CN115093472B - Sericin peptide with moisturizing function and preparation method and application thereof - Google Patents
Sericin peptide with moisturizing function and preparation method and application thereof Download PDFInfo
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
- C07K14/43586—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects from silkworms
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
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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
The invention provides sericin peptide with a moisturizing function and a preparation method and application thereof. The invention provides a sericin peptide with a moisturizing function, which at least comprises peptide segments GGS, AS and GS; based on the mass of the sericin peptide, the content of the peptide segment GGS is more than or equal to 0.80 percent, the content of the peptide segment AS is more than or equal to 0.20 percent, and the content of the peptide segment GS is more than or equal to 0.50 percent. The sericin peptide provided by the invention contains three functional peptide segments of GGS, AS and GS, and has an obvious moisturizing effect.
Description
Technical Field
The invention relates to a sericin peptide with a moisturizing function, a preparation method and application thereof, and relates to the technical field of fibroin processing.
Background
For a long time, silk is mainly used as a textile raw material, the content of protein in the silk is more than 98%, researchers begin to pay more attention to new application of the silk from the end of the seventies of the last century, the silk is applied to daily chemical industry, medicines, biological materials, health-care functional foods and other fields to different degrees successively at present, and the development of the silk protein becomes a research hotspot in recent years.
The fibroin mainly comprises fibroin and sericin, wherein the mass of the fibroin accounts for 70-80% of the total mass of the fibroin, is insoluble in water and ethanol, has a compact and ordered aggregation structure, and can be dissolved only by destroying the structure with a strong polar solvent; the sericin accounts for 20-30% of the total mass of the fibroin, is globular protein, has a relative molecular mass of 1.4-31.4 ten thousand, is composed of 18 amino acids, has the highest serine content of about 30%, is easily soluble in water, and has good hygroscopicity; with the intensive research on sericin, sericin has excellent cell affinity and biocompatibility, and has the functions of tyrosinase inhibitory activity, ultraviolet resistance, moisturizing, beautifying, hair care and the like.
Serine is a moisturizing factor naturally existing in human skin, has a good water molecule absorption function and is commonly used as a basic moisturizing agent in cosmetics, and sericin or fibroin rich in serine has the structural advantages of natural moisturizing, natural protein nutrition and skin care functional attributes, and has potential in developing moisturizing cosmetic raw materials.
At present, the deep processing method aiming at the fibroin focuses on removing sericin at high temperature and high pressure, and uses acid or alkali hydrolysis to obtain silk peptide, or uses an acid-base combined enzymolysis method to process the fibroin to prepare the fibroin peptide, the content of free amino acid in the obtained fibroin peptide or the fibroin peptide is high and is up to more than 13%, and harmful substances or certain pollution can be generated in the acid-base reagent treatment process.
Disclosure of Invention
The invention provides a sericin peptide with a moisturizing function, which shows good efficacy in the aspect of moisturizing through functional peptide segments, glycine-serine (Gly-Gly-Ser, GGS), alanine-serine (Ala-Ser, AS) and glycine-serine (Gly-Ser, GS) with specific mass contents.
The invention also provides a preparation method of the sericin peptide with the moisturizing function, wherein the sericin peptide prepared by the preparation method contains functional peptide segments with specific mass content, glycine-serine (Gly-Gly-Ser, GGS), alanine-serine (Ala-Ser, AS) and glycine-serine (Gly-Ser, GS), so that the sericin peptide shows good efficacy in the moisturizing aspect.
The invention also provides application of the sericin peptide in a moisture-preserving product.
The invention provides a sericin peptide with a moisturizing function, which at least comprises peptide segments GGS, AS and GS;
based on the mass of the sericin peptide, the content of the peptide segment GGS is more than or equal to 0.80 percent, the content of the peptide segment AS is more than or equal to 0.20 percent, and the content of the peptide segment GS is more than or equal to 0.50 percent.
In addition, in the sericin peptide provided by the invention, besides the special peptide segment, the content of protein in the sericin peptide is more than or equal to 85 percent, the content of free amino acid is less than or equal to 5 percent, the content of acid soluble protein is more than or equal to 80 percent, and the content of components with the molecular weight of less than 1000 is more than or equal to 85 percent.
In a specific embodiment, the sericin peptide is obtained by taking pupa-free silkworm cocoons as raw materials and sequentially carrying out sericin dissolution, fermentation, enzymolysis, adsorption decoloration and drying treatment;
wherein the fermentation uses candida utilis;
the enzymolysis comprises enzymolysis by using alkaline protease and neutral protease.
