CN109608520A - A kind of Functional Polypeptides and application thereof in pearl source - Google Patents

A kind of Functional Polypeptides and application thereof in pearl source Download PDF

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Publication number
CN109608520A
CN109608520A CN201811361112.4A CN201811361112A CN109608520A CN 109608520 A CN109608520 A CN 109608520A CN 201811361112 A CN201811361112 A CN 201811361112A CN 109608520 A CN109608520 A CN 109608520A
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functional polypeptides
pearl
pph
leucine
application
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CN109608520B (en
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尹浩
龙丽娟
李姣
李茹
尹团
杨勇
张偲
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South China Sea Institute of Oceanology of CAS
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South China Sea Institute of Oceanology of CAS
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
    • 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
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P39/00—General protective or antinoxious agents
    • A61P39/06—Free radical scavengers or antioxidants
    • 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
    • A61Q19/02—Preparations for care of the skin for chemically bleaching or whitening the skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Abstract

The invention discloses a kind of Functional Polypeptides and application thereof in pearl source.The amino acid sequence of the Functional Polypeptides is methionine-Ile-Ile-Leu-Leu-cysteine-serine-leucine-leucine (MIILLCSLL).Functional Polypeptides of the invention have the function of the biological interior free yl of good removing, anti-oxidation function, melanocyte pigment synthesis inhibitory activity, therefore Functional Polypeptides of the invention can be used for preparing free radical scavenger, antioxidant and the cosmetic material with whitening function.

