Cell active peptide composition with anti-allergy and red fading effects as well as preparation method and medical beauty application thereof

Abstract

The invention provides a cell active peptide composition with anti-allergy and red fading effects and a preparation method and medical beauty application thereof, and belongs to the technical field of medicine and beauty. The composition is prepared from dipeptide-1, tripeptide-1, palmitoyl tripeptide-8, palmitoyl tetrapeptide-7, sh-pentapeptide-1, hydrolyzed silk, a mussel extract, dipeptide-2, acetyl tetrapeptide-3, ceramide, 4-tert-butyl cyclohexanol, bisabolol, sodium hyaluronate and the like. The composition can repair skin barrier injury; the skin nerve dysfunction is improved; the immune function is enhanced, and skin inflammation is eliminated; the elasticity of capillary walls is enhanced, and couperose skin is repaired. The composition disclosed by the invention is applied to skin medicine and skin beauty, can effectively reduce the skin redness average value, the red area and the redness a value, strengthens the brick wall structure, is mild in effect, and has the functions of resisting allergy, fading red, relieving, calming and regulating immunity.

Description

Technical Field

[0001] The present invention belongs to the field of medicine and cosmetology technology, and specifically relates to a cell active peptide composition with anti-allergic and redness-removing effects, a preparation method thereof, and medical and cosmetology applications. Background Art

[0002] Skin, as the largest organ in the human body, plays multiple roles: it is our defense shield, protecting us from external aggression; it is a transmitter of sensation, allowing us to experience subtle changes in touch; it is an excretion channel, helping us to eliminate waste from the body; it is part of the immune system, resisting the invasion of pathogens. However, the skin is also extremely vulnerable to physical factors such as high temperature, strong ultraviolet radiation, high altitude climate, and chemical factors such as steroid hormones, preservatives, surfactants, etc., all of which may cause skin inflammation.

[0003] A healthy skin barrier has excellent tolerance to physical and chemical stimuli, and has good self-repair and regulation capabilities. In contrast, sensitive skin reacts more violently to minor external stimuli, and may experience itching, tingling, pins and needles, burning, tightness, dry skin, erythema, fine scales, and easy flushing. The skin is not only a physical barrier for the human body, but also an active neuro-endocrine-immune organ that involves the interaction of the nervous, endocrine, and immune systems. The causes and mechanisms of sensitive skin include damage to the skin barrier, abnormalities in the nervous sensory system, increased vascular reactivity, and immune inflammatory responses. Existing technologies lack comprehensive care for sensitive skin from the aspects of nervous system recovery, reduced vascular permeability, skin barrier repair, and inflammation control.

[0004] Therefore, there is an urgent need for a cell active peptide composition with anti-allergic and redness-removing effects, as well as a preparation method and medical and aesthetic applications thereof. Summary of the invention

[0005] The purpose of the present invention is to provide a cell active peptide composition with anti-allergic and redness-removing effects, a preparation method thereof, and medical and aesthetic applications.

[0006] In order to achieve the above object, the present invention provides the following technical solutions:

[0007] A cell active peptide composition with anti-allergic and redness-removing effects, comprising the following components in parts by weight: 1-2 parts of tripeptide-1, 0.1-0.8 parts of ceramide, 2-3 parts of hydrolyzed silk, 1.3-2.6 parts of mussel extract, 0.0001-0.2 parts of sodium hyaluronate, 0.0001-1 parts of 4-tert-butyl cyclohexanol, 0.0001-0.2 parts of dipeptide-1, 0.0001-0.2 parts of palmitoyl tripeptide-8, 0.0001-0.2 parts of palmitoyl tetrapeptide-7, 0.0001-0.15 parts of sh-pentapeptide-1, 0.0001-0.15 parts of dipeptide-2, 0.0001-0.2 parts of bisabolol, and 0.0001-0.15 parts of acetyl tetrapeptide-3;

[0008] The preparation method of the mussel extract is:

[0009] (1) taking fresh mussel meat from green-lipped mussels, crushing the mussel meat, and adding water 5 to 6 times the weight of the mussel meat to obtain a mixture;

[0010] (2) adding a composite enzyme to the mixture for enzymolysis at 30-35° C. for 1-2 days, inactivating the enzyme, and obtaining an enzymolysis product;

[0011] (3) adding composite bacteria to the enzymatic hydrolyzate for fermentation at 38-40° C. for 3-5 days, sterilizing, and obtaining a fermentation product;

[0012] (4) The fermentation product is first filtered using a 0.45 μm filter membrane to obtain a filtrate, and the filtrate is further ultrafiltered using a 10 kDa ultrafiltration membrane to obtain an ultrafiltrate, which is spray-dried to obtain a mussel extract.

[0013] Furthermore, the complex enzyme comprises pectinase, bromelain and chitosanase.