In a second aspect, the present invention provides a method for preparing any one of the sericin peptides, which comprises the following steps:
1) Dissolving out sericin in pupa-free silkworm cocoons to obtain a sericin solution;
2) Fermenting the sericin solution by using candida utilis to obtain sericin fermentation liquor after the fermentation is finished;
3) Adding alkaline protease and neutral protease into the sericin fermentation liquor for enzymolysis, and obtaining sericin enzymolysis liquid after enzymolysis is finished;
4) And adding active carbon into the sericin enzymolysis liquid for adsorption decoloration treatment, collecting filtrate after the treatment is finished, and drying the filtrate to obtain the sericin peptide.
In one embodiment, fig. 1 is a schematic flow chart of a method for preparing a sericin peptide according to an embodiment of the present invention, and as shown in fig. 1, the method specifically includes the following steps:
step 1) dissolving out sericin in pupa-free silkworm cocoons to obtain a sericin solution;
taking commercially available pupa-free silkworm cocoons as raw materials, and mixing the raw materials in a mass ratio of 1:10-30 mixing pupa-free silkworm cocoon with pure water, and treating at 110-125 deg.C for 10-90min, wherein sericin in silkworm cocoon is dissolved into pure water to obtain sericin solution.
Step 2) fermenting the sericin solution by using candida utilis to obtain sericin fermentation liquor after the fermentation is finished;
sterilizing the sericin solution obtained in the step 1), wherein the sterilization can be performed according to the conventional technical means in the field, for example, the sterilization is performed at 115-121 ℃ for 15-30min, and before the sterilization, the sericin solution can be concentrated, and specifically, a rotary evaporator can be used for removing part of water.
After sterilization, adding candida utilis into the sericin solution for fermentation, wherein the growth and metabolism process of the candida utilis can generate abundant short peptides and enzymes, which are beneficial to enriching enzyme systems of the next enzymolysis process, and simultaneously provides exogenous peptides which can be generated by non-silkworm cocoons, and the candida utilis does not generate ethanol under strict aerobic conditions, so that the candida utilis has good safety, and particularly the candida utilis (i)Candidautilis) Can be purchased from China center for culture collection and management of industrial microorganisms (CICC), the strain preservation number is CICC31170, and the colony number of the candida utilis is 10 based on the quality of the pupa-free silkworm cocoons per gram 5 -10 7 And controlling the fermentation temperature to be 28-32 ℃, carrying out shake culture, fermenting for 36-72h, filtering thalli after the fermentation is finished, and collecting fermentation liquor to obtain sericin fermentation liquor.
Step 3) adding alkaline protease and neutral protease into the sericin fermentation liquor for enzymolysis, and obtaining sericin enzymolysis liquor after enzymolysis is finished;
adding alkaline protease and neutral protease into the sericin fermentation liquor for enzymolysis, so that peptide bonds in the sericin are cut off to obtain short peptides, wherein in the enzymolysis process, based on per gram of pupa-free silkworm cocoons, the enzyme activity of the alkaline protease is 3000-6000U, the enzyme activity of the neutral protease is 500-1500U, the enzymolysis temperature is controlled to be 45-55 ℃, the time is 4-6 hours, and the sericin enzymolysis liquor is obtained after the enzymolysis is finished.
Step 4) adding activated carbon into the sericin hydrolysate to perform adsorption decoloration treatment, collecting filtrate after the treatment is finished, and drying the filtrate to obtain the sericin peptide;
after enzymolysis, raising the temperature of sericin enzymolysis liquid to 85-95 ℃, carrying out heat preservation treatment for 15-25min for enzyme deactivation, filtering to remove insoluble substances such as macromolecular protein and the like after enzyme deactivation, specifically using a ceramic membrane with the pore diameter of 10-20 KD, collecting supernatant, adding activated carbon into the supernatant for adsorption decoloration treatment to adsorb pigments in the supernatant, removing the activated carbon after adsorption treatment, collecting filtrate and drying to obtain sericin peptide, wherein the drying can be carried out in a spray drying tower, the air inlet temperature is controlled to be 120-140 ℃, and the air outlet temperature is controlled to be 80-100 ℃.
In a third aspect, the present invention provides the use of a sericin peptide as defined in any one of the above in a moisture-retaining product.
