CN101240312A - Method for preparing ACE inhibition peptide originate from fish skin - Google Patents
Method for preparing ACE inhibition peptide originate from fish skin Download PDFInfo
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- CN101240312A CN101240312A CNA2008100467456A CN200810046745A CN101240312A CN 101240312 A CN101240312 A CN 101240312A CN A2008100467456 A CNA2008100467456 A CN A2008100467456A CN 200810046745 A CN200810046745 A CN 200810046745A CN 101240312 A CN101240312 A CN 101240312A
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Abstract
A method for preparing ACE inhibition peptides from fish skin is provided. The method is prepared with tilapia skin, extracts fish skin albumen from tilapia skin, adapts prolease to hydrolysis through enzyme extinguishing, debitterizing, decolouring, de-flavoring, filtering, ion exchanging and concentrating to obtain fish skin proteolysis liquor, after untruly filter (cutoff molecular mass is 9000Da) the TSP-I, collect high activity component by SephadexG-15 gel chromatography, freeze and dry to obtain high activity ACE inhibition peptides. The invention has important meaning for satisfying integrated utilization of tilapia skin wastes and improving its attachment.
Description
Technical field
The present invention relates to a kind of preparation method who comes from the ace inhibitory peptide of fish-skin.
Background technology
Angiotensin-converting enzyme (ACE) plays an important role to blood pressure regulation, renin-angiotensin system (renin-angiotensin system at human body, RAS) and kallikrein kinin system (kallikrein-kinin system, KKS) in, ACE is a substrate with angiotensin I and bradykinin, cause vasoconstriction, cause elevation of the blood pressure.
Angiotensin converting enzyme inhibitor (ACEI) is to treat hypertension and main active drug in heart failure now, the ACE inhibitor of chemosynthesis has exposed many defectives when clinical use, as: action time is short, and blood pressure easily rebounds, and damage etc. is caused at a plurality of positions in the human body.ACE inhibitor-Zinc metallopeptidase Zace1 the inhibiting peptide that comes from food proteins is because of its edible safety height, and advantage such as have no side effect has caused people's extensive concern.
At present existing people isolates from food such as sardines, tuna, wheat, corn, soybean, sour milk, pure mellow wine to have ACE and suppresses active step-down peptide and demonstrated good prospects for application.
China is tilapia producing country the biggest in the world, and along with the rising year by year of fresh fish sheet, frozen fish fillet and bar frozen fish export volume, tankage such as consequent a large amount of fish-skins need to handle.These tankage not only can cause great waste, but also can cause the pollution of environment if effectively do not utilize.At present, external comparatively deep to the research of fish collagen protein, the research of relevant collagen of fish skin also has many reports, and still, to the relevant research of tilapia fishskin collagen protein, neither system also lacks the degree of depth.
Tilapia fishskin contains abundant collagen protein, if can make full use of it, by the bioactive peptide of enzyme process processing fresh-water fishes collagen protein acquisition inhibition ACE, will receive good economic benefits and social benefit to the raising that promotes people's quality of life.
Summary of the invention
The purpose of this invention is to provide a kind of separating and purifying technology that comes from the ace inhibitory peptide of fish-skin, obtain to have in the fish-skin polypeptide fragment of hypotensive activity.
The present invention is achieved like this, and its method steps is:
1, pre-treatment: the fish-skin after the cleaning soaks 1hr with the hydrochloric acid soln of 0.1mol/L and the sodium hydroxide solution of 0.1mol/L successively after degreasing.
2, water is carried: pretreated fish-skin is through washing to neutrality, and under 45 ℃ of conditions, behind the distilled water constant temperature homogenate 12hr with 10 times of volumes, suction filtration extracts supernatant liquor.
3, enzymolysis:, adopt papoid and neutral protease to carry out enzymolysis, the relatively hydrolysis result of two kinds of enzymes, and definite optimum enzymolysis condition under certain condition.
4, the enzyme that goes out: adopt 100 ℃, the 20min enzyme that goes out.
5, debitterize, decolour, take off flavor: adopt gac and composite decoloring agent (the gac yeast of 3g/L and cyclodextrin etc. mix) that enzymolysis solution is carried out debitterize, decolours, takes off flavor and handle respectively, relatively the effect of two kinds of methods.
6, filter: enzymolysis solution through debitterize, decolour, take off flavor and handle after, obtain clear liquid through 4000r/min centrifuging again.
7, ion-exchange: the ultrafiltrated of getting certain volume passes through 001*7 (732) strongly acidic styrene type cation exchange resin with the flow velocity of 8 times of column volume/h at normal temperatures, collect effluent liquid, again with the hydrolyzed solution behind the decationized Y sieve with the flow velocity of 8 times of column volume/h by 201*7 (717) strong basicity I type anionite-exchange resin, collect effluent liquid.