[0014] Furthermore, the enzymatic activity of pectinase in the mixture is 70U / mL-90U / mL; the enzymatic activity of bromelain in the mixture is 150U / mL-170U / mL; and the enzymatic activity of chitosanase in the mixture is 110U / mL-130U / mL.

[0015] Furthermore, the composite bacteria include Bifidobacterium longum, Bifidobacterium lactis and Lactobacillus rhamnosus.

[0016] Furthermore, the number of viable Bifidobacterium longum in the enzymatic hydrolysate was 3.0×10 9 CFU / mL-5.0×10 9 CFU / mL, number of live Bifidobacterium lactis 6.0×10 8 CFU / mL-8.0×10 8 CFU / mL, the number of live Lactobacillus rhamnosus cells is 0.5×10 9CFU / mL-1.5×10 9 CFU / mL.

[0017] Studies have shown that mussel extracts have potential anti-allergic effects, but mussel extracts on the market are usually extracted using organic reagents, which have the problems of low extraction efficiency and destruction of heat-sensitive components. When added to the system of the present invention, the anti-allergic effect is not ideal. In the present invention, mussel meat is first enzymatically hydrolyzed using a composite enzyme, and then fermented using a composite bacteria, and the obtained mussel extract has a better anti-allergic effect. The present invention first uses a composite enzyme to enzymatically hydrolyze mussel meat, which can effectively decompose proteins and other macromolecules in mussel meat, making it easier to absorb and possibly reducing the macromolecular structure that causes allergic reactions. Subsequently, composite bacteria are used for fermentation, and the fermentation process can not only further degrade proteins, but also produce some beneficial metabolites, such as short-chain fatty acids, etc. These metabolites may help to enhance the skin barrier function and reduce allergic reactions. The present invention improves the bioavailability of the extract, while changing the components that may cause allergic reactions, thereby reducing the risk of allergies, which is of great significance to consumers who want to obtain skin care benefits from marine organisms but are worried about allergic reactions. However, the improvement of the red-fading effect of the system by the mussel extract prepared by the present invention and the other components is not as good as adding commercially available mussel extracts.

[0018] Furthermore, the preparation method of hydrolyzed silk is:

[0019] S1, washing and boiling silkworm cocoon shells to degumming to obtain silk fibroin;

[0020] S2, the silk fibroin is divided into three groups, namely, silk fibroin group A, silk fibroin group B and silk fibroin group C; 7-10 parts by weight of water and 10 parts by weight of bacterial activity in the system are added to 1 part by weight of silk fibroin group A. 9 CFU / mL-10 10 CFU / mL of breve Bifidobacterium, ferment at 40-45°C for 40-50h, sterilize, and obtain a fermentation liquid of silk fibroin group A; add 7-10 parts by weight of water and 10 parts by weight of bacteria active in the system to 1 part by weight of silk fibroin group B; 9 CFU / mL-10 10 CFU / mL of Lactobacillus casei, fermented at 40-45°C for 60-70h, sterilized, to obtain a fermentation liquid of silk fibroin group B; 7-10 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group C; 9 CFU / mL-10 10 CFU / mL of Lactobacillus brevis, ferment at 40-45°C for 20-30h, sterilize, and obtain the silk fibroin group C fermentation liquid;

[0021] S3, decolorizing the silk fibroin group A fermentation liquid, the silk fibroin group B fermentation liquid and the silk fibroin group C fermentation liquid respectively through activated carbon, and filtering through a 0.22 μm micro-membrane to obtain a silk fibroin group A decolorizing liquid, a silk fibroin group B decolorizing liquid and a silk fibroin group C decolorizing liquid respectively;

[0022] S4, respectively concentrating and drying the silk fibroin group A decolorizing solution, the silk fibroin group B decolorizing solution and the silk fibroin group C decolorizing solution at low temperature, and then sterilizing them with ultraviolet light to obtain silk fibroin group A powder, silk fibroin group B powder and silk fibroin group C powder;

[0023] S5. The silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder are fully and uniformly mixed in a specific weight ratio to obtain hydrolyzed silk.

[0024] Furthermore, in step S5, the weight ratio of the silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder is 1:(1.2-1.4):(0.5-0.8).

[0025] In order to improve the redness-removing effect of the product of the present invention, the present invention attempts to add hydrolyzed silk to assist mussel extract to jointly improve the redness-removing effect, but the effect is not ideal. The present invention can obtain hydrolyzed silk compositions of different compositions by fermenting silk fibroin raw materials using different bacteria, and obtain hydrolyzed silk by compounding, and adding it to the system of the present invention to synergize with the remaining components to improve the redness-removing effect of the product. The hydrolyzed silk prepared by the present invention contains more effective ingredients that help skin recovery and soothing, and produces a synergistic effect with the remaining components such as mussel extract, which can more effectively relieve skin redness and swelling and reduce inflammatory reactions.

