CN110973341B - Method for preparing blue clam-rich small molecule peptide - Google Patents
Method for preparing blue clam-rich small molecule peptide Download PDFInfo
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- CN110973341B CN110973341B CN202010011503.4A CN202010011503A CN110973341B CN 110973341 B CN110973341 B CN 110973341B CN 202010011503 A CN202010011503 A CN 202010011503A CN 110973341 B CN110973341 B CN 110973341B
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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
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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
- A23L27/10—Natural spices, flavouring agents or condiments; Extracts thereof
- A23L27/14—Dried spices
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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Abstract
A method for preparing a blue clam rich small molecule peptide comprises the steps of adding crushed blue clam meat into water, adjusting the pH value, adding Novozym compound protease, flavourzyme flavor protease, yeast powder and lactic acid bacteria, and carrying out ultrahigh pressure treatment at the ultrahigh pressure of 150MPa-250MPa at room temperature for 40min-60min; continuously performing enzymolysis on the blue clam meat at the temperature of 45-55 ℃ for 3-4 h, then placing in boiling water at the temperature of 95-100 ℃ to inactivate enzyme for 10-20 min, centrifuging, taking supernatant, and performing spray drying to obtain the small-molecule active peptide powder of the blue clam meat. The advantages are that: the method has the advantages of simple process and convenient operation, the obtained peptide has small molecular weight, most of the peptides have the molecular weight of less than 500Da, the bitter taste of the peptides is reduced, and the flavor of the peptides is improved.
Description
Technical Field
The invention belongs to the technical field of deep processing of aquatic products, and particularly relates to a method for preparing a blue clam-rich small molecular peptide.
Background
The peptide is a molecular polymer with the molecular weight of 50 Da-10 000 Da and the structure between amino acid and protein, and the peptide is called as bioactive peptide after being proved by experiments to have the biological activities of resisting oxidation, resisting bacteria, resisting viruses, resisting cancers, reducing blood pressure, cholesterol, regulating nerves, regulating immunity and the like. Active peptides are generally defined according to their function, such as antimicrobial peptides, immunogenic peptides, antihypertensive peptides, etc., and also according to their molecular weight, which is < 1000 Da called small peptides or oligopeptides, 1000 Da-5 000 Da called polypeptides, 5000 Da-10 000 Da called large peptides, and >10 000 Da, typically proteins. The small molecular peptide has higher activity than the parent protein, is easy to digest, has higher bioavailability than the protein, can regulate the vital activity of an organism, and has special physiological functions.
At present, methods for preparing peptides include enzymatic hydrolysis, microbial fermentation, artificial synthesis, and the like. The enzymatic method is the most commonly used one. The advantages of the enzymatic method include: (1) the prepared bioactive peptide has stable performance and good stability under acidic conditions and at higher temperature; (2) compared with a chemical extraction method, the enzymolysis method has the advantages of more available protein resources, simple operation of the enzymolysis process, quick extraction period and easy control of the enzymolysis degree; (3) the enzymolysis method adopts specific protease to purposefully shear the peptide fragment so as to obtain the biological polypeptide with required functional activity, and meanwhile, the yield of the polypeptide is greatly improved compared with that of a chemical extraction method. The disadvantages of the enzymatic method are mainly: in the process of preparing the bioactive polypeptide by the enzymolysis method, the molecular weight distribution of the peptide is uncontrollable, a large amount of high molecular peptides generally exist, and the bioactive polypeptide needs to be further separated, so that the waste of the peptide is caused. The process of preparing bioactive peptide by enzymolysis produces bitter peptide, and the protein produces some hydrophobic amino acids in the enzymolysis process, which combine with bitter receptor on tongue tip to produce bitter taste. The bitter taste of the zymolytic protein greatly influences the application of the bioactive peptide.
Disclosure of Invention
The technical problem to be solved by the invention is to provide a method for preparing the blue clam-rich small molecular peptide, which has the advantages of simple process, convenient operation, low molecular weight of the obtained peptide, less than 500Da of the molecular weight of most of the peptide, reduced bitter taste of the peptide and improved flavor of the peptide.
