CN111184124A - Clam delicious peptide and preparation method and application thereof - Google Patents
Clam delicious peptide and preparation method and application thereof Download PDFInfo
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- CN111184124A CN111184124A CN202010041490.5A CN202010041490A CN111184124A CN 111184124 A CN111184124 A CN 111184124A CN 202010041490 A CN202010041490 A CN 202010041490A CN 111184124 A CN111184124 A CN 111184124A
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- 238000002360 preparation method Methods 0.000 title claims abstract description 16
- 108010053500 delicious peptide Proteins 0.000 title abstract description 13
- JYGRAOYMDDFOSM-FQJIPJFPSA-N (4s)-4-[[(2s)-4-carboxy-2-[[(2s)-3-carboxy-2-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]propanoyl]amino]butanoyl]amino]-5-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-oxopentano Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN JYGRAOYMDDFOSM-FQJIPJFPSA-N 0.000 title abstract description 12
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/04—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from fish or other sea animals
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L23/00—Soups; Sauces; Preparation or treatment thereof
- A23L23/10—Soup concentrates, e.g. powders or cakes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/23—Synthetic spices, flavouring agents or condiments containing nucleotides
- A23L27/235—Synthetic spices, flavouring agents or condiments containing nucleotides containing also amino acids
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/20—Synthetic spices, flavouring agents or condiments
- A23L27/26—Meat flavours
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/50—Soya sauce
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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Abstract
The invention discloses a clam fresh taste peptide and a preparation method and application thereof, belonging to the technical field of food additives and preparation methods thereof. The clam fresh taste peptide comprises any one or more polypeptides with an amino acid sequence of GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK, and the preparation method of the polypeptides comprises the following steps: taking meat from fresh clam, adding water for homogenizing, heating to obtain clam poaching liquid, and carrying out ultrafiltration separation, gel chromatography purification and RP-HPLC purification to obtain the delicious peptide. The umami peptide prepared by the method has the umami and salty taste enhancing effect, can be docked with an umami receptor T1R1/T1R3 based on molecular simulation, and has main binding sites of amino acid residues Asp196, Glu128, His125, His368, Glu281 and Arg34 on a T1R3 subunit. The delicious peptide seasoning adopts natural cooking and purification methods, has natural delicate flavor and good nutritional value, and is an ideal seasoning product.
Description
Technical Field
The invention belongs to the technical field of food additives and preparation methods thereof, and particularly relates to a clam umami peptide and a preparation method and application thereof.
Background
The delicious peptide is a small molecular peptide capable of presenting delicate flavor, has higher nutritive value and flavor activity, not only can endow food with delicious taste and enhance delicate flavor and mellow taste of the food, but also can enhance the freshness by cooperating with other substances, and can reduce the intake of salt and sodium glutamate (MSG) when used cooperatively. In addition, the umami peptide can reduce the bitter intensity, has good thermal stability, processing characteristics, fresh effect and nutritive value, and accords with the development trend of natural, nutritional and safe foods, so the umami peptide becomes a research hotspot of food umami science and a key direction of development of an umami agent in recent years.
The clams (Meretrix Meretrix) belong to the phylum Mollusca (Mollusca), the class Lamellibranchia (Lamellibranchia), the order Veneridae (Veneroida), the family Veneridae (Veneridae) and the genus Meretrix, and are one of the important marine economic shellfish in China. The clam is rich in nutrition and delicious in meat taste, is regarded as a delicacy by the emperor and the ink of the civilians in the past as well as is favored by the general people and is vegetatively reputed as the first-to-first-delicacy in every day. At present, researches and reports on the fresh taste components of the clams mainly focus on the contribution of nutritional components such as flavor development nucleotides, succinic acid, free amino acids, inorganic ions, glycogen and the like to the flavor of the clams, and most researches on the fresh taste peptides of the clams mainly use protease for enzymolysis, and enzymolysis mixed liquor of the fresh taste peptides is taken as the seafood flavor development peptides. On one hand, the fresh components of the clam are different from the natural clam fresh taste components due to enzymolysis, and the taste is different, on the other hand, the research on the structure of the flavor development peptide components is not sufficient, which is not beneficial to the development and utilization of the clam fresh taste peptides, so that the research and development of the structure and the fresh taste characteristics of the pure natural fresh taste peptides in the clam are significant, and the development of the clam fresh taste peptides with higher market potential is significant.
