CN103103242A - Antioxidant active peptide and preparation method thereof - Google Patents
Antioxidant active peptide and preparation method thereof Download PDFInfo
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- CN103103242A CN103103242A CN2013100093213A CN201310009321A CN103103242A CN 103103242 A CN103103242 A CN 103103242A CN 2013100093213 A CN2013100093213 A CN 2013100093213A CN 201310009321 A CN201310009321 A CN 201310009321A CN 103103242 A CN103103242 A CN 103103242A
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Abstract
The invention discloses an antioxidant active peptide and a preparation method thereof. The antioxidant active peptide is characterized by taking decapterus fish protein as the raw material, alkaline protease generated by bacillus subtilis 2709 is adopted for hydrolysis, after enzyme deactivation of the hydrolysate, the hydrolysate is separated through centrifugation, ultra-filtration, gel chromatography and reverse phase high performance liquid chromatography so as to determine the structures of two natural antioxidant peptide, the amino acid sequences are His-Asp-His-Pro-Val-Cys (histidine-aspartic acid-histidine-proline-valine-cysteine) and His-Glu-Lys-Val-Cys(histidine-glutamic acid-lysine-valine-cysteine), the concentration (EC50) for eliminating DPPH (1,1-Diphenyl-2-picrylhydrazyl) radical of 50% are 0.0310+/-0.0011mu M and 0.0677+/-0.0012mu M, the concentration for eliminating superoxide anion (O2-) radical of 50% are 0.3814+/-0.0017mu M and 0.3744+/-0.0021mu M, and the antioxidant active peptide has good antioxidant activity.
Description
Technical field
The invention belongs to the functional food field, be specifically related to the blue circle of marine low-value fish Scad fish protein antioxidation active peptides and preparation method thereof.
Background technology
The chemosynthesis class antioxidant that often is used as foodstuff additive is limited to use owing to itself having toxicity, side effect as BHA (BHA), butylated hydroxytoluene (BHT) etc.Natural antioxidants not only can prevent the oxidation of grease system in food, and can prevent the harm of free radical in human body, delay senility and various chronic degenerative disorders as cancer, coronary heart disease, diabetes etc.Peptide class between protein and amino acids, due to its special constructional feature, high security and significant biological activity and be widely studied.In recent years, people separate and have obtained a large amount of Natural Antioxidant Peptides from multiple animal/vegetable protein, and wherein animal protein source anti-oxidation peptide is in the majority with the aquatic products anti-oxidation peptide.And marine organisms are of a great variety, quantity is huge, and its protein all is being very different with terrestrial life albumen aspect amino acid whose composition and sequence, also increasingly active to its exploitation." aquatic science " the 7th phase 370-373 page in 2008 has reported that the hydrolysis marine protein prepares the high reactivity anti-oxidation peptide as Alaska pollock, mackerel, tuna etc.Chinese patent (ZL201010141974.3) discloses and has been derived from anti-oxidation peptide of collagen protein and uses thereof, separates and has obtained the anti-oxidation peptide of four different aminoacids sequences from collagen protein, and can be advantageously applied to food, makeup, healthcare products etc.
Blue circle Scad (Decapterus maruadsi), it is a kind of that the circle Scad of Perciformes Scad section belongs to.Claim again pond fish, Ba Lang fish etc.Be distributed in the Indian Ocean and the Pacific Ocean, China's main product in the South Sea, the East Sea, be one of important economic fish.Because price is low, processing and recovering means fall behind, and makes salty dry product or feed fish meal more and use, economic benefit is low.Many research is in recent years inquired into its comprehensive utilization, as " food research and development " the 12nd phase in 2007, " foodstuffs industry science and technology " the 1st phase in 2008 and " Guangdong Ocean University's journal " the 4th phase in 2009 all adopt the blue circle of different protease hydrolyzeds Scad albumen, take respectively the content of nitrogen recovery in enzymolysis product, amino nitrogen or polypeptide extraction yield selects the suitableeest proteolytic enzyme as index and use enzyme as experiment, and has carried out the investigation of enzymolysis process condition." Food science " the 1st phase in 2009 has been studied auxiliary material and each metal ion species impact on the circle of the indigo plant through Alcalase 2.4 enzymolysis Scad anti-oxidation peptide stability in temperature, pH value, food." China brewages " the 9th phase in 2009 is selected respectively neutral protease and the blue circle of Sumizyme MP enzymolysis Scad albumen with " food research and development " the 2nd phase in 2010, and utilizes the center combination test method to optimize the enzymolysis experiment condition." Chinese food journal " the 8th phase in 2012 has described response Surface Analysis method and has optimized the hydrolysis process condition of papoid and the blue circle of flavor protease hydrolysis Scad albumen, and adopts free radical scavenging activity to be studied the anti-oxidant activity of hydrolysate.These all only relate to enzymolysis processing technology or the aspects such as product anti-oxidant activity and Stability Determination thereof, and the preparation method that separation and purification goes out single antioxidation active peptides from indigo plant circle Scad fish protein there is not yet report.