The technical scheme of the invention is as follows:
a method for preparing a blue clam-rich small molecule peptide comprises the following specific steps:
(1) Selection of raw materials
Smashing blue clam meat for later use;
(2) Ultra high pressure treatment
Adding pulverized blue clam meat into water according to the mass ratio of the blue clam meat to the water of 1, adjusting the pH value to 6.5-7.5, adding Novozym compound protease 11039, flavourzyme flavor protease, yeast powder and lactic acid bacteria, wherein the addition amount of the Novozym compound protease 11039 accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the Flavourzyme flavor protease accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the yeast powder accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the lactic acid bacteria accounts for 0.1-0.2% of the weight of the blue clam meat, wherein the mass ratio of the Novozym compound protease 11039 to the Flavourzyme flavor protease is 1;
(3) Enzymolysis
Continuously performing enzymolysis on the blue clam meat at the temperature of 45-55 ℃ for 3-4 h, inactivating the enzyme in boiling water at the temperature of 95-100 ℃ for 10-20 min, centrifuging (8000 Xg, 20 min), and taking supernatant;
(4) Spray drying
And (3) carrying out spray drying on the centrifuged supernatant under the conditions that the air inlet temperature is 150-180 ℃ and the peristaltic pump rotates 500mL/h to obtain the small-molecule active peptide powder of the blue clam meat.
Further, the ultrahigh pressure is 250MPa, and the treatment time is 60 min.
Further, when the centrifugation of the step (3) is performed, the centrifugation speed is 8000 Xg, and the centrifugation time is 20 min.
Further, when the spray drying in the step (4) is carried out, the air inlet temperature is 150-180 ℃, and the spraying amount of a peristaltic pump is 500mL/h.
Further, the maltodextrin has a DE value of 8-10.
Furthermore, maltodextrin 5% of the mass of the blue clam meat can be added during spray drying.
The invention has the following beneficial effects:
performing ultrahigh pressure treatment before enzymolysis of the blue clam meat to ensure that the blue clam protein is aggregated, crosslinked and dissociated; the ultra-high pressure treatment changes the ultraviolet absorption peak value of the protein, influences the fluorescence and the maximum emission wavelength (lambda max), and exposes a large number of amino acid residues and hydrophobic sites. The ultrahigh pressure can destroy the tertiary and quaternary structure of the protein, so that the spatial structure of the protein is changed. When high pressure continues to act, the secondary structure of the protein is damaged, the protein is denatured, chromophoric groups and areas are changed, the structural stability of the protein is influenced, and the microstructure of the protein is damaged, so that-C = O and water molecules form new hydrogen bonds, thereby increasing the degree of proteolysis, promoting the release of flavor amino acids, improving the flavor of the enzymatic hydrolysate and improving the utilization rate of the protein. Meanwhile, the ultrahigh pressure treatment also has an activating effect on the flavor protease and the compound protease, thereby reducing the using amount of the protease and increasing the content of the small molecular peptide.
The contents of free amino acid, succinic acid and AMP in the enzymatic hydrolysate subjected to ultrahigh pressure enzymolysis are increased, and the monosodium glutamate equivalent is increased. The ultrahigh pressure coupling enzymolysis has obvious influence on the taste of the enzymolysis liquid, can improve the delicate flavor and reduce the bitter and fishy smell. By combining the analysis of the electronic nose and the volatile substances, the types and the contents of main volatile substances in the ultrahigh-pressure enzymolysis liquid are increased, the types and the contents of bad flavor substances are reduced, and the composition of the volatile substances is changed, so that the effect of increasing the fragrance is achieved.
The yeast powder and the lactic acid bacteria are added in the enzymolysis process, and the enzymolysis and the fermentation are carried out under the action of ultrahigh pressure, so that the flavor of the peptide is improved, and the bitter taste of the peptide is reduced.