The sericin peptide provided by the invention definitely contains functional peptide segments of GGS, AS and GS, the content of the peptide segment GGS is more than or equal to 0.80%, the content of the peptide segment AS is more than or equal to 0.20%, and the content of the peptide segment GS is more than or equal to 0.50%.
The implementation of the invention has at least the following advantages:
1. the sericin peptide provided by the invention definitely contains functional peptide segments of GGS, AS and GS, the content of the peptide segment GGS is more than or equal to 0.80%, the content of the peptide segment AS is more than or equal to 0.20%, and the content of the peptide segment GS is more than or equal to 0.50%, so that the sericin peptide has an obvious moisturizing effect.
2. In the preparation process of the sericin peptide, acid and alkali are not needed for treatment, and the sericin peptide has the characteristics of environmental friendliness.
Drawings
In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the drawings needed to be used in the description of the embodiments or the prior art will be briefly introduced below, and it is obvious that the drawings in the following description are some embodiments of the present invention, and for those skilled in the art, other drawings can be obtained according to these drawings without creative efforts.
FIG. 1 is a schematic flow chart of a method for preparing a sericin peptide according to an embodiment of the present invention;
FIG. 2 is a result of a moisture retention rate test of sericin peptides provided in examples of the present invention and comparative examples 1 to 4;
FIG. 3a shows the results of chromatographic assay of GGS standard;
FIG. 3b is a standard curve for GGS;
FIG. 4a shows the result of chromatographic detection of AS standard;
FIG. 4b is a standard curve of AS;
FIG. 5a is the chromatographic detection of GS standard;
FIG. 5b is a standard curve for GS;
FIG. 6a shows the results of the chromatographic detection of GGS in sericin peptide according to an embodiment of the present invention;
FIG. 6b shows the result of chromatographic detection of AS in sericin peptide according to an embodiment of the present invention;
FIG. 6c shows the result of chromatographic detection of GS in sericin peptide according to an embodiment of the present invention;
FIG. 7a is a chromatographic test result of GGS in sericin peptide according to comparative example 1;
FIG. 7b is the result of chromatographic determination of AS in sericin peptide according to comparative example 1;
FIG. 7c shows the results of chromatographic detection of GS in sericin peptide according to comparative example 1;
FIG. 8a is a result of chromatographic detection of GGS in sericin peptide according to comparative example 2;
FIG. 8b is the result of chromatographic determination of AS in sericin peptide according to comparative example 2;
FIG. 8c is a chromatographic test result of GS in the sericin peptide provided in comparative example 2 according to the present invention;
FIG. 9a shows the results of the chromatographic assay for GGS in sericin peptide according to comparative example 3;
FIG. 9b shows the result of chromatographic determination of AS in sericin peptide according to comparative example 3;
FIG. 9c shows the result of the chromatographic detection of GS in the sericin peptide as provided in comparative example 3 according to the invention;
FIG. 10a is a chromatogram detection result of GGS in sericin peptide according to the comparative example 4;
FIG. 10b shows the result of chromatographic determination of AS in sericin peptide according to comparative example 4;
FIG. 10c shows the result of the chromatographic detection of GS in the sericin peptide as provided in comparative example 4 of the invention;
fig. 11 is a result of moisture retention testing of sericin peptide and a characteristic peptide fragment provided in an embodiment of the invention.
Detailed Description
In order to make the objects, technical solutions and advantages of the present invention more apparent, the technical solutions in the embodiments of the present invention will be clearly and completely described below with reference to the embodiments of the present invention. All other embodiments, which can be derived by a person skilled in the art from the embodiments given herein without making any creative effort, shall fall within the protection scope of the present invention.
The pupa-free silkworm cocoons used in the following examples and comparative examples were obtained by procurement; candida utilis (A), (B)Candidautilis) Purchased from China center for culture collection and management of Industrial microorganisms (CICC), with the strain preservation number CICC31170; alkaline protease is purchased from sigma-Aldrich, neutral protease is purchased from Pongpo bioengineering Co., ltd, activated carbon is purchased from Guangdong Hua-activated carbon Co., ltd, and sodium hydroxide is purchased from Kangpo chemical industry.