8, concentrate: use Rotary Evaporators, thickening temperature is 50 ℃, and evaporating solns is to thick.
9, ultrafiltration: select the tubular fibre material for use, the operating pressure of ultrafiltration apparatus is 28psi, and the membrane permeation flux is 9.98LHM, and the uf processing time is 40min, and feeding temperature is 29 ℃, and material liquid pH value is 6.7.
10, gel chromatography: the collection ultrafiltrated enters gel chromatography and carries out further separation and purification, and separating medium is SephadexG-15, and chromatographic column (1.6 * 60cm), column chromatography condition: applied sample amount: 1.5ml; Flow velocity: 0.8ml/min; Eluent: distilled water; Detect wavelength: 220nm.
11, measure the inhibiting rate of ACE:, carried out certain research and modification according to particular cases such as the size of reaction system, ethyl acetate extraction amount, centrifugation times with reference to (1995) improved methods such as Nakamura.Measure the half-inhibition concentration (IC of each component peaks respectively
50), promptly institute's test sample product reach 50% o'clock pairing sample concentration to the ACE inhibiting rate.
According to table 1 each reagent is joined in the test tube, in 37 ℃ of water-baths, react 30min, reaction finishes the back and adds 1moL/LHCI with termination reaction (sample c need add HCl in advance) at once, behind the static 5min, in each test tube, add ethyl acetate (cold) 2.0mL, centrifugal 10min (4000r/min) behind the vortex mixing 2min, draw the 1.5mL ethyl acetate in another test tube, put into baking oven, 120 ℃ of solvent flashing 30min, the cooling back adds deionized water 3mL, measures its light absorption value behind the static 15min of vortex mixing 30sec under 228nm.
The method (ul) of table 1ACE vitro detection inhibiting rate
| Medicine | Sample number | ||
| a | b | c | |
| HCL | 0 | 0 | 125 |
| ACE | 0 | 0 | 20 |
| HHL | 60 | 60 | 60 |
| Inhibitor | 40 | 0 | 40 |
| Borate buffer | 0 | 375 | 0 |
| 37 ℃ of water-bath preheating 4-5min | |||
| ACE | 20 | 20 | 0 |
| 37 ℃ of water-bath 30min | |||
| HCL | 125 | 125 | 0 |
Calculation formula:
Aa: the simultaneous absorbance of ACE and ACE inhibitor in reaction;
Ab: unconstrained dose absorbance in reaction;
The absorbance of the blank reaction of Ac:ACE and HHL.
12, lyophilize: high reactivity ACE constituents for suppressing is behind-80 ℃ of pre-freeze 8hr, and vacuum lyophilization 72hr promptly gets product.
Advantage of the present invention is: 1, the prepared blood pressure lowering peptide of the present invention is the small-molecular peptides of fish-skin albumen through producing behind the protease hydrolyzed, be easy to human body and digest and assimilate fast, the hyperpietic is played the step-down effect, the normotensive is played health-care effect, and have no side effect, safe; 2, raw material of the present invention is a tilapia fishskin albumen, is the waste of tilapia processing, and technical transform of the present invention provides a new way for effective utilization of tilapia waste; 3, craft science of the present invention is reasonable, and is simple to operate, with low cost, has stronger industrial implementation; 4, products obtained therefrom of the present invention can be used as medicine, protective foods, food, foodstuff additive, medicine and increases agent etc., has wide market application prospect.
Embodiment
Below in conjunction with example the present invention is described in further detail.
Case study on implementation:
Take by weighing the tilapia fishskin that 100.0008g rinses well, soak 1hr with the hydrochloric acid soln of 700ml 0.1mol/L and the sodium hydroxide solution of 0.1mol/L successively after the skimming treatment, distilled water wash is to neutrality, under 45 ℃ of conditions, distilled water constant temperature homogenate 12hr with 1000ml, suction filtration extracts supernatant liquor, be warming up to 50 ℃-55 ℃, regulating the pH value is 6.0, add 0.04671g papoid constant temperature enzymolysis 2hr, heating in water bath 20min under 100 ℃ of hot conditionss then, enzymolysis reaction, promptly get the fish-skin protein enzymatic hydrolyzate, the tilapia fishskin protein hydrolysis degree is 12.3%.
Adopt composite decoloring agent (the gac yeast of 3g/L and cyclodextrin etc. mix) that the fish-skin protein enzymatic hydrolyzate is carried out debitterize, decolours, takes off the flavor processing, supernatant liquor is collected in 4000r/min centrifuging.Flow velocity with 8 times of column volume/h under the normal temperature passes through 001*7 (732) Zeo-karb, collect effluent liquid, recording its nitrogen recovery is 95.40%, again with the hydrolyzed solution behind the decationized Y sieve with the flow velocity of 8 times of column volume/h by 201*7 (717) anionite-exchange resin, collect effluent liquid, record its nitrogen recovery and be 93.31% and ratio of desalinization be 93.15%.Effluent liquid carries out uf processing after concentrating, and the ultrafiltration apparatus operating pressure is 28psi, and feed temperature is 29 ℃, and material liquid pH is 6.7, and uf processing 40min obtains fishskin polypeptide liquid.