Drawings
FIG. 1 is a graph of the UV absorption spectrum of a blue clam protein according to an example of the present invention and a comparative example;
FIG. 2 is a graph of the intrinsic fluorescence intensity of the blue clam protein of the examples and comparative examples of the present invention;
FIG. 3 is a graph of FT-IR of a blue clam protein of examples and comparative examples of the present invention;
FIG. 4 is an electron micrograph of the blue clam protein of the inventive example and the comparative example.
Detailed Description
The present invention will be described in further detail with reference to specific examples, but the embodiments of the present invention are not limited to the scope of the examples. These examples are intended to illustrate the invention only and are not intended to limit the scope of the invention.
Example 1
(1) Standing live blue clam in artificial seawater (prepared by sea rock crystal) with mass concentration of 4% for spitting sand, changing the artificial seawater every 2 hours until the spitting sand is finished, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing;
(2) Ultra high pressure treatment
1kg of crushed blue clam meat is taken, 1kg of water is added, the pH value is adjusted to 7.0, 1g of compound protease (Novozym 11039, the enzyme activity is 1.2 AU-A/g), 1g of Flavouzyme flavor protease (the enzyme activity is 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder are added, the ultrahigh pressure is 250MPa, the temperature is 25 ℃, and the treatment time is 60min;
(3) Enzymolysis
Performing enzymolysis on the blue clam meat at the temperature of 50 ℃ for 4h, then putting the blue clam meat in boiling water at the temperature of 95-100 ℃ to inactivate enzyme for 20min, centrifuging (8000 Xg, 20 min), and taking supernatant for later use;
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the blue clam meat into the centrifuged supernatant, and performing spray drying at the air inlet temperature of 150 ℃ under the condition that the spray amount of a peristaltic pump is 500mL/h to obtain the blue clam small-molecule active peptide powder.
Example 2
(1) Standing fresh blue clam in artificial seawater (prepared by seawater crystal) with mass concentration of 4% for spitting sand, changing artificial seawater every 2 hr until the spitting sand is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing;
(2) Ultra high pressure treatment
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.0, adding 1g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder, and treating for 60min at the ultrahigh pressure of 150MPa and the temperature of 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the original blue clam meat at 50 deg.C for 4 hr, inactivating enzyme in boiling water at 95-100 deg.C for 20min, centrifuging (8000 Xg, 20 min), and collecting supernatant;
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the clam meat into the centrifuged supernatant, and spray drying at the air inlet temperature of 150 ℃ and the spray amount of a peristaltic pump of 500mL/h to obtain the clam small-molecule active peptide powder.
Example 3
(1) Standing fresh blue clam meat in artificial seawater (prepared from sea crystal) with mass concentration of 4% for spitting sand, changing the artificial seawater every 2 hr until spitting sand is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and smashing.
(2) Ultra high pressure treatment
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.0, adding 1g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder, and treating for 60min at the ultrahigh pressure of 200 MPa and the temperature of 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the original blue clam meat at 50 deg.C for 4 hr, inactivating enzyme in boiling water at 95-100 deg.C for 20min, centrifuging (8000 Xg, 20 min), and collecting supernatant.
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the blue clam meat into the centrifuged supernatant, and performing spray drying at the air inlet temperature of 150 ℃ under the condition that the spray amount of a peristaltic pump is 500mL/h to obtain the blue clam small-molecule active peptide powder.
Example 4
(1) Standing fresh blue clam in artificial seawater (prepared by seawater crystal) with mass concentration of 4%, spitting sand, changing artificial seawater every 2 hr until the spitting sand is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing.
(2) Ultra high pressure treatment
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.0, adding 1g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder, and treating for 40min at the ultrahigh pressure of 250MPa and the temperature of 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the original blue clam meat at 50 deg.C for 4 hr, inactivating enzyme in boiling water at 95-100 deg.C for 20min, centrifuging (8000 Xg, 20 min), and collecting supernatant.
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the clam meat into the centrifuged supernatant, and spray drying at the air inlet temperature of 150 ℃ and the spray amount of a peristaltic pump of 500mL/h to obtain the clam small-molecule active peptide powder.
Example 5
(1) Standing fresh blue clam meat in artificial seawater (prepared from sea crystal) with mass concentration of 4% for spitting sand, changing the artificial seawater every 2 hr until spitting sand is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and smashing.