Examples
The preparation method of the sericin peptide provided by the embodiment comprises the following steps:
step 1, weighing 100g of pupa-free silkworm cocoons, putting the pupa-free silkworm cocoons into a crusher for crushing, cleaning the pupa-free silkworm cocoons by using pure water, removing floating dust and impurities on the surfaces of the pupa-free silkworm cocoons, and removing cleaning water, wherein the mass ratio of the cleaning water to the pupa-free silkworm cocoons is 1: mixing with purified water 20, treating at 121 deg.C under constant pressure for 30min, removing insoluble substances, and collecting supernatant.
Concentrating the supernatant with a rotary evaporator, controlling the temperature at 80 deg.C and the vacuum degree at-0.1 MPa, taking out the residual solution after half of water in the solution is evaporated, and sterilizing the residual solution at 121 deg.C for 15min to obtain sericin protein solution;
step 2, controlling the temperature of the sericin solution at 28-32 ℃, and adding the activated bacteria with the number of 10 8 Candida utilis (corresponding to 10) 6 /g of silkworm cocoon without pupa), continuously fermenting for 48 hours at 200rpm of a shaking table, and obtaining sericin fermentation liquor after the fermentation is finished;
step 3, adjusting the pH value of the sericin fermentation liquor to 9.0 by using a NaOH solution, then simultaneously adding alkaline protease and neutral protease, wherein the enzyme activity of the added alkaline protease is 5000U and the enzyme activity of the added neutral protease is 1000U based on each gram of pupa-free silkworm cocoons, carrying out enzymolysis for 6 hours at 50 ℃, and obtaining a sericin enzymolysis liquid after the enzymolysis is finished;
and 4, raising the temperature of the sericin hydrolysate to 95 ℃, keeping the temperature for 15min to inactivate protease, filtering the sericin hydrolysate by adopting a ceramic membrane with the aperture of 10KD, collecting supernatant, concentrating, specifically adopting a rotary evaporator, setting the temperature to be 80 ℃, setting the vacuum degree to be-0.1 MPa, and rotationally evaporating 920mL of water in filtrate.
Taking out the rest material liquid, heating to 70 deg.C, adding 4g of active carbon, stirring at 70 deg.C for 1 hr, adsorbing and decolorizing, removing active carbon after treatment, and collecting supernatant;
and (3) sending the supernatant into a spray drying tower (BH-100 pressure spray drying tower, jiangsu Bohong) for spray drying, and controlling the air inlet temperature to be 140 ℃ and the air outlet temperature to be 90 ℃ to obtain the sericin peptide.
Comparative example 1
The method provided by the comparative example can be referred to as an example, and is different from the method in that in the step 3, the enzymolysis time is 4 hours, specifically, the pH of the sericin fermentation liquor is adjusted to 9.0 by using a NaOH solution, meanwhile, alkaline protease and neutral protease are added, the enzymolysis is carried out for 4 hours at 50 ℃, and sericin enzymolysis liquid is obtained after the enzymolysis is finished.
Comparative example 2
The method provided by the comparative example can refer to the example, and is different from the method in that only alkaline protease is used for enzymolysis in the step 3, specifically, the pH of the sericin fermentation liquor is adjusted to 9.0 by using NaOH solution, the alkaline protease is added for enzymolysis for 6 hours at 50 ℃, and the sericin enzymolysis liquid is obtained after the enzymolysis is finished.
Comparative example 3
The method provided by the comparative example can refer to the example, and is different from the method in that only alkaline protease is used for enzymolysis in the step 3, specifically, the pH of the sericin fermentation liquor is adjusted to 9.0 by using NaOH solution, the alkaline protease is added for enzymolysis for 4 hours at 50 ℃, and the sericin enzymolysis liquid is obtained after the enzymolysis is finished.
Comparative example 4
The method provided by the comparative example can be referred to the example, and is different from the method in that only neutral protease is used for enzymolysis in step 3, specifically, the pH of the sericin fermentation liquor is adjusted to 9.0 by using NaOH solution, the neutral protease is added, enzymolysis is carried out for 4 hours at 50 ℃, and sericin enzymolysis liquid is obtained after the enzymolysis is finished.
The physicochemical indexes of the sericin peptides provided in the examples and the comparative examples 1-4 are detected by the following detection method, and the detection results are shown in table 1:
1. moisture and ash content detection: determining the moisture content by adopting a national standard method GB 5009.3-2010; the ash content is determined by adopting a national standard method GB 5009.4-2016.
2. Protein, peptide content and free amino acid detection: determining the content of protein (dry basis) by adopting a national standard method GB 5009.5-2010; and determining the content of acid-soluble protein, the content of free amino acid and the content of peptide by referring to a national standard method GB 22729-2008.