Disclosure of Invention
The invention aims to provide a clam umami peptide, which comprises the preparation method and the application field thereof. The clam delicious peptide fully protects natural delicious components in clams through a traditional boiling process, obtains high-purity clam delicious peptide by utilizing a chromatographic separation and purification technology, and performs sequence identification on the delicious peptide by combining MALDI-TOF/TOF MS, thereby disclosing amino acid sequences of seven clam delicious peptides, wherein the amino acid sequences are GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK respectively. The disclosed clam umami peptide has low umami threshold value and strong umami, has the effect of enhancing the umami and the salty taste, is an ideal food additive and a freshener, and lays a foundation for the research and the utilization of the subsequent clam umami peptide.
The invention is realized by the following technical scheme
A clam delicious peptide contains any one or more polypeptides with an amino acid sequence of GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK. The preparation method of the polypeptide comprises the following steps:
(1) preparing the freeze-dried powder of the poaching liquid, removing shells of fresh and alive clams to obtain meat, cleaning, draining, weighing, adding deionized water according to a proportion, homogenizing, heating, boiling, filtering with a filter cloth, centrifuging the filtrate, taking supernatant, and freeze-drying to obtain the freeze-dried powder of the poaching liquid.
(2) And (3) performing ultrafiltration separation, re-dissolving the decoction freeze-dried powder in ultrapure water to prepare a solution with the concentration of 10mg/mL, passing through an ultrafiltration membrane, collecting filtrate, and performing freeze drying to obtain ultrafiltrate freeze-dried powder.
(3) Purifying by gel chromatography, re-dissolving the ultrafiltrate lyophilized powder with ultrapure water to obtain a solution with the concentration of 10mg/mL, loading on a Sephadex G-15 gel chromatographic column, eluting with ultrapure water, collecting the 5 th peak component F5, and lyophilizing to obtain F5 lyophilized powder.
(4) RP-HPLC purification, dissolving the F5 freeze-dried powder in ultrapure water to prepare a solution with the concentration of 10mg/mL, further separating and purifying by using a reversed phase high performance liquid chromatography, collecting the 1 st main peak component F5-I, and freeze-drying to obtain the umami peptide freeze-dried powder.
In the step (1), the ratio of Chinese clam meat to deionized water is 1:3 (w/v); keeping the central temperature of the boiled rice for 20-30 min after the central temperature reaches 95-100 ℃ during boiling; centrifuging the boiled liquid for 20-30 min at the rotating speed of 5000 r/min.
The molecular weight cut-off of the ultrafiltration membrane in the step (2) is 3000Da, and ultrafiltration separation is carried out at the low temperature of 4 ℃.
The Sephadex G-15 gel chromatographic column in the step (3) has the elution conditions that: the sample loading amount is 2mL, the flow rate is 1mL/min, and the ultraviolet detection wavelength is 220 nm.
And (4) further separating and purifying the F5 freeze-dried powder by using reverse phase high performance liquid chromatography, wherein the chromatographic conditions are as follows: column YMC-Pack ODS-AQ C18 (250X 10mm, 5 μm), flow rate 1mL/min, detection wavelength 220nm, loading 100 μ L, mobile phase: a: acetonitrile (0.05% TFA), B: ultrapure water (0.05% TFA), isocratic elution: 10% A, 90% B, elution time 40 min.
The clam umami peptide containing seven peptide fragments can be prepared by the above embodiment.