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.0, adding 1g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder, and treating for 50 min at the ultrahigh pressure of 250MPa and the temperature of 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the original blue clam meat at 50 deg.C for 4 hr, inactivating enzyme in boiling water at 95-100 deg.C for 20min, centrifuging (8000 Xg, 20 min), and collecting supernatant.
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the clam meat into the centrifuged supernatant, and spray drying at the air inlet temperature of 150 ℃ and the spray amount of a peristaltic pump of 500mL/h to obtain the clam small-molecule active peptide powder.
Example 6
(1) Standing fresh blue clam in artificial seawater (prepared from sea crystal) with mass concentration of 4% for spitting sand, changing the artificial seawater every 2 hr until the spitting sand is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing;
(2) Ultra high pressure treatment
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 6.5, adding 2g of compound protease (Novozym 11039, the enzyme activity of 1.2 AU-A/g), 2g of Flavouzyme flavor protease (the enzyme activity of 500 LAPU/g), 2g of yeast powder and 2g of lactic acid bacteria powder, and treating for 60min under the conditions that the ultrahigh pressure is 250MPa, the temperature is 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the blue clam meat at the temperature of 45 ℃ for 3h, then putting the blue clam meat in boiling water at the temperature of 95-100 ℃ to inactivate enzyme for 15min, centrifuging (8000 Xg, 20 min), and taking supernatant for later use;
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the clam meat into the centrifuged supernatant, and spray drying at the air inlet temperature of 160 ℃ and the spray amount of a peristaltic pump of 500mL/h to obtain the clam small-molecule active peptide powder.
Example 7
(1) Standing live blue clam in artificial seawater (prepared by sea rock crystal) with mass concentration of 4% for spitting sand, changing the artificial seawater every 2 hours until the spitting sand is finished, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing;
(2) Ultra high pressure treatment
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.5, adding 1.5g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1.5g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1.5g of yeast powder and 1.5g of lactic acid bacteria powder, and treating for 60min at the ultrahigh pressure of 250MPa and the temperature of 25 ℃;
(3) Enzymolysis
Performing enzymolysis on the blue clam meat subjected to ultrahigh pressure at 55 ℃ for 3.5h, putting the blue clam meat in boiling water at 95-100 ℃ for inactivating enzyme for 10min, centrifuging (8000 Xg, 20 min), and taking supernatant for later use;
(4) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the blue clam meat into the centrifuged supernatant, and performing spray drying at the air inlet temperature of 180 ℃ under the condition that the spray amount of a peristaltic pump is 500mL/h to obtain the blue clam small-molecule active peptide powder.
Comparative example 1
(1) Standing fresh blue clam in 4% artificial seawater (prepared from sea Crystal), removing sand, changing water solution every 2 hr until sand removal is completed, taking out, draining, removing shell at 0 deg.C, taking out meat, and crushing.
(2) Enzymolysis
Taking 1kg of crushed blue clam meat, adding 1kg of water, adjusting the pH value to 7.0, adding 1g of compound protease (Novozym 11039, enzyme activity of 1.2 AU-A/g), 1g of Flavourzyme flavor protease (enzyme activity of 500 LAPU/g), 1g of yeast powder and 1g of lactic acid bacteria powder, carrying out water bath enzymolysis at 50 ℃ for 4h, carrying out enzyme deactivation at 100 ℃ for 20min, cooling, filtering, centrifuging (8000 Xg, 20 min), and taking supernatant for later use;
(3) Spray drying
Adding maltodextrin (DE value 8-10) accounting for 5% of the mass of the clam meat into the centrifuged supernatant, and spray drying at the air inlet temperature of 150 ℃ and the spray amount of a peristaltic pump of 500mL/h to obtain the clam small-molecule active peptide powder.
Table 1 shows the scoring criteria for the examples and comparative examples, with 10 trained panelists (5 men, 5 women; age 23-25 years) scoring the different products. Firstly, training the three aspects of taste, smell and color of the people; second, panelists individually received three random numbers of samples and distilled water at 25 ℃ to gargle between samples. After one group of tests was completed, the panelists were allowed to rest for 5 minutes and then another sample was again subjected to sensory evaluation.
