CN103204906A - Mussel meat protein antioxidative peptide and preparation method thereof - Google Patents
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Abstract
The invention relates to a mussel meat protein antioxidative peptide and a preparation method thereof. The invention is characterized in that the antioxidative peptide is a pentapeptide compound with an amino acid sequence of YPPAK (Tyr-Pro-Pro-Ala-Lys), and according to ESI-MS detection, a molecular ion peak of m/z [M+H]<+> 575.26 is given out. The preparation method comprises the steps consisting of slurry homogenizing, degreasing, mixing, enzymatic hydrolysis, desalination, ultrafiltration, chromatography and the like. The prepared high-activity antioxidative peptide YPPAK (Tyr-Pro-Pro-Ala-Lys) has a good removal effect on DPPH free radicals, hydroxyl free radicals and superoxide anion free radicals; meanwhile, the YPPAK (Tyr-Pro-Pro-Ala-Lys) shows a good inhibitory effect on lipid peroxidation. The YPPAK (Tyr-Pro-Pro-Ala-Lys) has the advantages of safety, no toxic and side effects, good antioxidant activity, easy digestion and absorption, etc., and can be used as a medicine, a health food or foodstuff additive and the like.
Description
Technical field
The present invention relates to protein antioxidant peptide, specifically refer to a kind of mussel meat protein antioxidant peptide and preparation method thereof.
Background technology
Antioxidant is that a class can weaken or dispel radical pair human body infringement and protection food is avoided the rotten class material of oxidative damage, mainly is divided into natural and two types of chemosynthesis.At present, with butylated hydroxy anisole (BHA), butylated hydroxytoluene (BHT) and tertiarybutylhydroquinone (TBHQ) be representative the chemosynthesis antioxidant since price relatively cheap, anti-oxidant activity good, thereby be widely applied in the foodstuffs industry.But the existing chemosynthesis antioxidant that studies show that all has disadvantageous effect in liver, the kidney and other organs to human body in varying degrees.Therefore, the application of chemosynthesis antioxidant has been subjected to considerable influence, and part developed country has limited the quantity of or banned use of chemosynthesis antioxidant to the human body toxic side effect.Therefore, seek efficient, safe natural antioxidants instead of chemical synthetized oxidation preventive agent and become the research focus.
Mussel belongs to Mollusca, lamellibranchiata, mussel order, Mytilidae, mussel belongs to, be the marine products bivalve shellfishs, be commonly called as blue or green mouthful, Hai Hong, have the title of " marine egg ", its protein contains 8 kinds of indispensable amino acids such as the Xie Ansuan, leucine of human body needs, and content is far above egg, chicken, duck, fish, shrimp and meat.There are some researches show, that mussel extract or mussel meat zymolyte have is antitumor, reducing blood-fat, anticoagulation, hypotensive, anti-oxidant, improve immunizing power isoreactivity function, the patent No. is that the Chinese invention patent of ZL200510110096.8 discloses a kind of " extract of Mytilus crassitesta Lischke, manufacture method and uses thereof ", and it is the application of extract aspect anti influenza and anti-SARS virus that utilizes Mytilus crassitesta Lischke; The patent No. is that the Chinese invention patent of ZL200510024391.1 discloses " a kind of Trachyostracous mussel extract that improves immunity function ", and it is that extract about Mytilus crassitesta Lischke is in the application aspect the immunomodulatory; Application number is that 201010296130.6 Chinese invention patent application discloses a kind of " preparation method and the application of anti-prostate cancer mussel enzymatic hydrolyzed extract ", and it is to utilize mussel meat Sumizyme MP (Alcalase) enzymatic hydrolyzed extract that prostate cancer cell is had good inhibited proliferation.Above patent is significant to intensive processing and the active exploitation of mussel.But the active substance that above patent is mentioned mostly is crude extract or total zymolyte, complicated component, and the quality control difficulty is bigger, thereby is subjected to the restriction of many aspects in application
Summary of the invention
Technical problem to be solved by this invention is that the present situation at prior art provides a kind of mussel meat protein antioxidant peptide that can remove free radical and suppress lipid peroxidation, and it can be used as the safe additive of medicine, protective foods and food.
Another technical problem to be solved by this invention provides a kind of preparation method of mussel meat protein antioxidant peptide.
The present invention solves the problems of the technologies described above the technical scheme that adopts: this mussel meat protein antioxidant peptide, it is characterized in that this anti-oxidation peptide is pentapeptide compound, aminoacid sequence is YPPAK (Tyr-Pro-Pro-Ala-Lys), and ESI-MS detects and provides molecular ion peak m/z[M+H]+575.26.