Summary of the invention
The invention provides and be derived from the blue circle of marine fishes Scad fish protein antioxidation active peptides and preparation method thereof, it is characterized in that take that indigo plant circle Scad fish protein is raw material, the hydrolysis by novo that adopts Bacillus subtilus 2709 to produce, separate and determine the wherein structure of two kinds of Natural Antioxidant Peptides through centrifugal, ultrafiltration, gel chromatography, RPLC multistep.
Specific implementation Step By Condition of the present invention is as follows:
(1) the reaction raw materials liquid that is 1～5wt% by indigo plant circle Scad fish protein powder with water mixing furnishing protein content; Then adding 0.002～0.05wt% Sumizyme MP, is 7.5～10 times hydrolysis 3～6 hours at 45～60 ℃ and pH, finally is heated to 100 ℃ with enzymolysis reaction;
(2) by step 1) enzymolysis solution that obtains is in 4 ℃, the centrifugal 10～15min of 8000r/min, and obtain supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid;
(3) take deionized water adopts Sephedex G-15 gel chromatography column separating step 2 as moving phase) ultrafiltrated permeation liquid that obtains, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in the 280nm place with the protein nucleic acid detector, No. 2 absorption peak (seeing Fig. 1) components of collecting high-activity freeze-drying;
(4) by step 3) freeze-dried component that obtains further separates with reversed-phase HPLC, use ODS post (Hedera ODS-C2,10 * 250mm), adopting water and acetonitrile (0～21～50% acetonitrile in 0～25～60min) containing 0.1% trifluoroacetic acid is the moving phase linear elution, detect elution peak under the 220nm wavelength and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, according to detecting spectrogram (seeing Fig. 2), collect active No. 1 the highest elutriant corresponding to absorption peak; Then use C18 post (HypersilODS-C18,4.6 * 250mm) instead No. 1 absorption peak elutriant is carried out to purifying again, gradient is 0～20% acetonitrile in 40min, flow velocity 0.5mLmin
-1, No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak according to detecting spectrogram (seeing Fig. 3) and collect respectively greater activity, obtain anti-oxidation peptide; Use the time-of-flight mass spectrometry instrument to measure and obtain two anti-oxidation peptides that aminoacid sequence is respectively His-Asp-His-Pro-Val-Cys (Histidine-aspartic acid-Histidine-proline(Pro)-α-amino-isovaleric acid-halfcystine) (seeing Fig. 4) and His-Glu-Lys-Val-Cys (Histidine-glutamic-lysine-α-amino-isovaleric acid-halfcystine) (seeing Fig. 5).
Adopt respectively ultra-oxygen anion free radical and DPPH free radical scavenging method to measure the resistance of oxidation of 2 anti-oxidation peptides.Anti-oxidation peptide His-Asp-His-Pro-Val-Cys removes 50%DPPH free radical desired concn (EC
50) be 0.0310 ± 0.0011 μ M, suitable with the removing ability of Natural Antioxidant Peptides gsh; Remove 50% ultra-oxygen anion free radical desired concn (EC
50) be 0.3814 ± 0.0017 μ M.Anti-oxidation peptide His-Glu-Lys-Val-Cys removes 50%DPPH free radical desired concn (EC
50) be 0.0677 ± 0.0012 μ M, remove 50% ultra-oxygen anion free radical desired concn (EC
50) be 0.3744 ± 0.0021 μ M.From result, 2 anti-oxidation peptides that are derived from the blue circle Scad flesh of fish of the present invention all have good anti-oxidant activity in these two kinds of detection system.
The present invention prepares the raw material sources cheapness of anti-oxidation peptide, aboundresources, and the preparation method is simple, cost is low and easy operation, has stronger suitability; The anti-oxidant activity of prepared anti-oxidation peptide is strong, good water solubility and safe, nontoxic, have no side effect etc., suitable food, makeup, the medicine and other fields of being applied to.