TABLE 1 sensory evaluation criteria
Table 2 shows the results of sensory evaluation, and differences between the examples and the comparative examples indicate that the effect of ultra-high pressure coupled enzymolysis on flavor improvement is significant.
TABLE 2 sensory evaluation results
The electronic tongue can evaluate the consistency of the system on the basis of quantifying sensory data by simulating a human taste recognition system. Therefore, the sensory and electronic tongue analysis method is combined, and the taste profile of the blue clam small molecular peptide can be reflected more truly. Table 3 shows the electronic tongue umami values of the examples and comparative examples. As can be seen from the table, the examples all have higher umami values than the comparative examples. The result is consistent with the sensory evaluation result, and the ultrahigh pressure is further proved to have remarkable effect on improving the flavor of the aquatic product small molecular peptide.
TABLE 3 electronic tongue (umami) results
The amino acids can stimulate the taste of consumers by enhancing the taste characteristics of the food, and can indirectly participate in food flavor development. Wherein, free Amino Acid (FAA) is an important flavor component, and the flavor mechanism is alpha-NH 3+ And gamma-COO-to form five-membered ring structure, and there is also synergistic effect between different amino acids and between amino acid and inosinic acid and other components. In addition, glu and Arg have umami taste, are involved in various physiological activities of the human body, and play important roles therein. Table 4 shows the free amino acid compositions and contents of examples and comparative examples.
Table 4 examples and comparative examples free amino acid content
Note: ND: no detection or less than the detection limit; "*": essential amino acids; TAA, total free amino acid content; EAA, essential amino acid content; the content unit of free amino acid is mg/100mL; the unit of the taste threshold is mg/100mL
The nucleotide is an important low molecular compound with special physiological functions in organisms, and most of foods contain natural flavor-developing nucleotide. Among them, inosinic acid (IMP) and Adenosine Monophosphate (AMP) are nucleotides which contribute most to the umami taste of marine products, and the threshold values are 25mg/100g and 50 mg/100g, respectively. Table 5 shows the nucleotide contents and TAV values of examples and comparative examples.
TABLE 5 nucleotide contents and TAV values of examples and comparative examples
Monosodium glutamate Equivalents (EUCs) represent umami intensity values, i.e. when the umami value of the synergistic effect of umami amino acids and nucleotides is equal to the umami value of what amount of monosodium glutamate is present. In order to more fully evaluate the umami taste, monosodium glutamate Equivalent (EUC) may be used to evaluate umami intensity. Table 6 shows the EUC values of the examples and the comparative examples, and it can be seen from Table 6 that the monosodium glutamate equivalent values of the examples are higher than those of the comparative examples.
TABLE 6 EUC result values
Organic acids are an important taste substance and are widely studied in foods. Lactic acid and succinic acid are main flavor development substances of aquatic products. Table 7 shows the organic acid contents and TAV values of the examples and comparative examples, and it can be seen from Table 7 that the succinic acid contents of the examples are higher than those of the comparative examples.
TABLE 7 examples and comparative examples organic acid content and TAV value
The gas chromatography-mass spectrometry technology is widely applied to various fields and becomes one of the most effective means for analyzing complex mixtures. The aroma in the food is composed of various aroma volatile substances. In order to investigate the nature of gas, many studies have been made on the classification of gas, and no special odor classification method has been formed in the food industry, and it is customary to simply classify the odor into fruit aroma, vegetable, tea, meat, baking, frying, fermentation aroma, etc. according to the biological source of odor and the food processing method. Table 8 is a description of the relative volatile content and odor of the examples and comparative examples. As can be seen from Table 8, the types of alcohols in the examples are significantly increased, and the content thereof is substantially increased relative to the comparative example; the types and the content of ketone substances are reduced; the esters of butyl acetate were found to be fruity in the examples. In conclusion, the examples improve the flavor of the small molecule peptides.
