CN101003828B - Method of producing bioactive peptide for anti high blood pressure by using protease of Switzerland lactobacillus to hydrolyze lactoprotein - Google Patents
Method of producing bioactive peptide for anti high blood pressure by using protease of Switzerland lactobacillus to hydrolyze lactoprotein Download PDFInfo
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- CN101003828B CN101003828B CN200710019430A CN200710019430A CN101003828B CN 101003828 B CN101003828 B CN 101003828B CN 200710019430 A CN200710019430 A CN 200710019430A CN 200710019430 A CN200710019430 A CN 200710019430A CN 101003828 B CN101003828 B CN 101003828B
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Abstract
This invention relates to a method for producing anti-hypertension active peptide by hydrolyzing lactalbumin with Lactobacillus helveticus protease. The method comprises: (1) pulverizing Lactobacillushelveticus ATCC15019, centrifuging, salting out, performing three-step column chromatography, and separating to obtain Lactobacillus helveticus ATCC15019 protease Q; (2) hydrolyzing lactalbumin withLactobacillus helveticus ATCC15019 protease Q; (3) performing ultrafine filtration, freeze-drying, performing Sephadex G-25 ion exchange column chromatography, and performing mu-Bondasphere C18, YMC-Park ODS-AP-303, YSK-Octadecyl 4PW and YMC-Pack ODS-100S reverse phase liquid phase chromatographic column chromatography to obtain polypeptides IPP and VPP. The method can obtain IPP and VPP at the same time, and is easier to control than the present fermentation method.
Description
Technical field
The present invention relates to Food science and biological technical field, be specifically related to the method that a kind of lactobacterium helveticus protease hydrolysis milk-protein is produced antihypertensive active peptide.
Technical background
Blood pressure lowering peptide is called angiotensin-converting enzyme (Angiotensin-I-converting Enzyme is called for short ACE) inhibiting peptide again, is the polypeptide short chain material that an isolated class has the effect that significantly brings high blood pressure down from food proteins.From the source, can be divided into milk-protein (comprising casein, whey-protein), leavened food, animal proteinum, vegetable-protein and natural A C E inhibiting peptide.These blood pressure lowering peptides that derive from food are usually by proteolytic enzyme protein hydrolysate and obtaining under mild conditions, the edible safety height, its jointly outstanding advantage is only the hyperpietic to be played hypotensive effect, and the normotensive is not had hypotensive effect, thereby does not have the generation of step-down over-education phenomenon.And the antihypertensive drugs of chemosynthesis (as captopril etc.), though it is very obvious to treat hypertensive effect, it is to the toxic side effect of kidney, and occurs symptoms such as ypotension, dry cough after taking medicine, it is worried that people are produced its security.Essential hypertension causes coronary heart disease easily, myocardial infarction, and therefore cerebral apoplexy and renal failure etc. become a very serious social public health problem.
In the numerous biologically active peptides of function, blood pressure lowering peptide claims to become the focus of bioactive peptide research because of its buck functionality that has no side effect.Isolating blood pressure lowering peptide from natural food albumen, though antihypertensive effect is so strong not as synthetic drugs, it has security, and also often has functions such as immunomodulatory and fat-reducing except that hypotensive.Find and isolate more short chain blood pressure lowering peptide from natural food albumen, one side provides the foundation for follow-up hypotensive activity detects, and the while also provides direction by the approach prevention and the alleviation hypertension of protective foods on the other hand.
Aspect milk protein, people such as Mullldly are by C18 solid phase extractions beta-lactoglobulin tryptic digestive juice, obtain peptide material with the fine wash-out of 20-25% second, afterwards the solid phase extractions thing is carried out mass spectroscopy, contain β-lgf segment (142-148), adopt 3KDa and 1KDa molecular weight mwco membrane can make ace inhibitory peptide rich long-pending.Maruyama etc. go out to have ACE from the separation and purification of bovine casein trypsin hydrolyzing thing and suppress active dodecapeptide, seven peptides, six peptides and pentapeptide, carry out SHR experiment afterwards, and blood pressure obviously reduces, and blood pressure and control group differ about 14mmHg around the.People such as Abubabar separate 6 peptides with antihypertensive active of acquisition by RP-HPLC from the Digestive system of the cheese whey protein of proteolytic enzyme-K, IPA wherein (Ile-Pro-Ala) has very strong activity.People such as Saito separate from 7 kinds of cheese, obtain 4 and have ACE and suppress active peptide, and SHR is had hypotensive effect.