Fishskin polypeptide liquid is through gel chromatography separation, and separating medium is SephadexG-15, and the chromatographic column specification is 1.6 * 60cm.Column chromatography condition: applied sample amount: 1.5ml; Flow velocity: 0.8ml/min; Eluent: distilled water; Detect wavelength: 220nm.Obtain 8 components under this separation condition, at-80 ℃ of pre-freeze 8hr, vacuum lyophilization 72hr is product with high reactivity ACE constituents for suppressing F.The half-inhibition concentration of each component sees Table 2.
Half-inhibition concentration (the IC of each component of table 2
50)
| Component | A | B | C | D | E | F | G | H |
| IC 50(ug/ml) | 46.36 | 69.52 | 57.88 | 58.14 | 22.37 | 20.08 | 0 | 0 |
Claims (1)
1, a kind of preparation method who comes from the ace inhibitory peptide of fish-skin is characterized in that method steps is:
(1) pre-treatment: the fish-skin after the cleaning soaks 1hr with the hydrochloric acid soln of 0.1mol/L and the sodium hydroxide solution of 0.1mol/L successively after degreasing;
(2) water is carried: pretreated fish-skin is through washing to neutrality, and under 45 ℃ of conditions, behind the distilled water constant temperature homogenate 12hr with 10 times of volumes, suction filtration extracts supernatant liquor;
(3) enzymolysis:, adopt papoid and neutral protease to carry out enzymolysis, the relatively hydrolysis result of two kinds of enzymes, and definite optimum enzymolysis condition under certain condition;
(4) enzyme that goes out: adopt 100 ℃, the 20min enzyme that goes out;
(5) debitterize, decolour, take off flavor: adopt gac and composite decoloring agent that enzymolysis solution is carried out debitterize, decolours, takes off flavor and handle respectively, relatively the effect of two kinds of methods;
(6) filter: enzymolysis solution through debitterize, decolour, take off flavor and handle after, obtain clear liquid through 4000r/min centrifuging again;
(7) ion-exchange: the ultrafiltrated of getting certain volume passes through 732 strongly acidic styrene type cation exchange resins with the flow velocity of 8 times of column volume/h at normal temperatures, collect effluent liquid, again with the hydrolyzed solution behind the decationized Y sieve with the flow velocity of 8 times of column volume/h by 717 strong basicity I type anionite-exchange resin, collect effluent liquid;
(8) concentrate: use Rotary Evaporators, thickening temperature is 50 ℃, and evaporating solns is to thick;
(9) ultrafiltration: select the tubular fibre material for use, the operating pressure of ultrafiltration apparatus is 28psi, and the membrane permeation flux is 9.98LHM, and the uf processing time is 40min, and feeding temperature is 29 ℃, and material liquid pH value is 6.7;
(10) gel chromatography: the collection ultrafiltrated enters gel chromatography and carries out further separation and purification, and separating medium is SephadexG-15, and chromatographic column (1.6 * 60cm), column chromatography condition: applied sample amount: 1.5ml; Flow velocity: 0.8ml/min; Eluent: distilled water; Detect wavelength: 220nm;
(11) lyophilize: high reactivity ACE constituents for suppressing is behind-80 ℃ of pre-freeze 8hr, and vacuum lyophilization 72hr promptly gets product.
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| CN102251003A (en) * | 2011-06-28 | 2011-11-23 | 国家海洋局第三海洋研究所 | Preparation technique of marine-organism-derived antihypertensive peptides |
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| CN103267510A (en) * | 2013-05-31 | 2013-08-28 | 中国科学院长春光学精密机械与物理研究所 | Electric jacking device for photoelectric theodolite |
| CN103923963A (en) * | 2014-04-10 | 2014-07-16 | 江南大学 | Method for preparing fish skin collagen and ACE inhibitory peptide |
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| WO2014194530A1 (en) * | 2013-06-08 | 2014-12-11 | 广州世优生物科技有限公司 | Method for preparing ace inhibitory peptides from hairtail leftovers |
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| CN105274171A (en) * | 2015-11-13 | 2016-01-27 | 潘发全 | Method of preparing antioxidant peptides by hydrolyzing skin of tilapias using compound protease |
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| CN113508828A (en) * | 2021-07-08 | 2021-10-19 | 泉州师范学院 | Preparation method of mackerel antihypertensive active peptide and application of mackerel antihypertensive active peptide in bread |
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