[0026] Furthermore, the weight ratio of mussel extract, hydrolyzed silk and tripeptide-1 is (1.2-1.5):(2.4-2.8):(1.9-2.2).

[0027] It was found in the experiment that the addition amount of mussel extract and hydrolyzed silk would affect the storage stability of the product. Improper storage of the product would easily cause an unpleasant odor or darken the color. Through a large number of experiments, it was found that when mussel extract, hydrolyzed silk and tripeptide-1 were compounded in a specific ratio, the stability of the product could be improved. The adhesiveness and antioxidant properties of the mussel extract of the present invention are combined with the moisture retention and film-forming properties of the hydrolyzed silk to form a more stable system. Tripeptide-1 is usually relatively stable and not easy to decompose. It can synergize with other ingredients to improve the stability of the overall formula.

[0028] Tripeptide-1: Helps repair damaged skin barrier by promoting the synthesis of extracellular matrix and enhancing the skin's regenerative capacity.

[0029] Ceramide: Ceramide is an important component of the skin barrier, and supplementing it can help repair and strengthen the skin barrier.

[0030] Sodium hyaluronate: It has strong hydrating capacity. Topical HA can regulate keratinocyte differentiation, inhibit inflammation levels, and enhance the production of endogenous HA, thereby repairing the skin barrier.

[0031] 4-tert-Butylcyclohexanol: 4-tert-Butylcyclohexanol provides immediate relief from skin pain and burning sensations by inhibiting TRPV-1. Studies have shown that 4-tert-Butylcyclohexanol significantly reduces TRPV-1 activation in vitro and has significant immediate anti-stinging / anti-burning effects in vivo.

[0032] Dipeptide-1: has analgesic, neuroprotective and neuromodulatory properties. It is synthesized at nerve endings and works by stimulating nerve cells to release methionine enkephalin, an opioid (i.e., relaxing, analgesic) messenger molecule with neuro- and immunomodulatory functions.

[0033] Palmitoyl Tripeptide-8: Derived from pro-opiomelanocortin (POMC), it can calm and soothe irritated skin and restore the skin to its normal sensitivity threshold.

[0034] Palmitoyl Tetrapeptide-7: Reduces IL-6 secretion, reduces inflammation after UVB exposure, and stimulates the production of laminins IV and V and collagen VII.

[0035] sh-pentapeptide-1: also known as thymopentin (TP5), with an amino acid sequence of RKDVY, is a fragment of amino acids 32-36 located in thymopoietin II (TPⅡ). It has similar biological activity to TPⅡ, can bidirectionally regulate the imbalanced immune system, and is an effective immunomodulator.

[0036] Dipeptide-2: An effective ACE inhibitor that promotes blood circulation by reducing vascular constriction.

[0037] Acetyl Tetrapeptide-3: Promotes endothelial formation and increases capillary elasticity.

[0038] Bisabolol: Bisabolol is a natural monoterpene alcohol extracted from German chamomile. It is widely used in cosmetics and medicines, especially for relieving sensitive skin, reducing skin inflammation and promoting skin health.

[0039] Furthermore, the cell active peptide composition comprises the following components in parts by weight: 1-2 parts of tripeptide-1, 0.1-0.8 parts of ceramide, 2-3 parts of hydrolyzed silk, 1.3-2.6 parts of mussel extract, 0.0001-0.2 parts of sodium hyaluronate, 0.0001-1 parts of 4-tert-butyl cyclohexanol, 0.0001-0.2 parts of dipeptide-1, 0.0001-0.2 parts of palmitoyl tripeptide-8, 0.0001-0.2 parts of palmitoyl tetrapeptide-7, 0.0001-0.15 parts of sh-pentapeptide-1, 0.0001-0.15 parts of dipeptide-2, 0.0001-0.2 parts of bisabolol, and 0.0001-0.15 parts of acetyl tetrapeptide-3.

[0040] The present invention also provides a method for preparing the cell active peptide composition, which comprises the following steps: weighing corresponding components according to weight ratio, mixing evenly, and sterilizing to obtain the cell active peptide composition.

[0041] The invention also provides application of the cell active peptide composition in skin products.

[0042] The present invention also provides application of the cell active peptide composition in medical cosmetology.

[0043] The invention also provides application of the cell active peptide composition in preparing cosmetics.

[0044] The present invention also provides application of the cell active peptide composition in preparing external skin medicine.

[0045] The present invention also provides application of the cell active peptide composition in preparing cosmetic products.

[0046] Compared with the prior art, the advantages and beneficial effects of the present invention are:

[0047] 1. Mussel extracts on the market are usually extracted using organic reagents, which have the problems of low extraction efficiency and destruction of heat-sensitive components. When added to the system of the present invention, the anti-allergic effect is not ideal. The present invention first enzymolyzes mussel meat with a composite enzyme and then ferments it with a composite bacteria, and the obtained mussel extract has a better anti-allergic effect.