TABLE 8 relative volatile component content Table
Note: "ND" means not detected
The biological enzymolysis technology is a process of decomposing protein into active components such as small molecular peptides, amino acids and the like through the catalytic action of enzyme. The degree of enzymatic hydrolysis also affects the type of peptide. The degree of hydrolysis is related to the nature of the enzyme, including the activity and type of activity of the enzyme. Ultra High Pressure (UHP) belongs to a cold processing technology, and has processing application superiority that a common processing technology cannot have compared with a shoulder processing technology. The high pressure treatment is likely to change the structure of the protein and expose new enzyme cutting sites, and has activating and inhibiting effects on the enzyme. Table 9 shows the enzyme activity values measured after the reaction system was subjected only to the ultrahigh pressure treatment in the examples and comparative examples, and it can be seen that the enzyme activities in the examples were increased as compared with those in the comparative examples.
TABLE 9 comparison of enzyme activities of examples and comparative examples
Ultraviolet absorption spectroscopy is the absorption of the ultraviolet spectrum based on the properties of chromophores and auxochromes of a substance, and can be used for identification and structural analysis of the substance. Among the 20 amino acids involved in protein composition, the R groups of tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) contain benzene ring conjugated double bond system, and show characteristic absorption band in ultraviolet region. FIG. 1 shows UV spectra of proteins treated under the pressure and time conditions of examples and comparative examples. It can be seen from the figure that the microenvironment and structure of the protein are changed after the ultrahigh pressure treatment in the examples, which may cause the protein to move or denature in a negative direction, resulting in the absorption of the protein being lower than that in the comparative examples. Second, the spatial structure of the protein was changed during the ultra-high pressure treatment due to the destruction of tryptophan, tyrosine and phenylalanine, so that it hardly peaked at 250 to 280 nm, compared to the control group.
The primary endogenous fluorescence analysis is the tryptophan (Trp) residue, which can be excited at 295 nm, thus eliminating interference from tyrosine residues. The ultra-high pressure treatment causes changes in protein conformation and even denaturation of protein molecules. In the process, the microenvironment and the position of the endogenous fluorescent chromophore in part of the amino acids are correspondingly changed. Therefore, the study of endogenous fluorescence spectroscopy is an effective means to monitor the effect of ultra-high pressure treatment on protein conformation. FIG. 2 shows fluorescence spectra of processed Cyclina sinensis protein using the conditions of pressure and time of examples and comparative examples. It can be seen that the ultra-high pressure in the examples leads to different conformational changes in the protein structure, increasing the residual amount of tryptophan in the hydrophobic microenvironment. Meanwhile, the ultrahigh pressure can change the spatial arrangement of protein molecules, destroy the interaction between hydrophobin molecules, cause the exposure of hydrophobic groups and further promote the hydrolysis of protein.
The infrared spectrum is an absorption spectrum of molecular vibration, chemical bonds in molecules have various vibration modes, and the obtained spectrum reflects the overall information of all secondary structures. All amino acid residues in the protein molecule are infrared chromophores, and the size of the protein molecule has little influence on the infrared determination of the proteinThe region has a plurality of characteristic absorption bands, wherein an amide I band (1600 to 1700 cm) -1 ) Is most valuable for studying its secondary structure. FIG. 3 is a graph of the infrared spectrum of the blue clam protein after treatment using the conditions of pressure and time of examples and comparative examples. As can be seen from the figure, several characteristic absorption peaks appear in the infrared region, blue clam protein 2918.30 cm -1 (amide B band) 1658.78 cm -1 (amide I band, -C = O), 1539.20 cm -1 The absorption peaks appear at the (amide II band). In the ultrahigh pressure treatment process, water molecules enter protein molecules under the action of high pressure, so that the internal structure of macromolecules is changed in a certain series, and the ultrahigh pressure treatment changes the secondary structure of the protein, so that the hydrolysis of the protein can be influenced.
A Scanning Electron Microscope (SEM) is a microscopic morphology observation means between a transmission electron microscope and an optical microscope, and can directly utilize the material performance of the surface material of a sample to carry out microscopic imaging. FIG. 4 is an electron micrograph at 20000 times after treatment of Cyclina protein using example pressure and time conditions and without ultra high pressure treatment of comparative example.