Adopt respectively DPPH method and ultra-oxygen anion free radical method to measure the radical scavenging activity of blue circle Scad fish protein anti-oxidation peptide in the present invention, these methods are all conventional detection methods, and concrete steps are as follows:
1, measure anti-oxidation peptide and remove 1,1-phenylbenzene trinitrophenyl-hydrazine (DPPH) free radical ability
Get testing sample 500 μ L, add the methanol solution of 500 μ L 0.1mM DPPH.Mix rear 30 ℃ of standing 30min of lower lucifuge, measure absorbance in the 515nm place.Calculate the DPPH radical scavenging activity according to following formula, wherein, with deionized water, substitute sample, the absorbance of surveying in contrast, substitutes DPPH solution with methyl alcohol, and the absorbance of surveying is as blank.
DPPH radical scavenging activity (%)=(control sample+blank sample-treat test sample) * 100%/control sample
2, measure anti-oxidation peptide and remove superoxide anion (O
2 -) the free radical ability
Get testing sample 200 μ L, add 5.7mL tris-HCl damping fluid (50mM, pH8.2), and 100 μ L 5mM pyrogallol solution, an A surveyed in the 320nm place every 30s after mixing
320nm, reaction 4min finishes, and obtains sample V
sample(being the average rate of change of every min photoabsorption).Replace pyrogallol solution with 10mmol/L HCl in blank tube, in 4min, pyrogallol autoxidation speed is V
in vain.
O
2 -radical scavenging activity (%)=[(V
in vain-V
sample)/V
in vain] * 100%
The accompanying drawing explanation
The protein detection spectrogram of elutriant when Fig. 1 is gel chromatography separation ultrafiltrated permeation liquid
Fig. 2 is that the HPLC of No. 2 absorption peaks in Fig. 1 elutriant detects spectrogram
Fig. 3 is that the HPLC of No. 1 absorption peak in Fig. 2 elutriant detects spectrogram
Fig. 4 is the aminoacid sequence mass spectrum of No. 1 absorption peak in Fig. 3 elutriant
Fig. 5 is the aminoacid sequence mass spectrum of No. 2 absorption peaks in Fig. 3 elutriant
embodiment:
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 1wt% with water mixing furnishing protein content; Then adding the 0.03wt% Sumizyme MP, is 8.0 times hydrolysis 3 hours at 50 ℃ and pH, finally is heated to 100 ℃ with enzymolysis reaction.By the mixed solution that obtains in 4 ℃, centrifugal 10～the 15min of 8000r/min, get the enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, the deionized water of take separates ultrafiltrated permeation liquid as moving phase adopts Sephedex G-15 gel chromatography, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in the 280nm place with the protein nucleic acid detector, No. 2 absorption peaks (seeing Fig. 1) of collecting high-activity further separate with reversed-phase HPLC, use ODS post (Hedera ODS-C2, 10 * 250mm), adopting water and acetonitrile (5～60% acetonitriles in 55min) containing 0.1% trifluoroacetic acid is the moving phase linear elution, detect elution peak under the 220nm wavelength and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, according to detecting spectrogram (seeing Fig. 2), collect active No. 1 the highest elutriant corresponding to absorption peak, then use C18 post (Hypersil ODS-C18,4.6 * 250mm) instead No. 1 absorption peak elutriant is carried out to purifying again, gradient is 0～20% acetonitrile in 30min, flow velocity 0.5mLmin
-1, No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak according to detecting spectrogram (seeing Fig. 3) and collect respectively greater activity, obtain anti-oxidation peptide, use time-of-flight mass spectrometry to measure and obtain two anti-oxidation peptides that aminoacid sequence is respectively His-Asp-His-Pro-Val-Cys (Histidine-aspartic acid-Histidine-proline(Pro)-α-amino-isovaleric acid-halfcystine) and His-Glu-Lys-Val-Cys (Histidine-glutamic-lysine-α-amino-isovaleric acid-halfcystine).