[0048] 2. The present invention can obtain hydrolyzed silk compositions of different compositions by fermenting silk fibroin raw materials with different bacteria. The hydrolyzed silk is obtained by compounding and added to the system of the present invention to synergize with other components to improve the red-fading effect of the product.

[0049] 3. The present invention compounds mussel extract, hydrolyzed silk and tripeptide-1 in a specific ratio to improve the stability of the product. DETAILED DESCRIPTION

[0050] The technical solutions in the embodiments of the present invention are described clearly and completely below. Obviously, the described embodiments are only part of the embodiments of the present invention, not all of them. Based on the embodiments of the present invention, all other embodiments obtained by ordinary technicians in this field without creative work are within the scope of protection of the present invention.

[0051] The enzymes and bacteria used in the present invention are commercially available products, as follows.

[0052] Bifidobacterium longum, accession number: SHBCCD24310, was purchased from Shanghai Microbiological Collection Center.

[0053] Bifidobacterium lactis, accession number: SHBCCD24728, was purchased from Shanghai Microbiological Collection Center.

[0054] Lactobacillus rhamnosus, accession number: SHBCCD73158, was purchased from Shanghai Microbiological Collection Center.

[0055] Bifidobacterium breve, accession number: SHBCCD24424JCM7017, was purchased from Shanghai Microbiological Collection Center.

[0056] Lactobacillus casei, accession number: SHBCCD24737, was purchased from Shanghai Microbiological Collection Center.

[0057] Lactobacillus brevis, accession number: SHBCCD14346, was purchased from Shanghai Microbiological Collection Center.

[0058] The enzymes used in the present invention were purchased from Shanghai Yuanye Biotechnology Co., Ltd.

[0059] Example 1

[0060] This embodiment provides a cell active peptide composition, comprising the following components in parts by weight: 1.3 parts of tripeptide-1, 0.5 parts of ceramide, 2.6 parts of hydrolyzed silk, 2.0 parts of mussel extract, 0.003 parts of sodium hyaluronate, 0.1 parts of 4-tert-butyl cyclohexanol, 0.0009 parts of dipeptide-1, 0.05 parts of palmitoyl tripeptide-8, 0.008 parts of palmitoyl tetrapeptide-7, 0.12 parts of sh-pentapeptide-1, 0.09 parts of dipeptide-2, 0.02 parts of bisabolol, and 0.03 parts of acetyl tetrapeptide-3.

[0061] The preparation method of the mussel extract is:

[0062] (1) taking fresh mussel meat from green-lipped mussels, crushing the mussel meat, and adding water 6 times the weight of the mussel meat to obtain a mixture;

[0063] (2) adding a composite enzyme to the mixture for enzymolysis at 32° C. for 2 days, inactivating the enzyme, and obtaining an enzymolysis product;

[0064] (3) adding composite bacteria to the enzymatic hydrolysate for fermentation at 39° C. for 4 days, sterilizing, and obtaining a fermentation product;

[0065] (4) The fermentation product is first filtered using a 0.45 μm filter membrane to obtain a filtrate, and the filtrate is then ultrafiltered using an ultrafiltration membrane with a molecular weight cutoff of 10 kDa to obtain an ultrafiltrate, which is spray-dried to obtain a mussel extract.

[0066] The complex enzyme comprises pectinase, bromelain and chitosanase.

[0067] The enzymatic activity of pectinase in the mixture was 80 U / mL; the enzymatic activity of bromelain in the mixture was 160 U / mL; and the enzymatic activity of chitosanase in the mixture was 120 U / mL.

[0068] The composite bacteria include Bifidobacterium longum, Bifidobacterium lactis and Lactobacillus rhamnosus.

[0069] The number of live Bifidobacterium longum added to the enzymatic hydrolysate was 4.0×10 9 CFU / mL, number of live Bifidobacterium lactis 7.0×10 8 CFU / mL, the number of live Lactobacillus rhamnosus cells is 1×10 9 CFU / mL.

[0070] The preparation method of hydrolyzed silk is:

[0071] S1, washing and boiling silkworm cocoon shells to degumming to obtain silk fibroin;

[0072] S2, the silk fibroin was divided into three groups, namely, silk fibroin group A, silk fibroin group B and silk fibroin group C; 8 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group A. 10 CFU / mL of Bifidobacterium breve was fermented at 42°C for 45h and sterilized to obtain a fermentation liquid of silk fibroin group A; 9 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group B. 9 CFU / mL of Lactobacillus casei, fermented at 42°C for 65h, sterilized, and obtained the fermentation liquid of silk fibroin group B; 8 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group C; 10 CFU / mL of Lactobacillus brevis, fermented at 42°C for 26h, sterilized, and obtained the silk fibroin group C fermentation liquid;

[0073] S3, decolorizing the silk fibroin group A fermentation liquid, the silk fibroin group B fermentation liquid and the silk fibroin group C fermentation liquid respectively through activated carbon, and filtering through a 0.22 μm micro-membrane to obtain a silk fibroin group A decolorizing liquid, a silk fibroin group B decolorizing liquid and a silk fibroin group C decolorizing liquid respectively;

[0074] S4, respectively concentrating and drying the silk fibroin group A decolorizing solution, the silk fibroin group B decolorizing solution and the silk fibroin group C decolorizing solution at low temperature, and then sterilizing them with ultraviolet light to obtain silk fibroin group A powder, silk fibroin group B powder and silk fibroin group C powder;

[0075] S5. Thoroughly mix the silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder in a weight ratio of 1:1.3:0.6 to obtain hydrolyzed silk.