In the process of preparing and screening the clam umami peptide, in order to further verify the technical effect of the invention, a series of related experiments are implemented, which are summarized as follows:
the measurement methods involved in sensory evaluation in the following experiments were as follows:
(1) sensory evaluation method of separated components and umami peptide: taking each level of separated components and the umami peptide to prepare 50mL of solutions of 1mg/mL respectively, taking the filtrate after filtration by a 0.22-micron filter membrane as sensory evaluation sample liquid, and carrying out rating evaluation by a sensory evaluation panel, wherein the score of each taste adopts the average value of the evaluation results of each evaluator.
(2) The method for measuring the freshness threshold of the delicious peptide comprises the following steps: preparing a mother solution with the concentration of 1mg/mL by using a synthetic peptide, gradually diluting the mother solution in a volume ratio of 1:1 by adopting a taste dilution analysis method (TDA) until the mother solution is just distinguished from other two blank controls, wherein the highest sample concentration which can be accurately evaluated by most (more than 6) sensory evaluators is the taste threshold value of a sample in water, and the tasters are required to describe the taste of the sample.
(3) The method for measuring the seasoning characteristics of the delicious peptide comprises the following steps: for the evaluation of flavor characteristics, the umami peptide was added to the simulated broth in a mode of simulated broth (2mg/mL sodium glutamate, 2mg/mL sodium chloride and 0.4mg/mL sucrose) + umami peptide, configured as a solution at a concentration of 0.2mg/mL, and the umami value and the salty value of the simulated broth + umami peptide solution were measured, and the sensory evaluation criteria were in accordance with the sensory evaluation method of umami peptide.
The sensory panel consisted of 16 laboratory panelists (8 men and 8 women, between the ages of 25-35), all with sensory training. The concentration of the samples in the sensory evaluation was scored from 0 to 10 points, with 0 points representing no taste and 10 points representing significant taste. The evaluation standards for sweetness, bitterness, sourness, saltiness, and umami were sucrose (1%), L-isoleucine (0.25%), citric acid (0.08%), sodium chloride (0.35%), and monosodium glutamate (0.35%), respectively, and the standard at this concentration was rated as 5 points.
Experiment I, sequence identification experiment of umami peptide
Performing sequence identification on the umami peptide freeze-dried powder by using MALDI-TOF/TOF MS, sucking 1 mu L of solution supernatant after enzymolysis to be spotted on a sample target, drying, spotting 1 mu L of α -cyano-4-hydroxycinnamic acid (HCCA) matrix solution, performing on-machine analysis after all the solution is dried, putting the sample target into a MALDI-TOF/TOF mass spectrometer, starting control software, and performing data acquisition, wherein mass spectrum acquisition parameters comprise a positive ion reflection mode, a first-stage mass spectrum molecular weight range of 700-3500Da, and a second-stage mass spectrum molecular weight range of 40-1050Da, and identifying to obtain seven umami peptides in the umami peptide freeze-dried powder, wherein the sequences are GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK, and the peptide sections correspond to the fresh peptide freeze-dried powder by using F5-I-a, F5-I-b, F5-I-c, F5-I-d, F5-I-e, F5-I-F and F5-I-g symbols.
Experiment two: chemical synthesis verification experiment
The seven peptide segments GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK are synthesized by a solid-phase synthesis method, and are entrusted to the Qiangyao biotechnology limited of China to be synthesized, and the purity of the seven peptide segments GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK is over 99 percent; sensory evaluation is carried out on the synthesized umami peptides, and the result shows that the seven umami peptides can present the umami; the freshness threshold values and flavor description results of the seven fresh taste peptides are listed in table 1, and as can be seen from the table, the threshold values of the seven fresh taste peptides are all 0.125mg/mL, and the seven fresh taste peptides can present various flavors and have rich taste, so that the seven fresh taste peptides are ideal seasoning raw materials.