Description

A kind of Functional Polypeptides and application thereof in pearl source
Technical field
The invention belongs to marine organisms Functional Polypeptides fields, and in particular to a kind of the new function peptide and its use in pearl source On the way.
Background technique
Pearl is beauty face-whitening-nourishing good merchantable brand from ancient times, and Compendium of Material Medica, which is recorded, claims " pearl coating surface makes us moist good color ".Existing For cosmetic industry, pearl, pearl shell and their zymolyte, it has also become the important component of whitening and freckle-removing product product, by Country's food officina's cosmetic material directory.
Functional Polypeptides are converted by pearl protein, are the effective means for improving its effect.Modern biology, pharmacology, medicine The study found that skin color and the content, size, type of melanin in skin and distribution are closely related, and tyrosinase promotes The hydroxylating of tyrosine and to the oxidation of DOPA be cell melanin formed necessary condition.Anti-oxidant, anti-oxidizing activities are Through at one of the main indicator for measuring white-skinned face function, in American-European cosmetics industry-leading, country is widely adopted.Meanwhile also having big Amount evidence shows that the whitening spot-removing function of pearl and its inoxidizability are closely related, and converts pearl protein to special The Functional Polypeptides of amino acid sequence can significantly improve the inoxidizability of pearl.Antioxidation in enzymatic hydrolysis release pearl keratin Functional peptide fragment, have become the important means for improving pearl raw material spot-eliminating beauty treatment effect, principle is, untreated pearl The amino acid sequence of a large amount of anti-oxidation functions, but these protein moleculars bulky complex itself are inlaid in albumen, biology is difficult to directly Absorption is connect, oxidation resistant functional domain is contacted with action target spot to be restricted, and giving full play to for white-skinned face function is constrained.Hydrolysis can be with So that macromolecular is converted into the oligopeptide that biology easily utilizes, exposes anti-oxidation function domain sufficiently, thus pearl protein hydrolysate Anti-oxidant, pigment generates inhibitory activity and is significantly higher than untreated raw material.Japanese scholars first discovery sour water solution pearl protein have compared with Strong anti-oxidant, tyrosine enzyme activity inhibitory activity, and obtain cosmetic use patent.It is improved through various countries, it is dirty with biological enzymes extraction Metachromia is strong, soda acid rambunctious is as catalyst, is prepared for pearl protein hydrolysate various in style.
Margarita cochonlin zymolyte has been widely used, as received in China " having used cosmetic material Names Catalogue " The Margarita extract of record.But be not much at present about the specific type of anti-oxidation peptide, the report of structure in zymolyte, it limits High activity pearl cosmetic material and other active optimizations of Novel pearl Functional Polypeptides, also constrain building for accurate Quality Control technology It is vertical, cause product level to be difficult to be promoted.
Summary of the invention
The first purpose of the invention is to provide one kind to have the biological interior free yl of good removing, anti-oxidant and inhibition The Functional Polypeptides in the pearl source of melanocyte pigment synthesis function.
Functional Polypeptides of the invention, contain 9 amino acid residues, and amino acid sequence is the different bright ammonia of methionine-isoleucine- Acid-Leu-Leu-cysteine-serine-leucine-leucine (MIILLCSLL), is a new construction peptides.
Functional Polypeptides of the invention are to be catalyzed pearl protein using the mixture of bromelain and keratinase as catalyst Hydrolysis, preparation gained, which has, removes biological interior free yl, anti-oxidant and inhibit melanocyte pigment synthesis activity Hydrolysate effective component.Through ultrafiltration, chromatographic process by it after being isolated and purified in hydrolysate, when using Matrix-assisted flight Between mass spectrometry method (MALDI-TOF-MS) analyze, identify its molecular weight be 1018.604Da, amino acid sequence be methionine-it is different Leu-Ile-Leu-Leu-cysteine-serine-leucine-leucine (MIILLCSLL).In NCBI In SWISS-PROT database retrieval, do not find obvious homologous sequence, should be the result shows that this Functional Polypeptides be from pearl The new construction peptide of generation.
A second object of the present invention is to provide above-mentioned Functional Polypeptides to prepare answering in free radical scavenger or antioxidant With.
A kind of free radical scavenger or antioxidant, which is characterized in that including above-mentioned Functional Polypeptides as effective component.
Third object of the present invention is to provide above-mentioned Functional Polypeptides in preparation there is melanocyte pigment synthesis to inhibit to live Application in the inhibitor of property.
A kind of melanocyte pigment synthesis inhibitor, which is characterized in that comprising above-mentioned Functional Polypeptides as effective component.
Fourth object of the present invention is to provide above-mentioned Functional Polypeptides and is preparing the application in cosmetic material, such as has black The cosmetic material of plain cytochromes synthesis inhibitory activity.
A kind of cosmetic material, which is characterized in that including above-mentioned Functional Polypeptides as active material.
The present invention carries out research and development for the problems of the prior art, by anti-oxidant, free radical resisting in pearl zymolyte, The tracking of people's chromatophore melanin production inhibitory activity ingredient separates, and prepares, identifies 1 structure novel, is active good Anti-oxidant peptides can be used for anti-oxidant high quality, free radical resisting and chromatophore Synthetic inhibitor of melanin, also act as simultaneously The quality control index of pearl zymolyte has the optimization of pearl protein enzymolysis process, the development of novel product Quality Control Technology Clear meaning.
Functional Polypeptides of the invention have the biological interior free yl of good removing and inhibit human melanoma cell pigment synthesis Function, therefore Functional Polypeptides of the invention can be used for preparing cosmetic material.
Detailed description of the invention:
Fig. 1 is PPH-I-3ODS HPLC chromatogram；
Fig. 2 is the MALDI-TOF-TOF mass spectrogram of objective function peptide (MIILLCSLL).
Specific embodiment:
The following examples are further illustrations of the invention, rather than limiting the invention.
Embodiment 1: the preparation of pearl enzymolysis protein
1, raw materials and reagents
Pearl powder in embodiment is provided by Guangzhou auspicious good fortune pearl processing Co., Ltd, crosses bag distribution packaging after 200 meshes And seal, it is saved in -20 DEG C.
Bromelain (enzyme activity is 400,000 U/g), is purchased from Nanning Pang Bo bioengineering Co., Ltd；Keratoprotein Enzyme (enzyme activity is 200,000 U/g), is purchased from Jinan Zhuo Dai Biotechnology Co., Ltd；DEAE-52 cellulose cation exchange resin Purchased from Whatman company, Sephadex G-15 gel resin is purchased from GE company.Ethyl alcohol, formaldehyde, isopropanol, sodium hydroxide, phosphorus Other reagents such as sour disodium hydrogen, sodium dihydrogen phosphate are that domestic analysis is pure.Test water is ultrapure water.
2, prepared by pearl protein
Pearl powder about 100g is weighed, water 100mL, ethyl alcohol 50mL is added to stir evenly.It is slowly added to 3M hydrochloric acid, until bubble-free It generates.Reactant is filtered, collects after precipitating is dried on filter paper and obtains pearl crude protein 5.6g, freezing.
3, the preparation of pearl enzymolysis protein
Pearl crude protein 5g is taken, 50ml bromelain/keratinase solution (enzyme bottom ratio is 4000U/g), solution is added Middle bromelain: keratinase=5:1 (w/w).PH to 6.5 is adjusted with 1mol/L HCl, 5h, reaction knot are hydrolyzed at 50 DEG C Be centrifuged 10min under Shu Hou, enzyme deactivation 10min living in boiling water, 6500r/min, remove insoluble impurities, at 15000r/min from Heart 10min takes supernatant, crosses 0.2 μm of filter membrane up to filtrate-pearl enzymolysis protein solution, zymolyte 3.8g, as pearl is lyophilized to obtain Protein hydrolysate.
The separation from pearl enzymolysis protein of embodiment 2 prepares new function peptide
1, Example 1 digests resulting pearl protein hydrolysate 3g, is dissolved in 100mL water and sample solution is made, with retention Molecular weight is the ultrafiltration membrance filter of 3kDa, and retention part and filtrate is lyophilized respectively, obtains two samples: PPH-I (molecular weight > 3kDa), PPH-II (molecular weight < 3kDa).(method detailed is shown in reality to the DPPH free radical scavenging ability of detection PPH-I and II respectively Apply example 3), the EC of PPH-I50The EC of=4.5mg/mL, PPH-II50=40.5mg/mL selects the stronger component of activity accordingly PPH-I continues to separate.
2, PPH-I is separated with G15 gel column, obtains 4 component piece PPH-I-1~4, after being lyophilized respectively, inspection Survey the EC of its DPPH free radical scavenging activity50Value, respectively 7.53mg/ml, 7.33mg/ml, 5.88mg/ml, 10.461mg/ ml。
The G15 gel post separation, condition are as follows: take PPH-I sample 1g to be dissolved in 5mL deionized water and chromatography is made The Sephadex G-15 solvent resistant column (2.6 × 100cm) for using pure water equilibrium in advance is added, with deionized water with 1mL in sample The flow velocity elution column of/min sequentially collects to obtain 4 chromatographic peak segments (PPH-I-1~4) according to UV (280nm) detector signal, It is lyophilized respectively.
3, the strongest segment PPH-I-3 of activity in the sample for taking previous step to prepare separates (chromatography with HPLC (ODS column) Figure is shown in Fig. 1), chromatographic peak flow point at 11.5 minutes is collected, objective function peptide PPH-I-3-11, test target function are obtained after freeze-drying The DPPH scavenging capacity of peptide, EC50Value is 0.82mg/mL, it is shown that good free radical scavenging ability.
The HPLC separation, the chromatograph used is Agilent1200HPLC type high performance liquid chromatography, and chromatographic column is Zorbax, SB C-18 column (column dimension: 4.6mm × 250mm, 5 μm of partial sizes, Agilent), Detection wavelength 280nm.Solvent system: A, 0.1% trifluoroacetic acid aqueous solution, B, acetonitrile (Merck & Co., Inc., chromatographically pure).Flow velocity: 1.0mL/min；Elution program: 0-5 points Clock, 5%B；5-30min, 5%B-55%B.PPH-I-3 (0.6g) is dissolved in 2mL0.1% trifluoroacetic acid (TFA) aqueous solution Sample solution is made.Separation 50 μ L of sample volume every time collects chromatographic peak segment (objective function peptide) at retention time 11.5min. Sample introduction, elution 40 times altogether, are lyophilized to obtain PPH-I-3-11 powder 295.3mg after merging target peak segment.
4, Structural Identification
Using Matrix-assisted-flight time mass spectrum method (MALDI-TOF-MS), PPH-I-3-11 structure is identified. MALDI-TOF (Ultraflextreme) mass spectrograph extracts reflective-mode using cation delay, to obtain highest resolution ratio And Mass accuracy.Using CHCA as matrix.When test, take 0.5uL PPH-I-3-11 sample solution point in MALDI stainless steel On target plate, solvent volatilization after, then put 0.5uLCHCA solution (0.5g/L, solvent be+50% aqueous acetonitrile of 0.1% trifluoroacetic acid Liquid), it volatilizes to obtain analysis sample at room temperature naturally.Make sample ionization using the 337nm laser that nitrogen laser reflects, is optimizing Parameter under, with 20kv voltage accelerate ion.The LIFT cell voltage of MS/MS experiment is set as 19kv, to reach final The acceleration voltage (reflected voltage) of 29kv.Precursor ion is selected using TIS (timed ion selector).By laser intensity tune After on section to the threshold value for the molecular ion for generating each peptide, 1000 times are irradiated to acquire MS/MS data.
Mass spectrometric data and the fragment parsing of PPH-I-3-11 is as shown in Figure 2.Molecular ion peak [M+1+] be located at 1018.604Da place.Fragment information is retrieved in the MS/MS database of Mascot, does not obtain significant result.And then it uses RapiDeNovo software software, the analysis with de novo sequencing method (de novo sequencing) to fragment ion, can be true Recognize the amino acid sequence of the Functional Polypeptides (PPH-I-3-11) are as follows: the methionine-bright ammonia of Ile-Ile-leucine- Acid-cysteine-serine-leucine-leucine (MIILLCSLL, particular sequence is as shown in SEQ ID NO.1). Met- Ile-Ile-Leu-Leu-Cys-Ser-Leu-Leu.Retrieval through the SWISS-PROT database in NCBI, does not find PPH- The homologous sequence of I-3-11 Functional Polypeptides, the result may indicate that the PPH-I-3-11 Functional Polypeptides of this purifying are from pearl protein The new construction peptide of generation.