[0076] The preparation method of the cell active peptide composition with anti-allergic and redness-removing effects of this embodiment comprises the following steps: weighing corresponding components according to weight ratio, mixing evenly, and sterilizing to obtain the cell active peptide composition.

[0077] Example 2

[0078] This embodiment provides a cell active peptide composition, comprising the following components by weight: 1.2 parts of tripeptide-1, 0.5 parts of ceramide, 2.8 parts of hydrolyzed silk, 1.9 parts of mussel extract, 0.01 parts of sodium hyaluronate, 0.0001 parts of 4-tert-butyl cyclohexanol, 0.2 parts of dipeptide-1, 0.0001 parts of palmitoyl tripeptide-8, 0.05 parts of palmitoyl tetrapeptide-7, 0.007 parts of sh-pentapeptide-1, 0.09 parts of dipeptide-2, 0.2 parts of bisabolol, and 0.12 parts of acetyl tetrapeptide-3.

[0079] The preparation method of the mussel extract is:

[0080] (1) taking fresh mussel meat from green-lipped mussels, crushing the mussel meat, and adding water 5 times the weight of the mussel meat to obtain a mixture;

[0081] (2) adding a composite enzyme to the mixture for enzymolysis at 30° C. for 1 day, inactivating the enzyme, and obtaining an enzymolysis product;

[0082] (3) adding composite bacteria to the enzymatic hydrolysate for fermentation at 38° C. for 3 days, sterilizing, and obtaining a fermentation product;

[0083] (4) The fermentation product is first filtered using a 0.45 μm filter membrane to obtain a filtrate, and the filtrate is further ultrafiltered using a 10 kDa ultrafiltration membrane to obtain an ultrafiltrate, which is spray-dried to obtain a mussel extract.

[0084] The complex enzyme comprises pectinase, bromelain and chitosanase.

[0085] The enzymatic activity of pectinase in the mixture was 70 U / mL; the enzymatic activity of bromelain in the mixture was 170 U / mL; and the enzymatic activity of chitosanase in the mixture was 110 U / mL.

[0086] The composite bacteria include Bifidobacterium longum, Bifidobacterium lactis and Lactobacillus rhamnosus.

[0087] The number of live Bifidobacterium longum in the enzymatic hydrolysate was 5.0×10 9 CFU / mL, number of live Bifidobacterium lactis 6.0×10 8 CFU / mL, number of live Lactobacillus rhamnosus bacteria 1.5×10 9 CFU / mL.

[0088] The preparation method of hydrolyzed silk is:

[0089] S1, washing and boiling silkworm cocoon shells to degumming to obtain silk fibroin;

[0090] S2, the silk fibroin was divided into three groups, namely, silk fibroin group A, silk fibroin group B and silk fibroin group C; 10 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group A. 9 CFU / mL of Bifidobacterium breve was fermented at 40°C for 50h and sterilized to obtain a fermentation liquid of silk fibroin group A; 10 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group B. 9 CFU / mL of Lactobacillus casei, fermented at 40°C for 60h, sterilized, and obtained the fermentation liquid of silk fibroin group B; 7 parts by weight of water and 10 parts by weight of bacterial activity in the system were added to 1 part by weight of silk fibroin group C; 9 CFU / mL of Lactobacillus brevis, fermented at 40°C for 30h, sterilized, and obtained the silk fibroin group C fermentation liquid;

[0091] S3, decolorizing the silk fibroin group A fermentation liquid, the silk fibroin group B fermentation liquid and the silk fibroin group C fermentation liquid respectively through activated carbon, and filtering through a 0.22 μm micro-membrane to obtain a silk fibroin group A decolorizing liquid, a silk fibroin group B decolorizing liquid and a silk fibroin group C decolorizing liquid respectively;

[0092] S4, respectively concentrating and drying the silk fibroin group A decolorizing solution, the silk fibroin group B decolorizing solution and the silk fibroin group C decolorizing solution at low temperature, and then sterilizing them with ultraviolet light to obtain silk fibroin group A powder, silk fibroin group B powder and silk fibroin group C powder;

[0093] S5. Thoroughly mix the silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder in a weight ratio of 1:1.2:0.5 to obtain hydrolyzed silk.