In summary, in the embodiment, the enzyme activity of the protease can be promoted by applying a certain pressure, the hydrolysis degree is increased, the protein utilization rate is improved, and the resource waste is reduced.
In the embodiment, the ultrahigh pressure treatment can change the tri-quaternary structure of the protein, and even the secondary structure can be changed. After high pressure is applied, the tertiary structure is destroyed, the secondary structure is exposed, the alpha helical structure which occupies 3.6 amino acid residues is changed, the amino acid residues are exposed on the surface and are easy to be dissociated, so that the hydrolysis degree of protein is improved, the content of flavor-developing substances in the enzymatic hydrolysate is increased, and the flavor of the enzymatic hydrolysate is improved.
The molecular weight section of the peptide is between 5000 and 50. The polypeptide with the molecular weight section of 1000-50 is called small peptide, oligopeptide, also called small molecule active polypeptide. Biologists refer to peptides as "chains of amino acids" and small molecule active polypeptides as "bioactive peptides". Dipeptides (dipeptides), tripeptides (tripeptides), and even polypeptides (polypeptides) are common. The mixture rich in small molecule peptides and amino acids with different molecular weights produced by acid-base hydrolysis or enzymolysis is called composite small molecule peptide in taste. The composite small molecular peptide not only has high nutritive value, but also has wide biological functions. Table 10 shows the molecular weight distributions of the peptides of the examples and comparative examples, from which it can be seen that the majority of the small peptides in the examples are in the range <500 Da.
TABLE 10 molecular weight distribution of peptides of examples and comparative examples
Claims (7)
1. A method for preparing a blue clam-rich small molecule peptide is characterized by comprising the following steps:
the method comprises the following specific steps:
(1) Selection of raw materials
Pulverizing the blue clam meat for later use;
(2) Ultra high pressure treatment
Adding ground blue clam meat into water according to the mass ratio of the blue clam meat to the water of 1, adjusting the pH value to be 6.5-7.5, adding Novozym compound protease, flavouzyme flavor protease, yeast powder and lactic acid bacteria, wherein the addition amount of the Novozym compound protease accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the Flavozym flavor protease accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the yeast powder accounts for 0.1-0.2% of the weight of the blue clam meat, the addition amount of the lactic acid bacteria accounts for 0.1-0.2% of the weight of the blue clam meat, the mass ratio of the Novozym compound protease to the Flavozym flavor protease is 1, the mass ratio of the yeast powder to the lactic acid bacteria is 1;
(3) Enzymolysis
Continuously performing enzymolysis on the blue clam meat at the temperature of 45-55 ℃ for 3-4 h, inactivating the enzyme in boiling water at the temperature of 95-100 ℃ for 10-20 min, centrifuging, and taking supernatant;
(4) Spray drying
And (4) centrifuging the supernatant, and performing spray drying to obtain the blue clam small-molecule active peptide powder.
2. The method for preparing the blue clam rich small molecule peptide according to claim 1, which is characterized in that: the ultrahigh pressure is 250MPa, and the treatment time is 60 min.
3. The method for preparing the blue clam rich small molecule peptide according to claim 1, which is characterized in that: when the step (3) is used for centrifugation, the centrifugation speed is 8000 Xg, and the centrifugation time is 20 min.
4. The method for preparing the blue clam rich small molecule peptide according to claim 1, which is characterized in that: and (4) during spray drying, the air inlet temperature is 150-180 ℃, and the spraying amount of the peristaltic pump is 500mL/h.
5. The method for preparing the blue clam rich small molecule peptide according to claim 1, which is characterized in that: during spray drying, maltodextrin 5% of the mass of the blue clam meat is also added.
6. The method for preparing the blue clam rich small molecule peptide according to claim 5, wherein: the DE value of the maltodextrin is 8-10.
7. The method for preparing the blue clam rich small molecule peptide according to claim 1, which is characterized in that: the Novozym compound protease is Novozym compound protease 11039.
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