CN100465284C - Functional mixed short peptide of peanut, and prepartion method - Google Patents
Functional mixed short peptide of peanut, and prepartion method Download PDFInfo
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- CN100465284C CN100465284C CNB2006101124793A CN200610112479A CN100465284C CN 100465284 C CN100465284 C CN 100465284C CN B2006101124793 A CNB2006101124793 A CN B2006101124793A CN 200610112479 A CN200610112479 A CN 200610112479A CN 100465284 C CN100465284 C CN 100465284C
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Abstract
This invention discloses a method for preparing functional mixed oligopeptides of peanut, which comprises: peptides more than 80 wt.%, ashes less than 8 wt.%, sugar less than 5 wt.%, weight loss after drying less than 7 wt.% and fat less than 5 wt.%. The content of oligopeptides with molecular weight lower than 1000 Da is higher than 60%. Trichloroacetic acid-nitrogen soluble index is higher than 99.5%. The functional mixed oligopeptides of peanut are prepared by: using powdery peanut proteins as the raw materials, hydrolyzing with enzymes and separating by membrane. Compared with powdery peanut proteins, the functional mixed oligopeptides have better solubility and higher stability. Besides, the functional mixed oligopeptides also have good antihypertensive and antioxidant effects, thus can be widely applied in such fields as pharmacy, daily chemicals and fermentation.
Description
Technical field
The present invention relates to biologically active peptides and preparation method thereof, particularly relate to the functional mixed short peptide and preparation method thereof of cultivating peanut.
Background technology
Main application at China's peanut is oily usefulness, and national peanut has 50% to be used to oil expression approximately, and along with the popularization of advanced milling process such as cold-press, aqua method, oil in the peanut and albumen can be utilized simultaneously.The development and use of China's Semen arachidis hypogaeae protein are started late, and the intensive processing technology is backward relatively, and product-mix is single, and is of low grade, and fabricated product lacks high in technological content deep processing, high-grade product still based on preliminary working.At present, the Semen arachidis hypogaeae protein product on the domestic market mainly is the powdery Semen arachidis hypogaeae protein, and its main application is as the basic material in the food-processing.Powdery Semen arachidis hypogaeae protein work in-process exists functional property and physiologically active is relatively poor, absorb shortcomings such as relatively poor, and it is imperative therefore to research and develop the Semen arachidis hypogaeae protein deep processed product with good function character and physiologically active.
Biologically active peptides (biologically active peptides or biopeptides) is meant the peptides that the vital movement to living organism is useful or have physiological action.Modern nutrient research shows: protein is in digestive tube under the digestive ferment effect, the hydrolysis end product is total free aminoacids and peptide, and being absorbed and used with complete form, but not former being absorbed of being thought of people with the total free aminoacids form by the small peptide that several amino-acid residues are formed.The contrary concentration gradient of little peptide is according to H
+Concentration or Ca
2+The active transport process of concentration has the dependent non-power consumption Na of pH
+, H
+Exchange system, little peptide movement system have that transport speed is fast, power consumption is low, it is saturated to be difficult for, and absorb the characteristics of uncontested property and inhibition between each peptide.
The approach of the production preparation of bioactive short peptide has three: the one, from natural organism, extract the various natural radioactivity peptide matters of itself inherent; The 2nd, the approach by protein degradation obtains biologically active peptides with various physiological functions; The 3rd, use synthetic method and prepare biologically active peptides.Exist biologically active peptides in the natural biological body, but it is higher to extract the biologically active peptides production cost from the natural biological body, and biologically active peptides content in vivo is generally very low, is difficult to realize large-scale production with various physiological functions; Synthesis method can be by the synthetic any bioactive peptide of people's wish, but cost height, side reaction reach the development that problem such as residual toxic compounds is restricting this technology more.
Summary of the invention
The purpose of this invention is to provide the functional mixed short peptide and preparation method thereof of cultivating peanut.