[0094] The preparation method of the cell active peptide composition with anti-allergic and redness-removing effects of this embodiment comprises the following steps: weighing corresponding components according to weight ratio, mixing evenly, and sterilizing to obtain the cell active peptide composition.

[0095] Comparative Example 1

[0096] The difference between this comparative example and Example 1 is: a cell active peptide composition, comprising the following components in parts by weight: 0.5 parts of tripeptide-1, 0.5 parts of ceramide, 1.6 parts of hydrolyzed silk, 2.8 parts of mussel extract, 0.003 parts of sodium hyaluronate, 0.1 parts of 4-tert-butyl cyclohexanol, 0.5009 parts of dipeptide-1, 0.05 parts of palmitoyl tripeptide-8, 0.008 parts of palmitoyl tetrapeptide-7, 0.12 parts of sh-pentapeptide-1, 0.09 parts of dipeptide-2, 0.52 parts of bisabolol, and 0.03 parts of acetyl tetrapeptide-3.

[0097] Comparative Example 2

[0098] The difference between this comparative example and Example 1 is that the mussel extract is a commercially available product purchased from Xi'an Ruierli Bioengineering Co., Ltd.

[0099] Comparative Example 3

[0100] The difference between this comparative example and Example 1 is that the complex enzyme includes neutral protease, ficin and pectinase.

[0101] The enzyme activity of neutral protease in the mixture is 80 U / mL; the enzyme activity of fig protease in the mixture is 160 U / mL; and the enzyme activity of pectinase in the mixture is 120 U / mL.

[0102] Comparative Example 4

[0103] The difference between this comparative example and Example 1 is that the composite bacteria include Bifidobacterium breve, Lactobacillus casei and Lactobacillus breve.

[0104] The number of live Bifidobacterium breve in the enzymatic hydrolysate was 4.0×10 9 CFU / mL, number of live Lactobacillus casei 7.0×10 8 CFU / mL, number of live Lactobacillus brevis 1×10 9 CFU / mL.

[0105] Comparative Example 5

[0106] The difference between this comparative example and Example 1 is that the hydrolyzed silk is a commercially available product purchased from Hubei Jianchu Biomedicine Co., Ltd.

[0107] Comparative Example 6

[0108] The difference between this comparative example and Example 1 is that Bifidobacterium breve is replaced by Bifidobacterium longum; Lactobacillus casei is replaced by Bifidobacterium lactis; and Lactobacillus breve is replaced by Lactobacillus rhamnosus.

[0109] Comparative Example 7

[0110] The difference between this comparative example and Example 1 is that the silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder in a weight ratio of 1:1:1 are fully and evenly mixed in a specific weight ratio to obtain hydrolyzed silk.

[0111] Comparative Example 8

[0112] The difference between this comparative example and Example 1 is: a cell active peptide composition, comprising the following components in parts by weight: 2 parts of tripeptide-1, 0.5 parts of ceramide, 2.2 parts of hydrolyzed silk, 1.7 parts of mussel extract, 0.003 parts of sodium hyaluronate, 0.1 parts of 4-tert-butyl cyclohexanol, 0.0009 parts of dipeptide-1, 0.05 parts of palmitoyl tripeptide-8, 0.008 parts of palmitoyl tetrapeptide-7, 0.12 parts of sh-pentapeptide-1, 0.09 parts of dipeptide-2, 0.02 parts of bisabolol, and 0.03 parts of acetyl tetrapeptide-3.

[0113] Performance Testing

[0114] 1. Anti-allergic test: Hyaluronidase activity test: Hyaluronic acid is widely present in the skin and other tissues. The relationship between hyaluronic acid and skin is very close. Macromolecular hyaluronic acid can inhibit inflammatory response, thereby alleviating the discomfort caused by skin inflammation. Macromolecular hyaluronic acid will be degraded under the action of hyaluronidase, resulting in a decrease in the content of macromolecular hyaluronic acid and decomposition to produce the degradation product N-acetylglucosamine. Determining N-acetylglucosamine in the reaction system can indirectly reflect the activity of hyaluronidase. The anti-allergic activity of the sample is evaluated by in vitro inhibition of hyaluronidase activity experiment. Inhibition of hyaluronidase activity can reduce the degradation of hyaluronic acid and reduce skin sensitivity.

[0115] Detection method: The cell active peptide compositions of Examples 1-2 and Comparative Examples 1-8 were mixed with hyaluronidase solution, respectively, the concentration of the cell active peptide composition in the solution was 7wt%, and the mixture was shaken and incubated at 37°C for 10min. A hyaluronate solution was added and incubated at 37°C for 45min. A BSA solution was added and incubated for another 10min, the OD600nm value was detected, and the hyaluronidase inhibition rate was calculated. See Table 1.