TABLE 1 Presence threshold and flavor description of umami peptides
Experiment three: umami peptide and umami receptor assay
(1) Homologous modeling of the umami receptor T1R1/T1R 3: the amino acid sequence of T1R1/T1R3 was retrieved from the Uniprotkb database, the metabotropic glutamate receptor mGluR1 was used as template protein, the SWISS-MODEL server was used to construct the homology MODEL, then the preliminary homology MODEL was introduced into Discovery Studio, and the MODEL was optimized using Minimization protocol, the results are shown in FIG. 1.
(2) Preparation of receptor proteins: removing the small molecular ligand and the solvent molecule from the homologous model obtained in the step (1), and adding a hydrogen atom and a CHARMM force field to be used as a receptor protein.
(3) Preparation of small molecule ligand: the seven umami peptides obtained in the example 2 are introduced into Discovery Studio to construct a three-dimensional structure of the small molecule peptide, and the small molecule peptide is optimized by using a Minimization ligand protocol to serve as a small molecule ligand.
(4) Molecule docking: performing molecular docking on the receptor protein in the step (2) and the small-molecule ligand in the step (3) in a discovery studio, wherein the binding site of the receptor and the ligand is defined by using a CDOCKER protocol, and the result is shown in FIG. 2. As can be seen from the figure, seven umami peptides and the umami receptor T1R1/T1R3 are all combined by being inserted into the "fly trap" (VFTD) of the T1R3 subunit, and the combination of the umami peptides and the T1R3 subunit is mainly through electrostatic interaction, hydrogen bonding, hydrophobic interaction and van der waals force generated between the amino acid residues of the receptor, which is probably due to the smaller cavity volume of the ligand binding region of the T1R1 subunit, while the peptide chain length of the obtained umami peptide is identified to be longer and difficult to combine with the T1R1 subunit. Table 2 and table 3 list the docking energies and binding sites of seven umami peptides to the umami receptor T1R1/T1R3, respectively, and it can be seen from the table that there is no correlation between docking energies and lengths of umami peptides, wherein the docking energy of umami peptide VTADESQQDVLK (F5-I-g) is the lowest and binding affinity is the strongest mainly because of its smallest docking distance to the receptor, and the binding sites of seven umami peptides to the T1R3 subunit are mainly amino acid residues Asp196, Glu128, His125, His368, Glu281 and Arg34 on the T1R3 subunit, wherein Asp196 is the most dominant amino acid residue.
TABLE 2 docking energy of umami peptides with the umami receptor T1R1/T1R3
TABLE 3 binding sites of umami peptides to umami receptor T1R1/T1R3
Experiment four: simulated broth experiment
Seven fresh peptides which are chemically synthesized are taken as raw materials, the seven fresh peptides are respectively added into simulated broth, and sensory evaluation is carried out by taking the simulated broth as a reference, the result is shown in figure 3, the simulated broth added with the fresh peptides has obviously improved fresh taste and salty taste compared with the simulated broth with simple flavor, wherein the improvement effect of the fresh taste is higher than the salty taste, and the seven peptide segments have the seasoning property, thereby being an ideal raw material for preparing the seasoning for increasing the freshness and reducing the salt.
Experiment five: umami taste protection and sensory evaluation in preparation process
In the preparation process of the clam umami peptide, the traditional boiling method is adopted in the early stage, natural umami components in clams are fully protected, in the later gel chromatography and RP-HPLC purification experiment processes, each separation peak component is collected, concentrated, freeze-dried and subjected to sensory evaluation, and the component with the highest umami value is selected as a sample for next separation and purification, so that the component with higher purity is obtained, and the loss of the umami components is avoided.
In conclusion, the clam umami peptide prepared by the invention has the following beneficial effects:
① the clam delicious peptide has natural delicate flavor, high strength and soft and harmonious taste;
② the clam fresh taste peptide has low fresh threshold value, has the effects of enhancing fresh taste and salty taste, has obvious fresh-increasing effect on simulated broth, and can be used for preparing salt-reducing and fresh-increasing seafood seasoning to reduce the intake of salt and sodium glutamate (MSG);
③ the clam fresh taste peptide has definite sequence, and the molecular action between the clam fresh taste peptide and the fresh taste receptor T1R1/T1R3 is researched by adopting a computer-aided molecular simulation method, thereby preliminarily explaining the fresh-keeping mechanism of the clam fresh taste peptide and having theoretical guiding significance for developing novel fresh taste peptide.