Summary of the invention
The purpose of this invention is to provide a kind of new method for preparing antihypertensive active peptide.
Method of the present invention may further comprise the steps:
(1) separation and purification of lactobacterium helveticus (Lactobacillus helveticus) ATCC15019 proteolytic enzyme Q: with centrifugal behind lactobacillus helveticus atcc-15019 bacterial cell disruptions of cultivating, collect its supernatant liquor, supernatant liquor is centrifugal after sulfate of ammoniac is saltoutd, taking precipitate is dissolved in distilled water, separate with DEAE Sephadex A-25 chromatography column by Sephadex G-100, Sepharose CL-6B again, collect and to produce the active elution peak of anti-ACE by lactoalbumin hydrolysate, obtain lactobacillus helveticus atcc-15019 proteolytic enzyme Q;
(2) proteolytic enzyme Q lactoalbumin hydrolysate: with lactobacillus helveticus atcc-15019 proteolytic enzyme Q lactoalbumin hydrolysates;
(3) separation and purification of antihypertensive peptide:
A, elder generation are that the ceramic membrane of 10nm carries out ultrafiltration to remove macromolecular substance to milk protein hydrolysate with the aperture, collect ultrafiltrated, lyophilize;
B, above-mentioned lyophilized powder is dissolved in aquae destillata, centrifugal, collect supernatant liquor, behind Sephadex G-25 ion exchange chromatography, again through μ Bondasphere C
18(3.9 * 150mm), YMC-Pack ODS-AP-303 (4.6 * 250mm), YSK-Octadecyl 4PW (3.9 * 150mm) and YMC-Pack ODS-100S (3.9 * 150mm) four step reversed-phase liquid chromatographies separate, collect and to produce the active elution peak of anti-ACE by lactoalbumin hydrolysate, make polypeptide ILE-PRO-PRO (Ile-Pro-Pro, IPP) and VAL-PRO-PRO (Val-Pro-Pro, VPP).
The said hydrolysising condition with lactobacillus helveticus atcc-15019 proteolytic enzyme Q lactoalbumin hydrolysates of above-mentioned steps (2) is preferred: milk-protein liquid initial pH value is 6.25-6.80, and proteolytic enzyme Q addition 0.10-0.20mg/mL is at 40 ℃ of following hydrolysis 2-4h.
In aforesaid method in the mentioned column chromatography for separation and reversed-phase liquid chromatography sepn process, said energy lactoalbumin hydrolysate produce the active wash-out honeybee of anti-ACE, difference because of the processing condition of concrete operations, difference as flow velocity, the time that can make its appearance is difference to some extent, but this is can be by learning in conjunction with conventional lactoalbumin hydrolysate and inhibition ACE activity test to those skilled in the art.
Through polypeptide IPP and the VPP that aforesaid method makes, has the active and antihypertensive activity of remarkable inhibition ACE; It suppresses the active IC of ACE
50Be respectively 5.15 and 9.13 μ M, irritate stomach with 1.80mg/kg and 3.60mg/kg dosage to the source property sent out hypertension mouse respectively, the maximum reducing value reaches 29 and 25mmHg respectively.
The present invention compares with existing method, have the following advantages: (1) can produce simultaneously with lactobacillus helveticus atcc-15019 proteolytic enzyme Q lactoalbumin hydrolysates has strong active polypeptide IPP of antihypertensive and VPP, and can not obtain IPP and VPP simultaneously with other method enzymolysis; (2) produce antihypertensive peptide with lactobacillus helveticus atcc-15019 proteolytic enzyme Q directionally hydrolyzing milk-proteins and produce the easier control of antihypertensive peptide, be convenient to produce in batches than existing fermentation method.
Description of drawings
Fig. 1 is IPP and VPP reversed phase chromatography separation figure (a-μ Bondasphere C
18, b-ODS-AP-303, c-YSK-Octadecyl 4PW, d-YMC-Pack ODS-100S; I peak VPP, II peak IPP).
Fig. 2 be the systolic pressure that the hypertension mouse is irritated stomach IPP and VPP change (●-IPP ,-◇-VPP)
Embodiment
Employed in the present invention term unless other explanation is arranged, generally has the implication of those of ordinary skills' common sense.
Below in conjunction with specific embodiment, and comparable data is described the present invention in further detail.Should be understood that these embodiment just in order to demonstrate the invention, but not limit the scope of the invention by any way.