[0116] Table 1: Hyaluronidase inhibition rate

[0117] Inhibition rate % Example 1 100 Example 2 99 Comparative Example 1 83 Comparative Example 2 85 Comparative Example 3 89 Comparative Example 4 90 Comparative Example 5 87 Comparative Example 6 88 Comparative Example 7 91 Comparative Example 8 96

[0118] 2. Redness fading effect test

[0119] 5-lipoxygenase is an enzyme involved in the synthesis of inflammatory mediators. It can initiate the process of converting arachidonic acid into leukotrienes, a class of substances associated with inflammatory responses. During skin inflammation, increased activity of 5-lipoxygenase can lead to inflammatory symptoms such as skin redness and swelling.

[0120] Sample group: The cell active peptide compositions of Examples 1-2 and Comparative Examples 1-8 were respectively accurately prepared into 1 mg / mL solutions using 100 mmol / L pH 6.9 phosphate buffer (PBS) for use.

[0121] Preparation of substrate solution: Prepare PBS buffer with a concentration of 200mmol / L pH9.0, accurately pipette 50μL of polysorbate-20 and disperse it in the PBS buffer solution, add 50μL of linoleic acid while shaking, mix well, add 1mol / L sodium hydroxide, and shake while adding until the whole system is clear, adjust the pH to 9.0, and add PBS to make up to 100mL;

[0122] 5-lipoxygenase inhibitory activity assay: PBS was used to prepare 0.2U / mL 5-lipoxygenase solution. Accurately pipette 50μL sample solution into a 96-well plate, add 100μL substrate solution, gently shake to mix, incubate at room temperature for 5min, quickly add 100μL enzyme solution, measure the absorbance A value (referring to the absorbance of the microplate reader at different wavelengths) at 234nm on a microplate reader at 0 and 5min of reaction, set the sample group (the concentration of each sample component is 0.2mg / mL) and the blank group (PBS instead of the sample), record the difference between the two A values, perform the operation three times in parallel, and calculate the inhibition rate according to the following formula: Inhibition rate = (△A0-△A) / △A0, where △A0 is the difference in A of the blank group, and △A is the difference in A of the sample group. The specific test results are shown in Table 2 below.

[0123] Table 2: 5-lipoxygenase inhibition rate comparison table

[0124]

[0125]

[0126] 3. Storage stability

[0127] The cell active peptide compositions prepared in Examples 1-2 and Comparative Examples 1-8 were sealed and stored, and placed in the following four environments for observation to test the storage stability.

[0128] Normal temperature: The sample is placed at 25°C, 60% RH (relative humidity) for 180 days.

[0129] Cold resistance: -10℃ for 30 days.

[0130] Hot and cold cycle: -10℃, 25%RH; 25℃, 60%RH; 38℃, 75%RH, 24h at each temperature, 30 cycles in total.

[0131] High temperature acceleration: The test conditions are 50℃±1℃, 25%RH±5%RH for 90 days.

[0132] No obvious change was recorded as pass, and odor and / or color change was recorded as fail.

[0133] The results are shown in Table 3.

[0134] Table 3: Stability test results

[0135]

[0136]

[0137] From the above performance test results, it can be seen that the cell active peptide compositions of Examples 1-2 have good anti-allergic and redness-removing effects, especially Example 1 has the most outstanding comprehensive performance, which is mainly due to the synergistic combination of multiple components.

[0138] However, the comparative examples were significantly inferior to the embodiments in the corresponding performance tests because they did not adopt the necessary technical solutions. In comparative example 1, the ratio of the components was changed, and it can be seen that the comprehensive effect decreased. In comparative example 2, commercially available mussel extract was used, and comparative examples 3-4 did not use the solution for preparing mussel extract. From the results, it can be seen that the anti-allergic effect was affected. Comparative example 5 used commercially available hydrolyzed silk, and comparative examples 6-7 did not use the solution for preparing hydrolyzed silk, and the red-fading effect of the product decreased. In comparative example 8, the ratio of mussel extract, hydrolyzed silk and tripeptide-1 was changed, and the storage stability of the product decreased. The above experimental results further prove the importance of the technical solution defined in the present invention for its technical effect.

[0139] The above is a preferred embodiment of the present invention. It should be pointed out that for ordinary technicians in this technical field, several improvements and modifications can be made without departing from the principles of the present invention. These improvements and modifications should also be regarded as the scope of protection of the present invention.