The preparation method of above-mentioned mussel meat protein antioxidant peptide is characterized in that comprising the steps:
1) mussel meat that will clean, shells is processed into homogenate with high-speed tissue mashing machine, add Virahol according to solid-liquid ratio 1g:2 ~ 4mL then, degreasing 20 ~ 24h in 30 ~ 35 ℃, centrifugal 10 ~ 15min removes Virahol in 2～6 ℃, 4000 ~ 5000rpm then, collects degreasing mussel meat solid substance;
2) described degreasing mussel meat solid substance is the phosphate buffered saline buffer of 0.05mol/L by solid-to-liquid ratio 1g:20 ~ 25mL adding concentration, and regulating pH is 6.5 ~ 7.5, obtains mixed solution;
3) described mixeding liquid temperature being risen to 55 ~ 65 ℃ and stir preheating 10 ~ 15min, is that benchmark adds 2.0 ~ 4.0% proteolytic enzyme with the quality of described degreasing mussel meat solid substance, at 55 ~ 65 ℃ of enzymolysis 2 ~ 4h, obtains enzymolysis product;
4) after constant temperature keeps 8 ~ 10min after the enzymolysis product of step 3) gained is warming up to 95 ~ 100 ℃, be cooled to 20 ~ 25 ℃, centrifugal then, obtain enzymolysis solution;
5) above-mentioned enzymolysis solution is added the phosphate buffered saline buffer of 0.05mol/L, making its concentration is 20 ~ 25mg/mL, ratio according to macroporous resin weight and enzymolysis solution volume 1g:40 ~ 50mL joins enzymolysis solution in the macroporous resin chromatography column, be that 45～55% ethanol carries out wash-out with purity then, at last in temperature below 40 ℃, vacuum tightness-0.1MPa steams with backspin and removes ethanol, and concentrated solution carries out lyophilize, gets desalination zymolyte dry powder;
6) above-mentioned desalination zymolyte dry powder is dissolved in the phosphate buffered saline buffer that pH is 0.04～0.06mol/L of 6.8～7.2 and is made into the solution that concentration is 8～12mg/mL, under the working temperature of the operating pressure of 0.1 ~ 0.15MPa and 20 ~ 25 ℃, adopt ultra-filtration membrane to carry out uf processing, collect molecular weight less than the 1kDa part, obtain the ultrafiltration enzymolysis solution, after the freeze-drying of ultrafiltration enzymolysis solution, get ultrafiltration enzymolysis solution lyophilized powder;
7) be that the phosphate buffered saline buffer of 0.04～0.06mol/L of 6.8～7.2 is made into the solution that concentration is 8～12mg/mL with above-mentioned ultrafiltration enzymolysis solution lyophilized powder pH, join anion-exchange resin column, water, 0.1mol/L, 0.5mol/L and 1.0mol/L NaCl solution carry out wash-out respectively then, every 5mL elutriant is collected 1 test tube, and according to the absorbancy drafting elution fraction graphic representation of every test tube elutriant under 280nm, wherein, the highest component of DPPH free radical scavenging activity is the ion-exchange enzymolysis solution, freeze-drying gets dry powder; Described ion-exchange enzymolysis solution lyophilized powder is made into the solution of 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), join in the gel chromatography column, with phosphate buffered saline buffer (0.05mol/L, pH7.0) carry out wash-out, every 5mL elutriant is collected 1 test tube, and draws the elution fraction graphic representation according to the absorbancy of every test tube elutriant under 280nm, wherein, the highest component of DPPH free radical scavenging activity is the preparing gel zymolyte, and freeze-drying gets dry powder;
Above-mentioned preparing gel zymolyte lyophilized powder is made into the solution of 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), carry out purifying with RPLC, collect the highest active polypeptide according to the absorbancy curve under the 280nm and anti-oxidant activity, namely get high reactivity anti-oxidation peptide YPPAK (Tyr-Pro-Pro-Ala-Lys).
Preferably, described mussel meat is Mytilus edulis meat.
Preferably, the proteolytic enzyme described in the step 3) is neutral protease, enzyme activity 〉=2.0 * 105U/g.