3. Detection of the distribution of the different molecular weight components: 5 peptide standards of ethionine-ethionine (molecular weight 189), ethionine-tyrosine-arginine (molecular weight 451), bacillase (molecular weight 1450), aprotinin (molecular weight 6500) and cytochrome C (molecular weight 12500) are respectively prepared into 0.1% (M/V) solution, filtered by a polytetrafluoroethylene filter membrane with the pore diameter of 0.2 mu M, and then subjected to analysis by a high performance liquid chromatograph (LC-20 AD type high performance liquid chromatograph, shimadzu corporation, japan), and the mobile phase: v (acetonitrile): v (water): v (trifluoroacetic acid) =45:55:0.1; sample introduction volume: 10 mu L of the solution; flow rate: 0.5mL/min; detection wavelength: 220nm; column temperature: detecting at 30 ℃ by using an ultraviolet detector; the data was processed using GPC software. Substituting the chromatographic data of the sample into a correction curve equation for calculation to obtain the peptide molecular weight and the distribution range of the sample. The relative percentages of the components in different molecular weight ranges can be calculated by peak area normalization.
TABLE 1 examples and physicochemical indices and yields of sericin peptides provided in comparative examples 1 to 4
As can be seen from table 1, the sericin peptide provided in the examples has a high peptide content, a low proportion of components having a relative molecular weight of 1000 or less, and a low content of free amino acids compared to the existing silk peptide or silk peptide products, which is advantageous for human absorption.
The moisturizing performance of the sericin peptides provided in the examples and the comparative examples 1-4 is tested by the following method:
mixing ammonium sulfate (NH) 4 ) 2 SO 4 (analytically pure, shanghai reagent-plant) dissolved in water to prepare saturated ammonium sulfate (NH) 4 ) 2 SO 4 Aqueous solution, placed in an air-dryer environment simulating 81% relative humidity (r.h.). Preparing the sample to be tested into 2% water solution, weighing with pure water, 2% serine, 2% glycerol, 5% glycerol, and 0.5% HA as control group, and recording as W 0 Sucking 200 mu L of the mixture, adding the mixture into a watch glass pasted with 3M adhesive tape, weighing the mixture after 4 hours and 8 hours respectively, and recording the weighing as W n Moisture retention (%) according to the formula = (W) n -W 0 )÷W 0 * Calculating to obtain the moisture retention rate by 100 percent; the results are expressed as mean. + -. Standard deviation and data analysis is performed using Tukey's method, p<0.05 indicates significant difference, marked by significant letters, with the same lettersI.e. without significant difference, and without the same letter, i.e. with significant difference, the test results are shown in fig. 2.
As shown in fig. 2, in an environment of 81% relative humidity (r.h.), the sericin peptide provided in the example was left for 4h and left for 8h, and pure water was used as a negative control, and the moisturizing ratio of the sericin peptide provided in the example was significantly different from that of pure water and comparative examples 1 to 4, and was higher than that of glycerol at the same concentration, but was not significantly different from that of serine, 2% and 5% glycerol, and 0.5% HA at the same concentration, which indicates that the sericin peptide provided in the example had the moisturizing effect equivalent to that of a 2% serine solution, 2% glycerol, 5% glycerol, and 5% HA.
And (III) identifying the characteristic structures of the sericin peptides provided in the examples and comparative examples 1 to 4 by the following method:
20.0mg of GGS, AS and GS standard substance powder (purchased from Suzhou Qiangyao Biotechnology Co., ltd., purity of more than or equal to 98%) is accurately weighed respectively, dissolved by adding water, uniformly mixed by vortex, and prepared into standard stock solution of 200 mug/mL after constant volume is 100 mL. And respectively taking 500 mu L of the standard stock solution, and fixing the volume to 10mL to obtain 10 mu g/mL of mixed standard intermediate working solution. The mixed standard intermediate working solution is gradually diluted by pure water to a series of standard working solutions of 1.95, 3.91, 7.81, 15.63, 31.25, 62.5, 125, 250 and 500 ng/mL.
The peptide sample was prepared at 20.0mg/mL with purified water, and diluted 10 with purified water 3 And multiplying and measuring.