The measurement of embodiment 3.DPPH radicals scavenging effect.
This experiment is using the free radical scavenging ability for using DPPH experimental evaluation sample.According to document (Hsu, K.C.；Lu, G.H.；Jao, C.L.,Antioxidative properties of peptides prepared from tuna cooking juice hydrolysates with orientase(Bacillus subtilis).Food Research International 2009,42, (5-6), 647-652.) method, the removing DPPH for measuring pearl protein zymolyte is free The active ability of base.According to default initial concentration, takes the sample of corresponding amount to be dissolved in the water to obtain sample solution, take 100 μ l samples Solution is added to 96 orifice plate the first rows, carries out concentration gradient dilution with ultrapure water, then being separately added into 100 μ l concentration is 2x10- 4The DPPH ethanol solution of mol/L, each concentration do three parallel laboratory tests, and blank test is to replace sample solution by dehydrated alcohol. Mixture is placed 37 DEG C and reacts 30min at dark.Light absorption value is measured at 517nm.The clearance rate of DPPH free radical according to Following formula is calculated:
In formula: S adds the absorbance after the reaction of DPPH for sample；SB is the dehydrated alcohol absorbance that sample adds；C is anhydrous Ethyl alcohol adds the absorbance of DPPH；CB is the absorbance of blank control
Amount effect curve is drawn according to result, the EC of DPPH scavenging capacity can be calculated50Value, i.e. half clear the dose.
The EC that the DPPH of Examples 1 and 2 major sample is removed50Value is see table 1.
Table 1, Examples 1 and 2 separation generate the EC that the DPPH of major sample is removed50Value
Sample PPH PPH-I PPH-II PPH-I-1 PPH-I-2 PPH-I-3 PPH-I-4 PPH-I-3-11
EC50(mg/mL) 30.5±9.2 4.5±1.1 40.5±3.2 7.53±0.53 7.33±0.13 5.88±2.5 10.46±2.3 0.82±0.25
The measurement of embodiment 4 pearl protein hydrolysate and PPH-I-3-11 iron ion reducing power (FRAP)
FRAP is the important measurement index of antioxidant function.This experiment reference literature (Eric A.Decker, and Barbara Welch, Role of ferritin as a lipid oxidation catalyst in muscle Food.J.Agric.Food Chem., 1990,38 (3), pp 674-677) method measurement sample FRAP value.
Take the TPTZ stock solution (with 40mmol/L dissolving with hydrochloric acid) of 10mmol/L, the Fe Cl of 20mmol/L3Solution and 0.3 The acetate buffer solution (pH3.6) of mol/L stands 1 hour at 37 DEG C with volume ratio 1:1:10 mixing, and fresh FRAP is made Working solution.
Respectively into the sample of 100 μ L setting concentration (0.1 and 1.0mg/mL), 300 μ L distilled water are added and 3mL is fresh matches The FRAP working solution of system, is sufficiently mixed, and after 37 DEG C are reacted 30 minutes, absorbance is measured at 593nm wavelength, is made with distilled water For blank control.Standard curve is drawn with 0-600 μM of Trolox standard solution.The reducing power (FRAP value) of sample is with life At Trolox micro-molar concentration indicate (μM TE).
Pearl protein hydrolysate PPH new function peptide PPH-I-3-11 (the bright ammonia of methionine-Ile-Ile- Acid-leucine-cysteine-serine-leucine-leucine；MIILLCSLL) the reducing power knot of positive control sodium sulfite Fruit is listed in table 2.As can be seen from Table 2, untreated pearl protein hydrolysate has certain reducing power, under 1mg/L dosage, FRAP Value has reached 160.58 μM of TE.The reducing power of new function peptide PPH-I-3-11 has reached 709.8 ± 2.8 μM of TE, approaches The level of inorganic reagent sodium sulfite illustrates that this is the new function peptide with good reduction activation.
The reducing power measurement experiment of table 2 pearl protein hydrolysate and new function peptide PPH-I-3-11
*PPH is pearl protein hydrolysate, and PPH-I-3-11 is the Functional Polypeptides of purifying, Na2SO3For positive control.
The melanocyte pigment of 5 Functional Polypeptides PPH-I-3-11 of embodiment generates inhibitory activity
People's epidermal melanocytes (HEM) are provided by Nanfang Medical Univ.Melanocyte culture medium, pancreatin/EDTA disappear Change liquid, pancreatin terminate liquid, poly-D-lysine and is purchased from Biotechnology Co., Ltd, Netac.
Cell culture, cytotoxicity detection, cell survival rate, melanin detection reference literature (Cho, M.；Ryu,M.； Jeong, Y.；Chung,Y.-H.；Kim,D.-E.；Cho,H.-S.；Kang,S.；Han,J.-S.；Chang,M.-Y.；Lee, C.-K., Cardamonin suppresses melanogenesis by inhibition of Wnt/β-catenin signaling.Biochemical and biophysical research communications 2009,390(3), 500-505.) in method carry out.
With 1 × 10 after HEM cell recovery4/cm2Density inoculating cell into culture bottle, be added melanocyte culture Base.After culture 24 hours adherent, (the methionine-Ile-Ile-leucine-of PPH-I-3-11 containing Functional Polypeptides is added Leucine-cysteine-serine-leucine-leucine；MIILLCSLL melanocyte culture medium), each concentration weight It is 3 times multiple.After continuing culture 2 days, with trypsin digestion cell, cell is collected into centrifuge tube.Cell is resuspended after centrifugation, then moves to EP Guan Zhong.It is centrifuged again, collects sediment, dissolve sediment using the NaOH solution of 1M, be placed in 37 degrees Celsius of incubators.To Melanin granule dissolution, then surveys its light absorption value at 490nm.Experimental result is as shown in table 3.
The influence of table 3, PPH-I-3-11 to HEM intracellular melanin content
Sample Final concentration (mg/mL) Melanin content (%) Cell survival rate
Control group 0 100±5.3 100±11.2
Positive control (arbutin) 1.5 68.3±12.5 86.3±9.5
PPH-I-3-11 1.0 96.6±8.8 91.6±5.8
PPH-I-3-11 2.0 82.3±15.5 96.9±3.6
PPH-I-3-11 4.0 63.3±6.2 93.4±15.2
PPH-I-3-11 8.0 41.1±18.8 91.4±7.2
PPH-I-3-11 16.0 40.5±2.8 82.2±5.2
There is inhibiting effect to melanin in HEM cell by Functional Polypeptides PPH-I-3-11 it can be seen from experimental result, And apparent dose-dependant is presented.When Functional Polypeptides PPH-I-3-11 content by 1.0mg/mL increases to 16.0mg/ in culture medium The content of mL, melanin drop to 40.5% by the 96.6% of blank control.Simultaneously compared with positive control arbutin, display compared with Low cytotoxicity removes 16mg/mL group, and cell survival rate is 90% or more.
Sequence table
<110>Chinese Academy of Science Nanhai Ocean Research Institute
<120>a kind of Functional Polypeptides and application thereof in pearl source
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 9
<212> PRT
<213>artificial sequence (Artificial Sequence)
<400> 1
Met Ile Ile Leu Leu Cys Ser Leu Leu
1 5