Claims

1. A cell active peptide composition with anti-allergic and redness-removing effects, characterized in that: The invention comprises the following components in parts by weight: 0.0001-2 parts of tripeptide-1, 0.0001-0.8 parts of ceramide, 0.0001-3 parts of hydrolyzed silk, 0.0001-2.6 parts of mussel extract, 0.0001-0.2 parts of sodium hyaluronate, 0.0001-1 parts of 4-tert-butyl cyclohexanol, 0.0001-0.2 parts of dipeptide-1, 0.0001-0.2 parts of palmitoyl tripeptide-8, 0.0001-0.2 parts of palmitoyl tetrapeptide-7, 0.0001-0.15 parts of sh-pentapeptide-1, 0.0001-0.15 parts of dipeptide-2, 0.0001-0.2 parts of bisabolol, and 0.0001-0.15 parts of acetyl tetrapeptide-3; The preparation method of the mussel extract is: (1) taking fresh mussel meat from green-lipped mussels, crushing the mussel meat, and adding water 5 to 6 times the weight of the mussel meat to obtain a mixture; (2) adding a composite enzyme to the mixture for enzymolysis at 30-35° C. for 1-2 days, inactivating the enzyme, and obtaining an enzymolysis product; (3) adding composite bacteria to the enzymatic hydrolyzate for fermentation at 38-40° C. for 3-5 days, sterilizing, and obtaining a fermentation product; (4) The fermentation product is first filtered using a 0.45 μm filter membrane to obtain a filtrate, and the filtrate is further ultrafiltered using a 10 kDa ultrafiltration membrane to obtain an ultrafiltrate, which is then spray-dried to obtain a mussel extract.

2. The cell active peptide composition according to claim 1, characterized in that: The complex enzyme comprises pectinase, bromelain and chitosanase.

3. The cell active peptide composition according to claim 1, characterized in that: The enzymatic activity of pectinase in the mixture is 70U / mL-90U / mL; the enzymatic activity of bromelain in the mixture is 150U / mL-170U / mL; and the enzymatic activity of chitosanase in the mixture is 110U / mL-130U / mL.

4. The cell active peptide composition according to claim 1, characterized in that: The composite bacteria include Bifidobacterium longum, Bifidobacterium lactis and Lactobacillus rhamnosus.

5. The cell active peptide composition according to claim 4, characterized in that: The number of live Bifidobacterium longum in the enzymatic hydrolysate was 3.0×10 9 CFU / mL-5.0×10 9 CFU / mL, number of live Bifidobacterium lactis 6.0×10 8 CFU / mL-8.0×10 8 CFU / mL, the number of live Lactobacillus rhamnosus cells is 0.5×10 9 CFU / mL-1.5×10 9 CFU / mL.

6. The cell active peptide composition according to claim 1, characterized in that: The preparation method of hydrolyzed silk is: S1, washing and boiling silkworm cocoon shells to degumming to obtain silk fibroin; S2, the silk fibroin is divided into three groups, namely, silk fibroin group A, silk fibroin group B and silk fibroin group C; 7-10 parts by weight of water and 10 parts by weight of bacterial activity in the system are added to 1 part by weight of silk fibroin group A. 9 CFU / mL-10 10 CFU / mL of breve Bifidobacterium, ferment at 40-45°C for 40-50h, sterilize, and obtain a fermentation liquid of silk fibroin group A; add 7-10 parts by weight of water and 10 parts by weight of bacteria active in the system to 1 part by weight of silk fibroin group B; 9 CFU / mL-10 10 CFU / mL of Lactobacillus casei, fermented at 40-45°C for 60-70h, sterilized, and obtained a silk fibroin group B fermentation liquid; 1 part by weight of silk protein C group is added with 7-10 parts by weight of water and 10 parts by weight of bacteria in the system. 9 CFU / mL-10 10 CFU / mL of Lactobacillus brevis, ferment at 40-45°C for 20-30h, sterilize, and obtain the silk fibroin group C fermentation liquid; S3, decolorizing the silk fibroin group A fermentation liquid, the silk fibroin group B fermentation liquid and the silk fibroin group C fermentation liquid respectively through activated carbon, and filtering through a 0.22 μm micro-membrane to obtain a silk fibroin group A decolorizing liquid, a silk fibroin group B decolorizing liquid and a silk fibroin group C decolorizing liquid respectively; S4, respectively concentrating and drying the silk fibroin group A decolorizing solution, the silk fibroin group B decolorizing solution and the silk fibroin group C decolorizing solution at low temperature, and then sterilizing them with ultraviolet light to obtain silk fibroin group A powder, silk fibroin group B powder and silk fibroin group C powder; S5. The silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder are fully and uniformly mixed in a specific weight ratio to obtain hydrolyzed silk.

7. The cell active peptide composition according to claim 6, characterized in that: In the step S5, the weight ratio of the silk fibroin group A powder, the silk fibroin group B powder and the silk fibroin group C powder is 1:(1.2-1.4):(0.5-0.8).

8. The cell active peptide composition according to claim 6, characterized in that: The weight ratio of mussel extract, hydrolyzed silk and tripeptide-1 is (1.2-1.5):(2.4-2.8):(1.9-2.2).

9. A method for preparing the cell active peptide composition according to any one of claims 1 to 8, characterized in that: The corresponding components are weighed according to the weight ratio, mixed evenly, and sterilized to obtain the cell active peptide composition.

10. Use of the cell active peptide composition according to any one of claims 1 to 8 in the preparation of skin products.

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