Preferred used macroporous resin is D101, and anionite-exchange resin is the DEAE-52 Mierocrystalline cellulose, and used gel is sephadex G-25; Described RPLC condition is: sample size 20 μ L; Chromatographic column is Zorbax C18(250mm * 4.6mm, 5 μ m); Column temperature is 30 ℃; Moving phase: A water (containing 0.1% trifluoroacetic acid) and B acetonitrile (containing 0.1% trifluoroacetic acid); Gradient elution: 0 ~ 55min acetonitrile concentration from 0 to 50%, every 5min increases by 5%; Elution speed 1.0mL/min; The ultraviolet detection wavelength is 280nm.
Compared with prior art, mussel meat protein antioxidant peptide provided by the present invention has good scavenging(action) to DPPH free radical (EC502.62mg/mL), hydroxyl radical free radical (EC500.228mg/mL) and ultra-oxygen anion free radical (EC500.072mg/mL); Simultaneously, YPPAK also demonstrates good lipid peroxidation restraining effect; YPPAK (Tyr-Pro-Pro-Ala-Lys) has good scavenging(action) to DPPH free radical, hydroxyl radical free radical and ultra-oxygen anion free radical; Simultaneously, YPPAK (Tyr-Pro-Pro-Ala-Lys) also demonstrates good lipid peroxidation restraining effect; YPPAK (Tyr-Pro-Pro-Ala-Lys) can be used as the additive of medicine, protective foods and food, and has advantages such as safe without toxic side effect, anti-oxidant activity is strong and be easy to digest and assimilate.Preparation technology is scientific and reasonable for this mussel meat protein antioxidant peptide, select for use neutral protease (neutrase) economical and practical with enzyme as enzymolysis, merge macroporous resin desalination, ultrafiltration classification and chromatographic refining simultaneously by biologic enzymolysis method, enzymolysis process is easily monitored, and the anti-oxidation peptide that makes simultaneously has higher activity.
Description of drawings
The RP-HPLC of Fig. 1 sephadex G-25 preparation zymolyte analyzes.
The mass spectrum of Fig. 2 YPPAK (Tyr-Pro-Pro-Ala-Lys).
The DPPH free radical scavenging activity of Fig. 3 YPPAK (Tyr-Pro-Pro-Ala-Lys).
The hydroxyl radical free radical of Fig. 4 YPPAK (Tyr-Pro-Pro-Ala-Lys) is removed active.
The ultra-oxygen anion free radical of Fig. 5 YPPAK (Tyr-Pro-Pro-Ala-Lys) is removed active.
It is active that the lipid peroxidation of Fig. 6 YPPAK (Tyr-Pro-Pro-Ala-Lys) suppresses.
Embodiment
Describe in further detail below in conjunction with the present invention of accompanying drawing embodiment.
The preparation method of mussel meat protein antioxidant peptide, preparation technology's flow process is as follows: mussel meat → degreasing → enzymolysis → zymolyte → macroporous resin desalination → ultrafiltration → ion exchange chromatography → gel permeation chromatography → high performance liquid chromatography preparation → anti-oxidation peptide.
Concrete steps are:
1) the meat high-speed tissue mashing machine of the Mytilus edulis that will clean, shells is processed into homogenate with it, adds Virahol in 30 ~ 35 ℃ of degreasing 24h according to solid-liquid ratio 1g:3mL then, and centrifugal 15min removes Virahol in 4 ℃, 5000rpm, collects solid substance.
2) degreasing mussel meat solid substance adds 0.05mol/L phosphate buffered saline buffer (pH7.0) by solid-to-liquid ratio 1g:25mL, gets mixed solution;
3) mixeding liquid temperature is risen to 60 ℃ and stir preheating 10min, add neutral protease (neutrase) according to 3% of degreasing mussel meat solid quality, hydrolysis temperature is 60 ℃, and enzymolysis time 3h gets enzymolysis product;
4) enzymolysis product of step 3) gained is gone out enzyme is handled:
1. enzyme goes out: enzymolysis product is warming up to 90 ~ 95 ℃, and after this temperature keeps 10min, is cooled to 20 ~ 25 ℃, with the centrifugal 15min of 5000rpm, gets enzymolysis solution then;
2. desalination: will add the 0.05mol/L phosphate buffered saline buffer in the enzymolysis solution, making its concentration is 20mg/mL, ratio according to macroporous resin weight and enzymolysis solution volume 1g:50mL joins enzymolysis solution in the macroporous resin chromatography column, be that 50% ethanol carries out wash-out with purity then, absorbancy is less than 0.05 under 280nm to elutriant, and at last in temperature below 40 ℃, vacuum tightness-0.1MPa steams the ethanol of removing in the elutriant with backspin, the surplus solution lyophilize gets desalination zymolyte dry powder;
