D., 3 mL, Sigma - Aldrich, St. Louis, MO, USA), pre - equilibrated with 40 mL of 10% acetonitrile at atmospheric pressure. After washing with 5 mL of 10% acetonitrile, it was then eluted with 5 mL of 70% acetonitrile. The eluate was removed of acetonitrile in a rotary evaporator and further freeze - dried using a freeze dryer;

[0063] (4) The freeze - dried fraction was collected and redissolved in 40 μL of 0.1% trifluoroacetic acid solution, and the endogenous polypeptide sequences in Chinese liquor were further identified by LC - MS / MS. The most abundant precursor ions were selected for HCD fragmentation in the dynamic scan (300 - 1800 m / z). The determination of the target value was based on predicted automatic gain control (PAGC). The dynamic exclusion time was 20 s. When m / z was 200, the measurement scan resolution was 70000, and the HCD spectral resolution was set to 17500. The normalized collision energy was 27 eV, and the bottom fill rate was defined as 0.1%, which specifies the minimum percentage that can reach the target value at the maximum fill time. Finally, the polypeptide sequences SDAE, TRLF, FDHGFAEQ, WAK, NVLH were identified.

[0064] The identification results of the polypeptides SDAE, TRLF, FDHGFAEQ, WAK, NVLH are as Figure 2 shown.

[0065] 2. Chemical synthesis of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, NVLH

[0066] The polypeptide sequences SDAE, TRLF, FDHGFAEQ, WAK, and NVLH were determined. The corresponding polypeptide powders were obtained by the Fmoc solid-phase synthesis method. 1.5 g of dichloride resin was added to a reaction column soaked with dichloromethane, and the resin was soaked with 15 mL of dichloromethane for 30 min to fully expand and was activated for use. 0.31 g of Fmoc-Cys(Acm)-OH was dissolved in dichloromethane, and then 0.5 mL of diisopropylethylamine was added. The mixture was added to the reaction vessel, and N2 was blown for reaction for 2 h. The reaction solution was filtered, 5 mL of methanol was added to block the reaction for 1 h, and then the resin was washed 3 times with dichloromethane, isopropanol, and N,N-dimethylformamide respectively. About 15 mL of a 20% piperidine solution in N,N-dimethylformamide was added for reaction for 5 min, and then filtered off. Then 15 mL was added for reaction for 20 min, and the resin was washed 2 times with isopropanol and 3 times with N,N-dimethylformamide. 0.55 g of Fmoc-Trp(boc)-OH and 0.35 g of 1-oxo-3-bis(dimethylaminocarbonyl)benzotriazolium tetrafluoroborate were dissolved in N,N-dimethylformamide, and were mixed with 0.6 mL of 1-hydroxybenzotriazole (2 mol / L) and 0.2 mL of 1-oxo-3-bis(dimethylaminocarbonyl)benzotriazolium tetrafluoroborate and added to the reaction vessel containing the resin. N2 was blown for reaction for 2 h, and then the resin was washed 2 times with isopropanol and 3 times with N,N-dimethylformamide. A small amount of resin was added to a 5% ninhydrin solution in absolute ethanol (W / V), and boiled in a water bath for 3 min. The resin was colorless, that is, a negative reaction, and the next reaction was carried out. The above steps (deprotection and peptide coupling) were repeated, and the amino acids were sequentially coupled in the order from the carboxyl terminus to the amino terminus according to the sequence of the linear peptide before cyclization. After the last amino acid was coupled, the Fmoc protecting group of the last amino acid was not removed temporarily. After washing and removing the Fmoc protection of the last amino acid, the cyclic peptide-resin complex was dried with N2 and added to a 50 mL small flask. A cleavage reagent prepared by mixing TFA / benzyl methyl sulfide / mercaptoethanol / water / phenol in a ratio of 10 mL / 0.5 mL / 0.25 mL / 0.5 mL / 0.75 g was added. After magnetic stirring at room temperature for 3 h, it was filtered and placed in ice-cold diethyl ether, placed in the refrigerator for 2 h, centrifuged and collected. The precipitate was dissolved in pure water, then placed in the refrigerator for freezing, and then the frozen ice-like substance was placed in a vacuum freeze dryer and freeze-dried to constant weight to obtain the crude peptide, and water was added to prepare a polypeptide mother liquor with a final concentration of 5.0 - 50 mg / mL.

[0067] Example 2: Detection of the properties of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH

[0068] The polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH prepared in Example 1 were detected for their effects on the volatilization of flavor substances.