Peanut functional mixed short peptide provided by the present invention, the weight percentage of peptide is higher than 80%, ash oontent≤8%, sugared content≤5%, weight loss on drying≤7%, fat≤5%; Molecular weight is less than small peptide content 〉=60% of 1000Da; Trichoroacetic acid(TCA) nitrogen soluble index 〉=99.5%.
The preparation method of this peanut functional mixed short peptide comprises the steps:
1) raw materials pretreatment: with water dissolution, it is extremely alkaline with solubilising to regulate pH with alkali, the centrifuging and taking supernatant with peanut protein powder; Regulate supernatant liquor pH to acid with acid, centrifugal collecting precipitation;
2) enzyme is handled: will precipitate with water dissolution, and add Sumizyme MP and carry out enzymolysis, and temperature 55-60 ℃, time 90-120min, pH7.0-9.0, basic protein enzyme dosage are 2500-3500U/g albumen; Then, add compound protease and continue to handle, temperature 55-60 ℃, time 40-70min, pH6.0-7.0, conjugated protein enzyme dosage are 1500-2500U/g albumen;
3) enzyme-deactivating: the protein solution that enzyme is handled is warming up to 90-95 ℃, keeps 10-20min to make enzyme-deactivating, and the centrifuging and taking supernatant liquor is peanut functional mixed short peptide stoste
4) ultrafiltration: is the ultra-filtration membrane of 5000-3000Da with gained peanut functional mixed short peptide stoste by molecular weight cut-off, removes the macromole segment, obtains peanut functional mixed short peptide liquid;
5) desalination, drying: gained peanut functional mixed short peptide liquid is passed through H continuously
+Type Zeo-karb and OH
-Type anionite-exchange resin, effluent liquid obtains described peanut functional mixed short peptide through concentrated, dry.
Wherein, the particle diameter of step 1) peanut protein powder is 60-80 orders.The weight ratio of peanut protein powder and water is 1:5-20, regulates pH to 8-9 with alkali lye; When regulating supernatant liquor pH to acidity with acid, pH is 4-5.Step 5) is 10-15 times of column volume/h by the flow velocity of ion exchange resin.
The present invention is a raw material with the powdery Semen arachidis hypogaeae protein, by enzymic hydrolysis, technology such as membrane sepn, prepare the peanut functional mixed short peptide, compare with the powdery Semen arachidis hypogaeae protein, have good solubility energy and stability, as: the viscosity of powdery Semen arachidis hypogaeae protein increases with concentration and raises rapidly, but the functional small peptide of peanut still keeps flowability under high density; Aspect solvability, the powdery Semen arachidis hypogaeae protein can form precipitation in its iso-electric point, and the functional small peptide of peanut still can keep dissolved state; Along with system temperature raises, thermally denature can take place and precipitate in the powdery Semen arachidis hypogaeae protein, and the functional small peptide of peanut then still keeps dissolved state.And, the inventor proves by experiment, peanut functional mixed short peptide of the present invention has the various biological function, as hypertension and anti-oxidant etc., it can be developed to relevant functional food such as antihypertensive beverage, hypertension pill, active peptide powder etc., can be widely used in industries such as medicine, daily use chemicals, fermentation.
Embodiment
The preparation of embodiment 1, peanut functional mixed short peptide
The preparation flow of peanut functional mixed short peptide of the present invention is as follows:
Refining → desalination → vacuum concentration → drying that enzyme → centrifugal → ultrafiltration is handled → gone out to raw materials pretreatment → enzyme.
Detailed process is:
1. raw materials pretreatment: the cold press peanut meal is made peanut protein powder through pulverizing, cross the 60-80 mesh sieve, peanut protein powder is further purified again:
Peanut protein powder → water-soluble (material water weight ratio 1:10) → alkali carry (regulate pH=8.5 with NaOH, 25 ℃, 25min) → centrifugal (800g, 5min) → supernatant liquid → acid heavy (with hydrochloric acid adjusting pH=4.5) → centrifugal (4200g, 15min) → collecting precipitation
2. enzyme is handled: will precipitate the Semen arachidis hypogaeae protein solution of preparation 4%, and carry out enzymolysis with Sumizyme MP earlier, condition is: hydrolysis temperature 55-60 ℃, hydrolysis time 90-120min, pH7.0-9.0, at the bottom of the enzyme than 2500-3500U/g albumen; Then, add compound protease and continue to handle, condition is hydrolysis temperature 55-60 ℃, hydrolysis time 40-70min, pH6.0-7.0, at the bottom of the enzyme than 1500-2500U/g albumen.