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 3wt% with water mixing furnishing protein content; Then adding the 0.005wt% Sumizyme MP, is 10 times hydrolysis 6 hours at 55 ℃ and pH, finally is heated to 100 ℃ with enzymolysis reaction.By the mixed solution that obtains in 4 ℃, centrifugal 10～the 15min of 8000r/min, get the enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, the deionized water of take separates ultrafiltrated permeation liquid as moving phase adopts Sephedex G-15 gel chromatography, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in the 280nm place with the protein nucleic acid detector, No. 2 absorption peaks (seeing Fig. 1) of collecting high-activity further separate with reversed-phase HPLC, use ODS post (Hedera ODS-C2, 10 * 250mm), adopting water and acetonitrile (0～60% acetonitrile in 60min) containing 0.1% trifluoroacetic acid is the moving phase linear elution, detect elution peak under the 220nm wavelength and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, according to detecting spectrogram (seeing Fig. 2), collect active No. 1 the highest elutriant corresponding to absorption peak, then use C18 post (Hypersil ODS-C18,4.6 * 250mm) instead No. 1 absorption peak elutriant is carried out to purifying again, gradient is 5～20% acetonitriles in 40min, flow velocity 0.5mLmin
-1, No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak according to detecting spectrogram (seeing Fig. 3) and collect respectively greater activity, obtain anti-oxidation peptide, use time-of-flight mass spectrometry to measure and obtain two anti-oxidation peptides that aminoacid sequence is respectively His-Asp-His-Pro-Val-Cys (Histidine-aspartic acid-Histidine-proline(Pro)-α-amino-isovaleric acid-halfcystine) and His-Glu-Lys-Val-Cys (Histidine-glutamic-lysine-α-amino-isovaleric acid-halfcystine).
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 5wt% with water mixing furnishing protein content; Then adding the 0.05wt% Sumizyme MP, is 8.0 times hydrolysis 4.5 hours at 45 ℃ and pH, finally is heated to 100 ℃ with enzymolysis reaction.By the mixed solution that obtains in 4 ℃, centrifugal 10～the 15min of 8000r/min, get the enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, the deionized water of take separates ultrafiltrated permeation liquid as moving phase adopts Sephedex G-15 gel chromatography, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in the 280nm place with the protein nucleic acid detector, No. 2 absorption peaks (seeing Fig. 1) of collecting high-activity further separate with reversed-phase HPLC, use ODS post (Hedera ODS-C2, 10 * 250mm), adopting water and acetonitrile (5～55% acetonitriles in 60min) containing 0.1% trifluoroacetic acid is the moving phase linear elution, detect elution peak under the 220nm wavelength and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, according to detecting spectrogram (seeing Fig. 2), collect active No. 1 the highest elutriant corresponding to absorption peak, then use C18 post (Hypersil ODS-C18,4.6 * 250mm) instead No. 1 absorption peak elutriant is carried out to purifying again, gradient is 5～20% acetonitriles in 50min, flow velocity 0.5mLmin
-1, No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak according to detecting spectrogram (seeing Fig. 3) and collect respectively greater activity, obtain anti-oxidation peptide, use time-of-flight mass spectrometry to measure and obtain two anti-oxidation peptides that aminoacid sequence is respectively His-Asp-His-Pro-Val-Cys (Histidine-aspartic acid-Histidine-proline(Pro)-α-amino-isovaleric acid-halfcystine) and His-Glu-Lys-Val-Cys (Histidine-glutamic-lysine-α-amino-isovaleric acid-halfcystine).
Claims (2)
1. a method for preparing blue circle Scad fish protein antioxidation active peptides, is characterized in that take that indigo plant circle Scad fish protein is raw material, the hydrolysis by novo that adopts subtilis 2709 to produce, and concrete technology is:
(1) the reaction raw materials liquid that is 1～5wt% by indigo plant circle Scad fish protein powder with water mixing furnishing protein content, then add 0.002～0.05wt% Sumizyme MP, be 7.5～10 times hydrolysis 3～6 hours at 45～60 ℃ and pH, finally be heated to 100 ℃ of enzymes that go out and obtain enzymolysis solution;
(2) by enzymolysis solution in 4 ℃, the centrifugal 10～15min of 8000r/min, obtain supernatant liquor and use ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid;
(3) take the penetrating fluid that deionized water adopts Sephedex G-15 gel chromatography column separating step 2 to obtain as moving phase, and detecting and measure the anti-oxidant activity of the elutriant that each peak is corresponding in the 280nm place with the protein nucleic acid detector, No. 2 absorption peak (seeing Fig. 1) components the freeze-drying of collecting high-activity obtain the freeze-drying body;
(4) freeze-drying body step 3 obtained further separates with reversed-phase HPLC, use ODS post (Hedera ODS-C2,10 * 250mm), adopting water and acetonitrile (0～21～50% acetonitrile in 0～25～60min) containing 0.1% trifluoroacetic acid is the moving phase linear elution, detect elution peak under the 220nm wavelength and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, according to detecting spectrogram (seeing Fig. 2), collect active No. 1 the highest elutriant corresponding to absorption peak; Then use C18 post (Hypersil ODS-C18,4.6 * 250mm) instead No. 1 absorption peak elutriant is carried out to purifying again, gradient is 0～20% acetonitrile in 40min, flow velocity 0.5mLmin
-1, No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak according to detecting spectrogram (seeing Fig. 3) and collect respectively greater activity, obtain two anti-oxidation peptides.