Detailed Description
The following further illustrates the embodiments of the invention, which are not limited to the above embodiments, and any modifications or substitutions in the basic spirit of the embodiments are also included in the scope of the invention as claimed.
Example 1
A preparation method of clam umami peptide, polypeptide thereof comprises the following steps:
(1) preparing clam poaching liquid freeze-dried powder: removing shell of fresh living Meretrix meretrix Linnaeus, cleaning Meretrix meretrix Linnaeus meat, draining, weighing, adding deionized water at a feed-liquid ratio of 1:3(w/v), homogenizing, heating, decocting, keeping for 20min when the central temperature reaches 95 deg.C, cooling to room temperature after heating, filtering with filter cloth, centrifuging the filtrate at 4 deg.C for 20min at 5000r/min, collecting supernatant, and freeze drying to obtain lyophilized powder of Meretrix meretrix Linnaeus decoction.
(2) And (3) ultrafiltration separation: re-dissolving lyophilized powder of the clam poaching solution in ultrapure water to obtain a solution with a concentration of 10mg/mL, performing ultrafiltration separation at 4 ℃ by using an ultrafiltration membrane with a molecular weight cutoff of 3000Da, collecting filtrate, and freeze-drying to obtain ultrafiltrate lyophilized powder.
(3) And (3) gel chromatography purification: redissolving the ultrafiltrate freeze-dried powder by ultrapure water, preparing a solution with the concentration of 10mg/mL, loading the solution on a Sephadex G-15 gel chromatographic column, and eluting by ultrapure water, wherein the elution conditions are as follows: the sample loading amount is 2mL, the flow rate is 1mL/min, the ultraviolet detection wavelength is 220nm, one tube is collected by the component collector every 3min, and 7 components are obtained as a result, and the chromatogram is shown in FIG. 4. And respectively collecting each separated peak component, concentrating, freeze-drying, performing sensory evaluation, selecting the component with the highest umami value as a sample for next separation and purification, and selecting the fifth peak component F5 with the highest umami value for next separation to obtain the component with higher purity.
(4) RP-HPLC purification: preparing F5 lyophilized powder into a solution with the concentration of 10mg/mL, and further separating by using reverse phase high performance liquid chromatography, wherein the chromatographic conditions are as follows: column YMC-Pack ODS-AQ C18 (250X 10mm, 5 μm), flow rate 1mL/min, ultraviolet detection wave 220nm, sample loading 100 μ L, mobile phase: a: acetonitrile (0.05% TFA), B: ultrapure water (0.05% TFA), isocratic elution: 10% A, 90% B, elution time 40 min. The chromatogram is shown in FIG. 5, collecting main component F5-I, and freeze drying to obtain Meretrix meretrix umami peptide lyophilized powder.
Example 2
(1) Preparing clam poaching liquid freeze-dried powder: removing shell of fresh living Meretrix meretrix Linnaeus, cleaning Meretrix meretrix Linnaeus meat, draining, weighing, adding deionized water at a feed-liquid ratio of 1:3(w/v), homogenizing, heating, decocting, keeping for 30min when the central temperature reaches 100 deg.C, cooling to room temperature after heating, filtering with filter cloth, centrifuging the filtrate at 4 deg.C for 30min at 5000r/min, collecting supernatant, and freeze drying to obtain lyophilized powder of Meretrix meretrix Linnaeus decoction.
(2) And (3) ultrafiltration separation: the same as in example 1.
(3) And (3) gel chromatography purification: redissolving the ultrafiltrate freeze-dried powder by ultrapure water, preparing a solution with the concentration of 10mg/mL, loading the solution on a Sephadex G-15 gel chromatographic column, and eluting by ultrapure water, wherein the elution conditions are as follows: the sample loading amount is 2mL, the flow rate is 1mL/min, the ultraviolet detection wavelength is 220nm, the fifth peak component F5 is collected, and freeze drying is carried out to obtain F5 freeze-dried powder.