3. enzyme-deactivating: be rapidly heated to 90-95 ℃, keep 10-20min to make enzyme-deactivating, the centrifugal 20-30min of 4200g afterwards, solid-liquid separation, supernatant liquor be peanut functional mixed short peptide stoste.
4. ultrafiltration is refining: making the functional small peptide of peanut mix stoste is the ultra-filtration membrane of 5000Da by molecular weight cut-off, removes the macromole segment in the peanut functional mixed short peptide stoste, obtains peanut functional mixed short peptide liquid.
5. desalination: deionization exchange resin immersion treatment in water was adorned post after 24 hours, with 7.5% hydrochloric acid or 10%NaOH it was handled respectively then, was converted into H
+Type Zeo-karb and OH
-Type anionite-exchange resin, water cleans to subacidity or slight alkalinity stand-by again.
With the functional small peptide liquid of gained peanut, pass through H with the flow velocity of 10 times of column volume/h
+The type Zeo-karb removes positively charged ion, stops application of sample when treating the effluent liquid pH=4.0 left and right sides, afterwards this effluent liquid is passed through OH with same flow velocity
-Type anionite-exchange resin removes negatively charged ion, stops application of sample when effluent liquid is slightly acidic.
6. concentrated, dry: to solid content 35-40%, dry powder is made in spray-dried or lyophilize by vacuum concentration, product yield 〉=50% (in protein content).
Gained peanut functional mixed short peptide dry powder is a kind of white or micro-yellow powder, and peptide content is 85%, ash content 5%, sugared content 5%, weight loss on drying 6%, fat 4%; Trichoroacetic acid(TCA) nitrogen soluble index (TCA-NSI) is 99.7%.The molecular weight of gained mixed short peptide is less than 5000, and wherein molecular weight is less than small peptide content 〉=60% of 1000Da.
Solubility experiment shows that this peanut functional mixed short peptide can both be water-soluble under all pH; The thermostability experiment shows that product of the present invention is very stable to heat, and system temperature reaches 100 ℃ can not produce precipitation yet.
The functional experiment of embodiment 2, peanut functional mixed short peptide
1. the mensuration of antihypertensive active
100 μ l samples are added in the 100 μ l 0.05M borate buffer solutions, and pH of buffer is 8.3, comprising 0.3M NaCl, 25mU angiotensin-converting enzyme (ACE), 37 ℃ of preheating 10min; Add 150 μ l hippuryl histidyl-leucines (HHL) and start reaction, 37 ℃ of reaction 1h add 1M hydrochloric acid 250 μ l termination reactions; Add 1.5ml ethyl acetate extraction urobenzoic acid afterwards, carry out after whirlpool mixes centrifugal (1800g, 15min); Draw the 1ml ethyl acetate layer and move in another test tube, oven dry is dissolved in after the cooling in the 3ml deionized water again, and 228nm measures its light absorption value down,
ACE suppresses active (%)=(A
a-A
b)/(A
a-A
c) * 100%
A wherein
a: the optical density(OD) when not having inhibitor
A
b: the optical density(OD) when having inhibitor and enzyme
A
c: the optical density(OD) when inhibitor and enzyme do not exist
2. remove ultra-oxygen anion free radical
In a series of test tube, add 9ml0.05M, the Tris-Hcl damping fluid of pH=8.2, add sample solution 100 μ l, blank group adds the distilled water with volume, the 0.045M pyrogallol (with the 0.01MHCL preparation) that adds 100 μ l again, whirlpool decollator concussion three minutes adds 100 μ l, 10% xitix stopped reaction, surveys light absorption value immediately at the 325nm place.