The test was carried out using an ultra high performance liquid chromatograph NexeraX2 coupled with a triple quadrupole mass spectrometer system (shimadzu, japan), which specifically included: LC-30AD x2 infusion pump, SIL-30AC autosampler, CTO-20AC column incubator, CBM-20A system controller, LCMS-8060 triple quadrupole mass spectrometer, labSolutionsVer.5.91 chromatographic workstation. XS205DU analytical balance (mettler toledo, usa); QL-901 vortex mixer (Linebel instruments manufacturing Co., ltd., china).
Liquid chromatography conditions: and (3) chromatographic column: inertsilODS-3 (5 μm, 2.1X 250mm); mobile phase: a is 0.1% formic acid water solution, B is 0.1% formic acid acetonitrile solution; gradient elution procedure: 0-15minB0-50%;15-20minB50-100%;20-25minB100%;25.1 to 35minB0 percent; flow rate: 0.2mL/min; sample introduction volume: 5 mu L of the solution; column temperature: 40 ℃.
Mass spectrum conditions: ionization mode: ESI, positive ion mode; ion spray voltage: +4.5kV; flow rate of atomizing gas: nitrogen gas is 3.0L/min; heating airflow rate: nitrogen gas is 10L/min; flow rate of drying gas: nitrogen gas is 10L/min; DL temperature: at 250 ℃; heating module temperature: 400 ℃; ion source temperature: 300 ℃; scanning mode: multiple Reaction Monitoring (MRM); residence time: 100ms; delay time: 3ms; MRM parameters: see table 2.
TABLE 2 MRM optimization parameters for standards
* Representing quantitative ions
FIGS. 3a to 5b show the results of chromatographic detection and standard curves of GGS, AS and GS standards, respectively, FIGS. 6a to 10c show the results of chromatographic detection of characteristic peptide fragments in sericin peptides provided in examples and comparative examples 1 to 4, respectively, and it can be seen from FIGS. 3a to 10c that the examples and comparative examples 1 to 3 each contain three characteristic peptide fragments, while the comparative example 4 contains only a trace amount of characteristic peptide fragments GGS and GS, and the calculation results are shown in Table 3 by calculating the content of characteristic structures in each group of sericin peptides based on the standard curves.
TABLE 3 content of three characteristic peptides in examples and comparative examples 1-4
According to the results of table 3, compared with comparative examples 1-4, the sericin peptide provided in the example has three characteristic peptide segments of GGS, AS and GS at the same time, and the content is obviously superior to that of comparative examples 1-4, which indicates that the preparation method provided in the example can effectively carry out enzymolysis on fibroin and effectively obtain three characteristic peptide segments of GGS, AS and GS.
(IV) the functions of the characteristic structures of the sericin peptides provided in examples and comparative examples 1 to 4 were evaluated as follows:
three characteristic peptide fragment standard products of GGS, AS and GS and sericin peptide provided in the example are prepared into 0.4% aqueous solution, and a moisturizing rate test is carried out by a moisturizing function evaluation method provided in the second part (part II), and the test result is shown in fig. 11.
AS shown in fig. 11, pure water is used AS a negative control, the sericin peptide provided in the example has a certain moisture retention function, and the change trend of the moisture retention rate of the sericin peptide after being placed for 4h and 8h is consistent with that of the peptide segments GGS, AS and GS.
Finally, it should be noted that: the above embodiments are only used to illustrate the technical solution of the present invention, and not to limit the same; while the invention has been described in detail and with reference to the foregoing embodiments, it will be understood by those skilled in the art that: the technical solutions described in the foregoing embodiments may still be modified, or some or all of the technical features may be equivalently replaced; and the modifications or the substitutions do not make the essence of the corresponding technical solutions depart from the scope of the technical solutions of the embodiments of the present invention.
Claims (7)
1. The sericin peptide with the moisturizing function is characterized by comprising peptide segments GGS, AS and GS;
based on the mass of the sericin peptide, the content of the peptide segment GGS is more than or equal to 0.80 percent, the content of the peptide segment AS is more than or equal to 0.20 percent, and the content of the peptide segment GS is more than or equal to 0.50 percent;
the sericin peptide is obtained by taking pupa-free silkworm cocoons as raw materials and sequentially carrying out sericin dissolution, fermentation, enzymolysis, adsorption decoloration and drying treatment;
wherein the fermentation uses candida utilis;
the enzymolysis comprises enzymolysis by using alkaline protease and neutral protease;
based on each gram of pupa-free silkworm cocoon, the enzyme activity of the alkaline protease is 3000-6000U, and the enzyme activity of the neutral protease is 500-1500U;
the temperature of the enzymolysis is 45-55 ℃, and the time is 4-6h.