2. indigo plant claimed in claim 1 is justified Scad fish protein antioxidation active peptides, and its aminoacid sequence is respectively His-Asp-His-Pro-Val-Cys (Histidine-aspartic acid-Histidine-proline(Pro)-α-amino-isovaleric acid-halfcystine) (its mass spectrum is shown in Fig. 4) and His-Glu-Lys-Val-Cys (Histidine-glutamic-lysine-α-amino-isovaleric acid-halfcystine) (its mass spectrum is shown in Fig. 5).
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Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103936817A (en) * | 2014-04-30 | 2014-07-23 | 江南大学 | Preparation method for fish protein antioxidant peptide |
| CN104087638A (en) * | 2014-07-29 | 2014-10-08 | 湖南农业大学东方科技学院 | Method for preparing antioxidative peptide through fermentation of rice residue by use of bacillus subtilis |
| CN104177477A (en) * | 2014-08-28 | 2014-12-03 | 滨州万嘉生物科技有限公司 | Fish anti-oxidation active peptide and preparation method thereof |
| CN104530187A (en) * | 2014-12-11 | 2015-04-22 | 华南理工大学 | Saury antioxidative peptide as well as separation and extraction method and application thereof |
| CN105219825A (en) * | 2015-09-07 | 2016-01-06 | 中国水产科学研究院南海水产研究所 | The preparation method of the anti-oxidant calcium ion chelating peptide of a kind of Lan Yuan Ajigasawa |
| CN106036746A (en) * | 2016-06-23 | 2016-10-26 | 阿波食品有限公司 | Decapterus maruadsi seafood seasoner and preparation method thereof |
| CN108103130A (en) * | 2017-12-25 | 2018-06-01 | 大连深蓝肽科技研发有限公司 | The combination technique of extraction separation small active peptides from marine protein resource |
| CN109529011A (en) * | 2019-01-08 | 2019-03-29 | 广东兴亿海洋生物工程股份有限公司 | Marine fishes oligopeptide has effects that the application in the drug, health care product or food that inhibit liver cancer cells in preparation |
| CN109913486A (en) * | 2019-04-11 | 2019-06-21 | 中国科学院新疆理化技术研究所 | A kind of biological expression of anti-oxidation peptide NV13 recombination and application |
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Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103936817A (en) * | 2014-04-30 | 2014-07-23 | 江南大学 | Preparation method for fish protein antioxidant peptide |
| CN104087638A (en) * | 2014-07-29 | 2014-10-08 | 湖南农业大学东方科技学院 | Method for preparing antioxidative peptide through fermentation of rice residue by use of bacillus subtilis |
| CN104087638B (en) * | 2014-07-29 | 2017-06-16 | 湖南农业大学 | A kind of method that utilization fermentation of bacillus subtilis rice residue prepares anti-oxidation peptide |
| CN104177477A (en) * | 2014-08-28 | 2014-12-03 | 滨州万嘉生物科技有限公司 | Fish anti-oxidation active peptide and preparation method thereof |
| CN104530187A (en) * | 2014-12-11 | 2015-04-22 | 华南理工大学 | Saury antioxidative peptide as well as separation and extraction method and application thereof |
| CN105219825A (en) * | 2015-09-07 | 2016-01-06 | 中国水产科学研究院南海水产研究所 | The preparation method of the anti-oxidant calcium ion chelating peptide of a kind of Lan Yuan Ajigasawa |
| CN106036746A (en) * | 2016-06-23 | 2016-10-26 | 阿波食品有限公司 | Decapterus maruadsi seafood seasoner and preparation method thereof |
| CN108103130A (en) * | 2017-12-25 | 2018-06-01 | 大连深蓝肽科技研发有限公司 | The combination technique of extraction separation small active peptides from marine protein resource |
| CN109529011A (en) * | 2019-01-08 | 2019-03-29 | 广东兴亿海洋生物工程股份有限公司 | Marine fishes oligopeptide has effects that the application in the drug, health care product or food that inhibit liver cancer cells in preparation |
| CN109913486A (en) * | 2019-04-11 | 2019-06-21 | 中国科学院新疆理化技术研究所 | A kind of biological expression of anti-oxidation peptide NV13 recombination and application |
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