Remove ability (SA)=(A of free radical
0-A
S)/A
0* 100%
A wherein
0Be blank sample measured value, AS is the sample determination value
3. remove hydroxy radical qiao
In test tube, add 0.5ml9.1mM Whitfield's ointment-ethanolic soln successively, the sample of 0.5ml, 0.5ml9mMFe
2+Solution, 3.5ml distilled water adds 5ml88mM H at last
2O
2, after colour developing shakes up, under 510nm, measure and remove activity.
Removing ability=(A
0-A
s)/A0*100%
A wherein
0(replacing sample with sample solvent) is blank sample measured value, A
sBe the sample determination value
4. remove hexichol for bitter taste acyl (DPPH) free radical
1.5ml sample is added into 1.5ml, in the DPPH95% ethanolic soln of 0.1mM, at room temperature places 30min after the mixture concussion, 517nm measures absorbancy.
P＝(1-(A
1-A
2)/A
3)*100％
A wherein
1: the DPPH+ sample
A
2: 95% ethanol+sample
A
3: DPPH+ distilled water
5. anti-oxidant
The phosphate buffered saline buffer that adds 1.5ml0.15M (pH7.0) in the 10ml tool plug glass test tube adds 100 μ l samples respectively, the Fecl of 100 μ l 50mM linolic acid-ethanolic solns and 50 μ l 50mM
2-EDTA solution adopts whirlpool decollator concussion three minutes, in 50 ℃ of dark place water bath heat preservation for some time.
3ml75% ethanol, the above-mentioned mixed solution of 100 μ l, the Fec l of 100 μ l1M
21MHCL solution, 100 μ l30%KSCN adopt the concussion of whirlpool decollator after three minutes, measure solution absorbency at 480nm immediately.
AA＝(A
0-A
S)/A
0*100％
Wherein anti-oxidant barren absorbancy is A
0, adding antioxidant is that absorbancy is A
S
The functionally active detected result of gained peanut functional mixed short peptide is as follows:
Antihypertensive active: it is 50% that 0.4mg/ml sample ACE suppresses activity;
Remove ultra-oxygen anion free radical: 25mg/ml sample clearance rate is 33.83%;
Remove hydroxy radical qiao: 15mg/ml sample clearance rate is 64.77%;
Remove the DPPH free radical: 10mg/ml sample clearance rate is 71.6%;
Anti-oxidant: 25mg/ml sample anti-oxidant activity is 42.99%.
Claims (5)
1, the functional mixed short peptide of cultivating peanut, it is characterized in that: the weight percentage of peptide is higher than 80% in the described mixed short peptide, ash oontent≤8%, sugared content≤5%, weight loss on drying≤7%, fat≤5%; Molecular weight is less than small peptide content 〉=60% of 1000Da; Trichoroacetic acid(TCA) nitrogen soluble index 〉=99.5%; Described peanut functional mixed short peptide prepares according to the following procedure:
1) raw materials pretreatment: peanut protein powder with water dissolution, is added alkaline extraction albumen, the centrifuging and taking supernatant; With Acid precipitation supernatant, centrifugal collecting precipitation;
2) enzyme is handled: will precipitate with water dissolution, and add Sumizyme MP and carry out enzymolysis, and temperature 55-60 ℃, time 90-120min, pH7.0-9.0, basic protein enzyme dosage are 2500-3500U/g albumen; Then, add compound protease and continue to handle, temperature 55-60 ℃, time 40-70min, pH6.0-7.0, conjugated protein enzyme dosage are 1500-2500U/g albumen;
3) enzyme-deactivating: the protein solution that enzyme is handled is warming up to 90-95 ℃, keeps 10-20min to make enzyme-deactivating, and the centrifuging and taking supernatant liquor is peanut functional mixed short peptide stoste;
4) ultrafiltration: is the ultra-filtration membrane of 5000-3000Da with peanut functional mixed short peptide stoste by molecular weight cut-off, removes macromolecular gluco, obtains peanut functional mixed short peptide liquid;
5) desalination, drying: peanut functional mixed short peptide liquid is passed through H continuously
+Type Zeo-karb and OH
-Type anionite-exchange resin, effluent liquid obtains described peanut functional mixed short peptide through concentrated, dry.