Claims (9)

1. a kind of Functional Polypeptides, which is characterized in that its amino acid sequence are as follows: methionine-Ile-Ile-leucine- Leucine-cysteine-serine-leucine-leucine.
2. Functional Polypeptides described in claim 1 are preparing the application in free radical scavenger.
3. a kind of free radical scavenger, which is characterized in that contain Functional Polypeptides described in claim 1 as active constituent.
4. Functional Polypeptides described in claim 1 are preparing the application in antioxidant.
5. a kind of antioxidant, which is characterized in that contain Functional Polypeptides described in claim 1 as active constituent.
6. Functional Polypeptides described in claim 1 are preparing the application in melanocyte pigment synthesis inhibitor.
7. a kind of melanocyte pigment synthesis inhibitor, which is characterized in that contain Functional Polypeptides described in claim 1 as work Property ingredient.
8. Functional Polypeptides described in claim 1 are preparing the application in cosmetic material.
9. a kind of cosmetic material, which is characterized in that it contains Functional Polypeptides described in claim 1.
CN201811361112.4A 2018-11-15 2018-11-15 Pearl-derived functional peptide and application thereof Active CN109608520B (en)

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN112877389A (en) * 2021-01-20 2021-06-01 广州市尚梓化工科技有限公司 Preparation method of pearl bright white peptide and application of pearl bright white peptide in whitening cosmetics

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