CN103103242B - Antioxidant active peptide and preparation method thereof - Google Patents
Antioxidant active peptide and preparation method thereof Download PDFInfo
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- CN103103242B CN103103242B CN201310009321.3A CN201310009321A CN103103242B CN 103103242 B CN103103242 B CN 103103242B CN 201310009321 A CN201310009321 A CN 201310009321A CN 103103242 B CN103103242 B CN 103103242B
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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 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 is often 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 people's interior free yl, 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 aquatic products anti-oxidation peptide.And marine organisms are of a great variety, quantity is huge, and its protein is all 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 hydrolysis marine protein prepares 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, from collagen protein, separate and obtained the anti-oxidation peptide of four different aminoacids sequences, and can be advantageously applied to food, makeup, healthcare products etc.
Blue circle Scad (Decapterus maruadsi), the one 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, select the suitableeest proteolytic enzyme as experiment enzyme taking the content of nitrogen recovery, amino nitrogen in enzymolysis product or polypeptide extraction yield as index respectively, and carried out the investigation of enzymolysis process condition." Food science " the 1st phase in 2009 has been studied auxiliary material and the impact of each metal ion species on the indigo plant circle Scad anti-oxidation peptide stability through Alcalase2.4 enzymolysis 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 center combination test method to optimize 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 study the anti-oxidant activity of hydrolysate.These all only relate to the aspect such as enzymolysis processing technology or 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 taking indigo plant circle Scad fish protein as raw material, adopt the hydrolysis by novo that produces of Bacillus subtilus 2709, 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 DEG C and pH, is finally heated to 100 DEG C with enzymolysis reaction;
(2) by step 1) enzymolysis solution that obtains is in 4 DEG C, 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) adopt Sephedex G-15 gel chromatography column separating step 2 taking deionized water 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 280nm place with protein nucleic acid detector, No. 2 absorption peak (seeing Fig. 1) components of collecting high-activity freeze-drying;
(4) by step 3) the freeze-dried component reversed-phase HPLC that obtains further separates, use ODS post (Hedera ODS-C2,10 × 250mm), adopting containing water and the acetonitrile (0～21～50% acetonitrile in 0～25～60min) of 0.1% trifluoroacetic acid is moving phase linear elution, under 220nm wavelength, detect elution peak and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, collect active No. 1 the highest elutriant corresponding to absorption peak according to detecting spectrogram (seeing Fig. 2); 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, collect respectively No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak of greater activity according to detecting spectrogram (seeing Fig. 3), obtain anti-oxidation peptide; Use time-of-flight mass spectrometry instrument mensuration acquisition aminoacid sequence to be respectively two anti-oxidation peptides of 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, removing 50% ultra-oxygen anion free radical desired concn (EC50) is 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 preparation method is simple, cost is low and easily 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 L0.1mM DPPH..Mix lucifuge at latter 30 DEG C and leave standstill 30min, measure absorbance in 515nm place.Calculate DPPH radical scavenging activity according to following formula, wherein, substitute sample with deionized water, the absorbance of surveying in contrast, substitutes DPPH solution with methyl alcohol, and the absorbance of surveying is as blank.
DPPH self-love base is removed ability (%)=(control sample+blank sample-treat test sample) × 100%/control sample
2, measure anti-oxidation peptide and remove superoxide anion (O2-) free radical ability
Get testing sample 200 μ L, add 5.7mL tris-HCl damping fluid (50mM, pH8.2), and 100 μ L5mM pyrogallol solution, after mixing, survey an A in 320nm place every 30s
320nm, reaction 4min finishes, and obtains sample V
sample(being the average rate of change of every min photoabsorption).In blank tube, replace pyrogallol solution with 10mmol/L HCl, in 4min, pyrogallol autoxidation speed is V
in vain.
O
2 -radical scavenging activity (%)=[(V
in vain-V
sample)/V
in vain] × 100%
Brief description of the drawings
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:
Embodiment 1
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 1wt% with water mixing furnishing protein content; Then adding 0.03wt% Sumizyme MP, is 8.0 times hydrolysis 3 hours at 50 DEG C and pH, is finally heated to 100 DEG C with enzymolysis reaction.By the mixed solution obtaining in 4 DEG C, centrifugal 10～the 15min of 8000r/min, get enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, adopt Sephedex G-15 gel chromatography to separate ultrafiltrated permeation liquid taking deionized water as moving phase, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in 280nm place with 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 containing water and the acetonitrile (5～60% acetonitriles in 55min) of 0.1% trifluoroacetic acid is moving phase linear elution, under 220nm wavelength, detect elution peak and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, collect active No. 1 the highest elutriant corresponding to absorption peak according to detecting spectrogram (seeing Fig. 2), 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, collect respectively No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak of greater activity according to detecting spectrogram (seeing Fig. 3), obtain anti-oxidation peptide, use time-of-flight mass spectrometry mensuration acquisition aminoacid sequence to be respectively two anti-oxidation peptides of 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).