(4) RP-HPLC purification: the clam fresh taste peptide freeze-dried powder is obtained in the same way as the example 1.
Example 3
(1) Preparing clam poaching liquid freeze-dried powder: removing shell of fresh living Meretrix meretrix Linnaeus, cleaning Meretrix meretrix Linnaeus meat, draining, weighing, adding deionized water at a feed-liquid ratio of 1:3(w/v), homogenizing, heating, decocting, keeping for 25min when the central temperature reaches 95 deg.C, cooling to room temperature after heating, filtering with filter cloth, centrifuging the filtrate at 4 deg.C for 25min at 5000r/min, collecting supernatant, and freeze drying to obtain lyophilized powder of Meretrix meretrix Linnaeus decoction.
(2) And (3) ultrafiltration separation: the same as in example 1.
(3) And (3) gel chromatography purification: the same as in example 2.
(4) RP-HPLC purification: the clam fresh taste peptide freeze-dried powder is obtained in the same way as the example 1.
Example 4
100mg of the clam umami peptide prepared in examples 1-3 and 0.35g of sodium glutamate were added to 100ml of deionized water as experimental groups, and sensory evaluation was performed with no umami peptide as a control group. (0.35% sodium glutamate control group assigned a 5 point umami taste)
Compared with a control group, the clam umami peptide prepared in the embodiment 1 has the umami score increased from 5 to 7.5; compared with a control group, the clam umami peptide prepared in the embodiment 2 has the umami score increased from 5 to 7.5; by using the clam umami peptide prepared in example 3, the umami score is increased from 5 to 7 compared with the control group.
Example 5
100mg of the umami peptide prepared in examples 1 to 3 was added to 100ml of soy sauce, and then diluted twice with deionized water as an experimental group, and sensory evaluation was performed with no umami peptide as a control group. (Soy sauce control group, diluted twice without addition of umami peptide, was judged to have umami taste of 5 points)
Compared with a control group, the clam umami peptide prepared in the embodiment 1 has the umami score increased from 5 to 7.5; compared with a control group, the clam umami peptide prepared in the embodiment 2 has the umami score increased from 5 to 7; by using the clam umami peptide prepared in example 3, the umami score is increased from 5 to 7.5 compared with the control group.
The comparison experiment of the embodiment 4 and the embodiment 5 shows that the clam umami peptide has obvious beneficial effect in practical application and can realize good fresh-improving effect on the original basis, so that the umami peptide has good application prospect.
Drawings
F5-I-a, F5-I-b, F5-I-c, F5-I-d, F5-I-e, F5-I-F and F5-I-g respectively represent umami peptide GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK.
FIG. 1A model of cognate mimetic receptors for the umami receptor T1R1/T1R3 (A) and a Pogram (B);
FIG. 2 shows the molecular docking results of seven clam fresh taste peptides F5-I-a (A), F5-I-b (B), F5-I-c (C), F5-I-d (D), F5-I-e (E), F5-I-F (F) and F5-I-g (G) with the fresh taste receptor T1R1/T1R 3;
FIG. 3 effect of seven clam umami peptides on simulated broth flavor;
FIG. 4 Sephadex G-15 gel chromatogram of ultrafiltrate component with less than 3000Da of clam boiled water;
FIG. 5 RP-HPLC separation chromatogram of Sephadex G-15 gel fraction F5.
Claims (10)
1. A clam umami peptide which is characterized by comprising any one or more polypeptides with an amino acid sequence of GLLPDGTPR, RPNPFENR, STMLLESER, ANPGPVRDLR, QVAIAHRDAK, VLPTDQNFILR, VTADESQQDVLK.
2. The meretrix umami peptide of claim 1, wherein the umami peptide has an umami and salty taste enhancing effect with a umami threshold of 0.125 mg/mL.