[0069] (1) Effects of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH on the volatilization of ester component mixtures (ethyl hexanoate, ethyl acetate, ethyl butyrate, ethyl lactate)

[0070] Esters in Chinese liquor are substances formed by the reaction of acids and alcohols, and most of them have aromatic flavors. Ester substances also have an important impact on the flavor and taste of Chinese liquor, and the content of ester substances in most Chinese liquors is relatively high.

[0071] According to the normalization method, the relative content of volatile flavor substances was statistically analyzed. The lower the relative content value, the stronger the inhibitory effect on volatilization. The results are as Figure 3 shown in Figure A. The inhibition rates of polypeptides TRLF and FDHGFAEQ on ester components (ethyl hexanoate, ethyl acetate, ethyl butyrate, ethyl lactate) reached 15% and 4.16% respectively. Among them, after adding polypeptide TRLF to the ester solution, the relative content of esters decreased significantly. After adding WAK, the content of esters increased (41.67%), which proved that polypeptides TRLF, FDHGFAEQ, and WAK can affect the volatilization of esters.

[0072] (2) Effects of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH on the volatilization of pyrazine component mixtures (tetramethylpyrazine, 2,3-dimethylpyrazine, diethylpyrazine, acetylpyrazine)

[0073] As Figure 3 shown in Figure B, the inhibition rates of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH reached 10.44%, 65.66%, 1.35%, 16.49%, and 35.35% respectively. Among them, the inhibitory effect was most obvious after adding polypeptide TRLF to the pyrazine solution, which has important inspiration for the blending of Jiangxiang-type Chinese liquor.

[0074] (3) Effects of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH on the volatilization of acid component mixtures (hexanoic acid, acetic acid, butyric acid, lactic acid)

[0075] Acid compounds play an important role in the flavor and quality of Chinese liquor. Appropriate amounts of acids can adjust the quality and taste of the liquor body. As Figure 3 shown in Figure C, the inhibition rates of polypeptides TRLF and NVLH reached 21.45% and 9.24% respectively. After adding polypeptides TRLF and NVLH to the acid solution, the relative content of acids also decreased slightly, proving that polypeptides TRLF and NVLH have an obvious inhibitory effect on the volatility of acids.

[0076] The above results show that there are obvious interaction relationships between polypeptide TRLF and acids, esters, and pyrazines. FDHGFAEQ and WAK can promote the volatility of acids and esters. Polypeptide SDAE can inhibit the volatilization of pyrazine substances. Polypeptide TRLF can inhibit the volatilization of acids, esters, and pyrazine substances. Polypeptide FDHGFAEQ can inhibit the volatilization of esters and pyrazine substances. Polypeptide WAK can inhibit the volatilization of pyrazine substances. Polypeptide NVLH can inhibit the volatilization of acids and pyrazine substances.

[0077] Therefore, polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH can be used to regulate the volatilization effect of flavor substances in liquor products and prepare liquor products with specific flavors.

[0078] Example 3: Application of polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH in reducing the volatilization of flavor substances in liquor products

[0079] Before the storage of Chinese liquor, polypeptides SDAE, TRLF, FDHGFAEQ, WAK, and NVLH were added to the liquor at an addition amount of 0.01 mg / mL, and then the liquor was stored.

[0080] It was detected that the contents of flavor substances (caproic acid, acetic acid, butyric acid, lactic acid, ethyl caproate, ethyl acetate, ethyl butyrate, ethyl lactate, ligustrazine, 2,3-dimethylpyrazine, diethylpyrazine, acetylpyrazine) in the Chinese liquor body added with polypeptides were higher than those in the Chinese liquor without the addition of polypeptides after storage.

[0081] The series of detailed descriptions listed above are only specific descriptions of the feasible embodiments of the present invention, and they are not intended to limit the protection scope of the present invention. Any equivalent embodiments or changes made without departing from the technical spirit of the present invention should be included in the protection scope of the present invention.

Claims

1. A method for improving the flavor of wine products, characterized in that, Add a polypeptide to the wine, and the polypeptide is Thr-Arg-Leu-Phe (TRLF) or Asn-Val-Leu-His (NVLH); The improvement of flavor is to inhibit the volatilization of esters, acids or pyrazines in the wine.

2. A method for reducing the volatilization of flavor substances during the storage of wine products, characterized in that, Add the polypeptide to the wine before storage, and the polypeptide is Thr-Arg-Leu-Phe (TRLF) or Asn-Val-Leu-His (NVLH); The flavor substances are esters, acids or pyrazines.

3. The method according to claim 2, wherein The wine products include: distilled spirits, fermented wines and blended wines.

Citation Information

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