3. ultrafiltration: above-mentioned desalination zymolyte dry powder is dissolved in 0.05mol/L phosphate buffered saline buffer (pH7.0) is made into the solution that concentration is 10mg/mL, under the working temperature of the operating pressure of 0.1 ~ 0.15MPa and 20 ~ 25 ℃, adopt ultra-filtration membrane to carry out uf processing, collect molecular weight less than the 1kDa part, get the ultrafiltration enzymolysis solution, with its freeze-drying, get ultrafiltration enzymolysis solution lyophilized powder;
4. anion-exchange chromatography: the solution that above-mentioned ultrafiltration enzymolysis solution lyophilized powder is made into 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), separate through DEAE-52 Mierocrystalline cellulose anionite-exchange resin, the difference water, 0.1mol/L, 0.5mol/L and 1.0mol/L NaCl solution carries out wash-out, every 5mL elutriant is collected 1 test tube, and according to the absorbancy drafting elution fraction graphic representation of every test tube elutriant under 280nm, each chromatographic peak is a component, wherein, the highest component of DPPH free radical scavenging activity is the ion-exchange enzymolysis solution, with its freeze-drying, get ion-exchange enzymolysis solution lyophilized powder;
5. gel chromatography chromatography: above-mentioned ion-exchange enzymolysis solution lyophilized powder is made into the solution that concentration is 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), through sephadex G-25 column chromatography for separation, carry out wash-out with 5 times of column volume phosphate buffered saline buffers, every 5mL elutriant is collected 1 test tube, and according to the absorbancy drafting elution fraction graphic representation of every test tube elutriant under 280nm, each chromatographic peak is a component, wherein, the highest component of DPPH free radical scavenging activity is the preparing gel zymolyte, with its freeze-drying, get preparing gel zymolyte lyophilized powder.
6. high performance liquid chromatography is refining: above-mentioned preparing gel zymolyte lyophilized powder is made into the solution that concentration is 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), and (RP-HPLC) carries out purifying with RPLC; Condition: sample size 20 μ L; Chromatographic column is Zorbax C18(250mm * 4.6mm, 5 μ m; Column temperature is 30 ℃; Moving phase: A water (containing 0.1% trifluoroacetic acid) and B acetonitrile (containing 0.1% trifluoroacetic acid); Gradient elution: 0-55min acetonitrile concentration from 0 to 50%, every 5min increases by 5%; Elution speed 1.0mL/min; UV detection wavelength 280nm gets 1 high reactivity anti-oxidation peptide according to the absorbancy curve under the 280nm and anti-oxidant activity.
7. structure detection: collect active 1 the highest anti-oxidation peptide, detecting through RPLC (RP-HPLC) is simple spike (Fig. 1), utilize albumen/peptide sequence analysis-e/or determining aminoacid sequence to be YPPAK (Tyr-Pro-Pro-Ala-Lys), ESI-MS detects and provides molecular ion peak m/z[M+H]+575.26(Fig. 2).
The mussel meat protein antioxidant peptide YPPAK (Tyr-Pro-Pro-Ala-Lys) that makes is carried out DPPH free radical scavenging experiment, and test-results is seen Fig. 3; Carry out hydroxyl radical free radical and remove experiment, test-results is seen Fig. 4; Carry out ultra-oxygen anion free radical and remove experiment, test-results is seen Fig. 5; Carry out lipid peroxidation and suppress experiment, test-results is seen Fig. 6.
Experimental result by Fig. 3 to Fig. 6 can be learnt: YPPAK (Tyr-Pro-Pro-Ala-Lys) has good scavenging(action) to DPPH free radical (EC502.62mg/mL), hydroxyl radical free radical (EC500.228mg/mL) and ultra-oxygen anion free radical (EC500.072mg/mL); Simultaneously, YPPAK also demonstrates good lipid peroxidation restraining effect.
Claims (5)
1. a mussel meat protein antioxidant peptide is characterized in that this anti-oxidation peptide is pentapeptide compound, and aminoacid sequence is YPPAK (Tyr-Pro-Pro-Ala-Lys), and ESI-MS detects and provides molecular ion peak m/z[M+H]+575.26.