2, the preparation method of the described peanut functional mixed short peptide of claim 1 comprises the steps:
1) raw materials pretreatment: peanut protein powder with water dissolution, is added alkaline extraction albumen, the centrifuging and taking supernatant; Regulate supernatant liquor pH to acid with acid, centrifugal collecting precipitation;
2) enzyme is handled: will precipitate with water dissolution, and add Sumizyme MP and carry out enzymolysis, and temperature 55-60 ℃, time 90-120min, pH7.0-9.0, basic protein enzyme dosage are 2500-3500U/g albumen; Then, add compound protease and continue to handle, temperature 55-60 ℃, time 40-70min, pH6.0-7.0, conjugated protein enzyme dosage are 1500-2500U/g albumen;
3) enzyme-deactivating: the protein solution that enzyme is handled is warming up to 90-95 ℃, keeps 10-20min to make enzyme-deactivating, and the centrifuging and taking supernatant liquor is peanut functional mixed short peptide stoste;
4) ultrafiltration: is the ultra-filtration membrane of 5000-3000Da with gained peanut functional mixed short peptide stoste by molecular weight cut-off, removes macromolecular gluco, obtains peanut functional mixed short peptide liquid;
5) desalination, drying: gained peanut functional mixed short peptide liquid is passed through H continuously
+Type Zeo-karb and OH
-Type anionite-exchange resin, effluent liquid obtains described peanut functional mixed short peptide through concentrated, dry.
3, preparation method according to claim 2 is characterized in that: the particle diameter of step 1) peanut protein powder is 60-80 orders.
4, preparation method according to claim 2 is characterized in that: in the step 1), the weight ratio of peanut protein powder and water is 1:5-20, regulates pH to 8-9 with alkali lye; When regulating supernatant liquor pH to acidity with acid, pH is 4-5.
5, preparation method according to claim 2 is characterized in that: step 5) is through H
+Type Zeo-karb and OH
-The flow velocity of type anionite-exchange resin is 10-15 times of column volume/h.
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| CN100465284C true CN100465284C (en) | 2009-03-04 |
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| CN101455403B (en) * | 2008-12-29 | 2012-09-12 | 陕西天宝大豆食品技术研究所 | Peanut peptide nutrient food and preparation method thereof |
| CN101979653A (en) * | 2010-10-19 | 2011-02-23 | 山东省农业科学院农产品研究所 | Peanut antihypertensive peptide and preparation method thereof |
| CN101965898B (en) * | 2010-11-11 | 2012-06-27 | 湖北远成药业有限公司 | Method for extracting peanut peptide |
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| CN102174628B (en) * | 2011-01-12 | 2013-12-25 | 武汉百信正源生物技术工程有限公司 | Preparation method of peanut bioactive peptides |
| CN102150740A (en) * | 2011-04-27 | 2011-08-17 | 山东省花生研究所 | Method for preparing peanut antioxidant peptides |
| CN102250999A (en) * | 2011-06-01 | 2011-11-23 | 山东省花生研究所 | Separating and purifying method of peanut bioactive peptide |
| CN102251001B (en) * | 2011-06-22 | 2013-10-30 | 华南理工大学 | Preparation method of vegetable protein antioxidant |
| CN102239954B (en) * | 2011-07-01 | 2013-03-06 | 华南理工大学 | Preparation and decolouring methods of peanut proteins |
| CN102232465B (en) * | 2011-08-16 | 2013-01-09 | 山东省花生研究所 | Process for preparing peanut antioxidant peptide |
| CN102273543B (en) * | 2011-08-16 | 2012-10-10 | 山东省花生研究所 | Method for preparing peanut antioxidant peptide through ultrasonic-assisted enzymolysis |
| CN102334588B (en) * | 2011-08-26 | 2013-04-03 | 山东省花生研究所 | Preparation method for enzyme-modified peanut protein |
| CN106579329A (en) * | 2016-12-14 | 2017-04-26 | 翟珺 | Polypeptide compound antioxidant |
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