2. The sericin peptide according to claim 1, wherein the sericin peptide comprises 85% or more of protein, 5% or less of free amino acid, 80% or more of acid-soluble protein and 85% or more of components having a relative molecular weight of 1000 or less.
3. A method for preparing the sericin peptide as defined in any one of claims 1 to 2, comprising the steps of:
1) Dissolving out sericin in the pupa-free silkworm cocoons to obtain a sericin solution;
2) Fermenting the sericin solution by using candida utilis to obtain sericin fermentation liquor after the fermentation is finished;
3) Adding alkaline protease and neutral protease into the sericin fermentation liquor for enzymolysis, and obtaining sericin enzymolysis liquid after enzymolysis is finished;
4) Adding activated carbon into the sericin hydrolysate for adsorption decoloration treatment, collecting filtrate after the treatment is finished, and drying the filtrate to obtain the sericin peptide;
based on per gram of the pupa-free silkworm cocoons, the enzyme activity of the alkaline protease is 3000-6000U, and the enzyme activity of the neutral protease is 500-1500U;
the temperature of the enzymolysis is 45-55 ℃, and the time is 4-6h.
4. The method according to claim 3, wherein step 1) comprises: according to the mass ratio of 1:10-30, mixing the pupa-free silkworm cocoons with pure water, and treating at 110-125 ℃ for 10-90min to dissolve out sericin in the pupa-free silkworm cocoons to obtain the sericin solution.
5. The method of claim 3, wherein the amount of the surfactant is controlled on a per gram basisThe pupa-free silkworm cocoon has a colony number of 10 5 -10 7 And (4) respectively.
6. The method according to claim 3 or 5, wherein the fermentation temperature is 28-32 ℃ and the fermentation time is 36-72h.
7. Use of the sericin peptide as set forth in any one of claims 1-2 in a moisture-retaining product.
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| PCT/CN2022/133579 WO2024040769A1 (en) | 2022-08-25 | 2022-11-22 | Sericin protein peptide having moisturizing function, method for preparing same, and use thereof |
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Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008289370A (en) * | 2007-05-22 | 2008-12-04 | Dai Ichi Kogyo Seiyaku Co Ltd | Method for producing aqueous solution of sericin, and aqueous solution of sericin |
| WO2010100569A2 (en) * | 2009-01-23 | 2010-09-10 | Biology Centre As Cr, V.V.I. | Natural biodegradable adhesive from the silk |
| CN102978270A (en) * | 2012-12-26 | 2013-03-20 | 蒋立宪 | Preparation method for tussah silk glutin powder |
| CN112409469A (en) * | 2020-11-04 | 2021-02-26 | 付俊 | Extraction method of silk peptide |
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| FR2698869B1 (en) * | 1992-12-09 | 1995-02-24 | Morelle Jean | Acylamino acids obtained from fibers from Bombyx Mori. |
| JP2005052066A (en) * | 2003-08-04 | 2005-03-03 | Japan Science & Technology Agency | Method for producing acylated sericin |
| CN115093472B (en) * | 2022-08-25 | 2023-01-06 | 中国食品发酵工业研究院有限公司 | Sericin peptide with moisturizing function and preparation method and application thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008289370A (en) * | 2007-05-22 | 2008-12-04 | Dai Ichi Kogyo Seiyaku Co Ltd | Method for producing aqueous solution of sericin, and aqueous solution of sericin |
| WO2010100569A2 (en) * | 2009-01-23 | 2010-09-10 | Biology Centre As Cr, V.V.I. | Natural biodegradable adhesive from the silk |
| CN102978270A (en) * | 2012-12-26 | 2013-03-20 | 蒋立宪 | Preparation method for tussah silk glutin powder |
| CN112409469A (en) * | 2020-11-04 | 2021-02-26 | 付俊 | Extraction method of silk peptide |
Non-Patent Citations (2)
| Title |
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| Enzymatic production of bioactive peptides from sericin recovered from silk industry wastewater;Wu, JH等;《Process Biochemistry》;20081231;第43卷(第5期);第480-487页 * |
| 丝胶蛋白酶解产物的保湿与美白作用研究;靳春平等;《日用化学工业》;20140731;第44卷(第7期);第394-397页 * |
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