2. the preparation method of mussel meat protein antioxidant peptide as claimed in claim 1 is characterized in that comprising the steps:
1) mussel meat that will clean, shells is processed into homogenate with high-speed tissue mashing machine, add Virahol according to solid-liquid ratio 1g:2 ~ 4mL then, degreasing 20 ~ 24h in 30 ~ 35 ℃, centrifugal 10 ~ 15min removes Virahol in 2～6 ℃, 4000 ~ 5000rpm then, collects degreasing mussel meat solid substance;
2) described degreasing mussel meat solid substance adds the 0.05mol/L phosphate buffered saline buffer by solid-to-liquid ratio 1g:20 ~ 25mL, and regulating pH is 6.5 ~ 7.5, obtains mixed solution;
3) described mixeding liquid temperature being risen to 55 ~ 65 ℃ and stir preheating 10 ~ 15min, is that benchmark adds 2.0 ~ 4.0% proteolytic enzyme with the quality of described degreasing mussel meat solid substance, at 55 ~ 65 ℃ of enzymolysis 2 ~ 4h, obtains enzymolysis product;
4) enzymolysis product of step 3) gained is warming up to 95 ~ 100 ℃ after behind constant temperature 8 ~ 10min, be cooled to 20 ~ 25 ℃, centrifugal then, obtain enzymolysis solution;
5) above-mentioned enzymolysis solution is added the 0.05mol/L phosphate buffered saline buffer, making its concentration is 20 ~ 25mg/mL, ratio according to macroporous resin weight and enzymolysis solution volume 1g:40 ~ 50mL joins enzymolysis solution in the macroporous resin chromatography column, be that 45～55% ethanol carries out wash-out with purity then, at last in temperature below 40 ℃, vacuum tightness-0.1MPa steams with backspin and removes ethanol, and concentrated solution carries out lyophilize, gets desalination zymolyte dry powder;
6) above-mentioned desalination zymolyte dry powder is dissolved in the phosphate buffered saline buffer that pH is 0.04～0.06mol/L of 6.8～7.2 and is made into the solution that concentration is 8～12mg/mL, under the working temperature of the operating pressure of 0.1 ~ 0.15MPa and 20 ~ 25 ℃, adopt ultra-filtration membrane to carry out uf processing, collect molecular weight less than the 1kDa part, obtain the ultrafiltration enzymolysis solution, after the freeze-drying of ultrafiltration enzymolysis solution, obtain lyophilized powder;
7) be that the phosphate buffered saline buffer of 0.04～0.06mol/L of 6.8～7.2 is made into the solution that concentration is 8～12mg/mL with above-mentioned lyophilized powder pH, join anion-exchange resin column, water, 0.1mol/L, 0.5mol/L and 1.0mol/L NaCl solution carry out wash-out respectively then, every 5mL elutriant is collected 1 test tube, and according to the absorbancy drafting elution fraction graphic representation of every test tube elutriant under 280nm, wherein, the highest component of DPPH free radical scavenging activity is the ion-exchange enzymolysis solution, freeze-drying gets dry powder; Described ion-exchange enzymolysis solution lyophilized powder is made into the solution of 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), join in the gel chromatography column, with phosphate buffered saline buffer (0.05mol/L, pH7.0) carry out wash-out, every 5mL elutriant is collected 1 test tube, and draws the elution fraction graphic representation according to the absorbancy of every test tube elutriant under 280nm, wherein, the highest component of DPPH free radical scavenging activity is the preparing gel zymolyte, and freeze-drying gets dry powder;
Above-mentioned preparing gel zymolyte lyophilized powder is made into the solution of 10mg/mL with 0.05mol/L phosphate buffered saline buffer (pH7.0), carry out purifying with RPLC, collect the highest active polypeptide according to the absorbancy curve under the 280nm and anti-oxidant activity, namely get high reactivity anti-oxidation peptide YPPAK (Tyr-Pro-Pro-Ala-Lys).
3. preparation method according to claim 2 is characterized in that the mussel meat described in the step 1) is Mytilus edulis meat.
4. preparation method according to claim 2 is characterized in that the proteolytic enzyme described in the step 3) is neutral protease, enzyme activity 〉=2.0 * 105U/g.
5. chromatography method according to claim 2 is characterized in that used macroporous resin is D101, and anionite-exchange resin is the DEAE-52 Mierocrystalline cellulose, and used gel is sephadex G-25; Described RPLC condition is: sample size 20 μ L; Chromatographic column is Zorbax C18(250mm * 4.6mm, 5 μ m); Column temperature is 30 ℃; Moving phase: A water (containing 0.1% trifluoroacetic acid) and B acetonitrile (containing 0.1% trifluoroacetic acid); Gradient elution: 0 ~ 55min acetonitrile concentration from 0 to 50%, every 5min increases by 5%; Elution speed 1.0mL/min; The ultraviolet detection wavelength is 280nm.
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