3. The clam umami peptide according to claim 1, wherein the umami peptide can be interfaced with umami receptor T1R1/T1R3 based on molecular simulation, and the main binding sites are amino acid residues Asp196, Glu128, His125, His368, Glu281 and Arg34 located on the T1R3 subunit.
4. The clam umami peptide of claim 1, wherein the preparation method of the polypeptide comprises the following steps:
(1) preparing a poaching liquid freeze-dried powder, namely removing shells of fresh and alive clams to obtain meat, cleaning, draining, weighing, adding deionized water in proportion to homogenate, heating, boiling, filtering with a filter cloth, centrifuging the filtrate, taking supernatant, and freeze-drying to obtain the poaching liquid freeze-dried powder;
(2) performing ultrafiltration separation, redissolving the decoction freeze-dried powder in ultrapure water to prepare a solution with the concentration of 10mg/mL, passing through an ultrafiltration membrane, collecting filtrate, and performing freeze drying to obtain ultrafiltrate freeze-dried powder;
(3) purifying by gel chromatography, re-dissolving the ultrafiltrate lyophilized powder with ultrapure water to obtain a solution with a concentration of 10mg/mL, loading on Sephadex G-15 gel chromatographic column, eluting with ultrapure water, collecting peak 5 component F5, and lyophilizing to obtain F5 lyophilized powder;
(4) and (3) RP-HPLC purification, dissolving the F5 freeze-dried powder in ultrapure water to prepare a solution with the concentration of 10mg/mL, further separating and purifying by using a reversed phase high performance liquid chromatography, collecting the 1 st main peak component F5-I, and freeze-drying to obtain the clam umami peptide freeze-dried powder.
5. The method for preparing clam umami peptide according to claim 4, wherein the ratio of clam meat to deionized water in step (1) is 1:3 (w/v); keeping the central temperature of the boiled rice for 20-30 min after the central temperature reaches 95-100 ℃ during boiling; centrifuging the boiled liquid for 20-30 min at the rotating speed of 5000 r/min.
6. The method for preparing clam umami peptide according to claim 4, wherein the ultrafiltration membrane in the step (2) has a molecular weight cut-off of 3000Da, and the ultrafiltration separation is carried out at a low temperature of 4 ℃.
7. The method for preparing clam umami peptide according to claim 4, wherein the SephadexG-15 gel chromatographic column in step (3) is eluted under the following conditions: the sample loading amount is 2mL, the flow rate is 1mL/min, and the ultraviolet detection wavelength is 220 nm.
8. The method for preparing clam umami peptide according to claim 4, wherein in the step (4), the F5 lyophilized powder is further separated and purified by reverse phase high performance liquid chromatography, and the chromatographic conditions are as follows: column YMC-Pack ODS-AQ C18 (250X 10mm, 5 μm), flow rate 1mL/min, detection wavelength 220nm, loading 100 μ L, mobile phase: a: acetonitrile (0.05% TFA), B: ultrapure water (0.05% TFA), isocratic elution: 10% A, 90% B, elution time 40 min.
9. The use of the clam umami peptide of claim 1 in the preparation of seasonings, food products and health products.
10. The seasoning of claim 9 wherein the seasoning comprises monosodium glutamate, chicken essence, chicken powder, soy sauce, soup cubes.
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| CN111557430B (en) * | 2020-05-25 | 2022-11-29 | 渤海大学 | Umami peptide separated from fish sauce and application thereof |
| CN113248565A (en) * | 2021-02-10 | 2021-08-13 | 渤海大学 | Active peptide with delicate flavor |
| CN113390994B (en) * | 2021-06-16 | 2023-03-21 | 上海应用技术大学 | Method for extracting, separating, identifying and verifying bitter peptides in yellow wine |
| CN113390994A (en) * | 2021-06-16 | 2021-09-14 | 上海应用技术大学 | Method for extracting, separating, identifying and verifying bitter peptides in yellow wine |
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