Embodiment 2
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 3wt% with water mixing furnishing protein content; Then adding 0.005wt% Sumizyme MP, is 10 times hydrolysis 6 hours at 55 DEG C and pH, is finally heated to 100 DEG C with enzymolysis reaction.By the mixed solution obtaining in 4 DEG C, centrifugal 10～the 15min of 8000r/min, get enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, adopt Sephedex G-15 gel chromatography to separate ultrafiltrated permeation liquid taking deionized water as moving phase, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in 280nm place with 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 containing water and the acetonitrile (0～60% acetonitrile in 60min) of 0.1% trifluoroacetic acid is moving phase linear elution, under 220nm wavelength, detect elution peak and collect and measure each peak anti-oxidant activity, flow velocity 1.5mLmin
-1, collect active No. 1 the highest elutriant corresponding to absorption peak according to detecting spectrogram (seeing Fig. 2), 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 0.5mL.min
-1, collect respectively No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak of greater activity according to detecting spectrogram (seeing Fig. 3), obtain anti-oxidation peptide, use time-of-flight mass spectrometry mensuration acquisition aminoacid sequence to be respectively two anti-oxidation peptides of 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).
Embodiment 3
Get the reaction raw materials liquid that blue circle Scad fish protein powder is 5wt% with water mixing furnishing protein content; Then adding 0.05wt% Sumizyme MP, is 8.0 times hydrolysis 4.5 hours at 45 DEG C and pH, is finally heated to 100 DEG C with enzymolysis reaction.By the mixed solution obtaining in 4 DEG C, centrifugal 10～the 15min of 8000r/min, get enzymolysis supernatant liquor and use the ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid, adopt Sephedex G-15 gel chromatography to separate ultrafiltrated permeation liquid taking deionized water as moving phase, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in 280nm place with 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 containing water and the acetonitrile (5～55% acetonitriles in 60min) of 0.1% trifluoroacetic acid is moving phase linear elution, under 220nm wavelength, detect elution peak and collect and measure each peak anti-oxidant activity, flow velocity 1.5mL.min
-1, collect active No. 1 the highest elutriant corresponding to absorption peak according to detecting spectrogram (seeing Fig. 2), 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, collect respectively No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak of greater activity according to detecting spectrogram (seeing Fig. 3), obtain anti-oxidation peptide, use time-of-flight mass spectrometry mensuration acquisition aminoacid sequence to be respectively two anti-oxidation peptides of 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 preparation method for blue circle Scad fish protein antioxidation active peptides, is characterized in that taking indigo plant circle Scad fish protein as 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 DEG C and pH, be finally heated to 100 DEG C of enzymes that go out and obtain enzymolysis solution;
(2) by enzymolysis solution in 4 DEG C, the centrifugal 10～15min of 8000r/min, obtains supernatant liquor and uses ultra-filtration membrane ultra-filtration and separation that molecular weight is 5000Da to collect penetrating fluid;
(3) penetrating fluid that adopts Sephedex G-15 gel chromatography column separating step 2 to obtain taking deionized water as moving phase, and detect and measure the anti-oxidant activity of the elutriant that each peak is corresponding in 280nm place with protein nucleic acid detector, collect the highly active No. 2 absorption peak components of spectrogram 1 freeze-drying and obtain freeze-drying body;
(4) freeze-drying body reversed-phase HPLC step 3 being obtained further separates, use ODS post Hedera ODS-C2,10 × 250mm, adopting containing water and the acetonitrile of 0.1% trifluoroacetic acid is moving phase linear elution, gradient is 0～21～50% acetonitrile in 0～25～60min, flow velocity 1.5mLmin
-1, under 220nm wavelength, detect elution peak and collect and measure each peak anti-oxidant activity, collect active No. 1 the highest elutriant corresponding to absorption peak according to detecting spectrogram 2; Then use C18 post Hypersil ODS-C18 instead, 4.6 × 250mm, carries out purifying again to No. 1 absorption peak elutriant, and gradient is 0～20% acetonitrile in 40min, flow velocity 0.5mLmin
-1, collect respectively No. 1 and No. 2 corresponding elutriant the lyophilizes of absorption peak of greater activity according to detecting spectrogram 3, obtain two anti-oxidation peptides.
2. the indigo plant circle Scad fish protein antioxidation active peptides that preparation method obtains according to claim 1, its 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).
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN103936817A (en) * | 2014-04-30 | 2014-07-23 | 江南大学 | Preparation method for fish protein antioxidant peptide |
| 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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