In following embodiment, various processes of Xiang Ximiaoshuing and method are not ordinary methods as known in the art.The source of agents useful for same, trade(brand)name and be necessary to list its moiety person indicate when occurring first that all used thereafter identical reagent if no special instructions, and is all identical with the content of indicating first.
Embodiment 1:
The bioactive peptide preparation
(1) lactobacillus helveticus atcc-15019 is seeded in 4 liters of MRS (yeast powders of 0.8%, 1.2% peptone and 1.2% glucose) in the substratum, cultivated 22 hours down at 37 ℃, 8000rpm * 10min centrifugation gets somatic cells mud, somatic cells repeatedly with the centrifugal somatic cells that gets of aquae destillata flushing, is scattered in somatic cells in the damping fluid that pH is 6.8-7.0 200W * 10min ultrasonic disruption again, solution after the fragmentation is centrifugal through 4800rpm * 30min, collects its supernatant liquor.Supernatant liquor is saltoutd through sulfate of ammoniac, 6000rpm * 15min centrifugal collecting precipitation, throw out is dissolved in the distilled water, through Sephadex G-100 (elutriant is the sodium phosphate buffer of 0.04M, and flow velocity 1.0mL/min detects wavelength 280nm) chromatography, collect each elution peak respectively, to be used for lactoalbumin hydrolysate (pH is 6.8-7.0,40 ℃ of following hydrolysis 4h), hydrolyzed solution is used to suppress the ACE activity test; After the energy lactoalbumin hydrolysate produces the active elution peak of anti-ACE (elutriant between the 155-175min) lyophilize, be dissolved in the 0.05M tris-HCI buffer (Tris-HCl) of pH7.5, with aperture is the filtering membrane filtration of 0.2 μ m, (elutriant is the 0.05MTris-HCl damping fluid of pH7.5 to filtered liquid through Sepharose CL-6B, flow velocity 1.0mL/min, detect wavelength 280nm) chromatography, collect and to produce the active elution peak of anti-ACE (elutriant between the 181-195min) by lactoalbumin hydrolysate, after the lyophilize, the phosphoric acid buffer that is dissolved in 0.02MpH7.5 is molten, with aperture is the filtering membrane filtration of 0.2 μ m, (elutriant is that the phosphoric acid buffer of 0.02MpH7.5 is molten to filtered liquid through DEAE Sephadex A-25, flow velocity 1.0mL/min, detect wavelength 280nm) gel filtration chromatography, collect and can produce the active elution peak of anti-ACE (elutriant between the 176-187min) by lactoalbumin hydrolysate, lyophilize makes lactobacillus helveticus atcc-15019 proteolytic enzyme Q.
(2) get cow's milk, 6000rpm * 10min centrifugal degreasing, skimming milk adjusts to 6.60 at 90 ℃ of sterilization 15min with its pH, be cooled to 40 ℃ after, the dosage of pressing 0.12mg/mL adds proteolytic enzyme Q, at 40 ℃ of following hydrolysis 4h, hydrolyzed solution;
(3) be that the ceramic membrane of 10nm carries out ultrafiltration removing macromolecular substance to newborn hydrolyzate with the aperture, collect ultrafiltrated, lyophilize; Again the above-mentioned lyophilized powder that obtains is dissolved in aquae destillata, 5000rpm * 15min is centrifugal, collects supernatant liquor, and (elutriant is the 0.30mol/LNH of pH9.0 through Sephadex G-25 gel chromatography
4AC, flow velocity is 1mL/min, the detection wavelength is 220nm), collect and to produce the active elution peak of anti-ACE (elutriant between the 56-64min) by lactoalbumin hydrolysate, after the lyophilize, get antihypertensive active peptide IPP and VPP through following anti-phase high pressure liquid chromatography separation and purification of four steps again: at first, by μ Bondasphere C
18(3.9 * 150mm) chromatographic columns are separated, elutriant A is an acetonitrile: water: three fluoroacetic acid (100: 900: 1, V/V), elutriant B is an acetonitrile: water: three fluoroacetic acid (900: 100: 1, V/V), adopt linear gradient elution method, in 0～40min elution time, B liquid concentration rises to 45% from 0%, in 41～70min elution time, B liquid concentration rises to 75% from 45%, in 71～90min elution time, B liquid concentration rises to 100% from 75%, the flow velocity of each valency section elutriant is 1.0mL/min, and the detection wavelength is 220nm, collects to produce the active elution peak of anti-ACE (elutriant between the 21-26min) by lactoalbumin hydrolysate, lyophilize: second step, above-mentioned lyophilized powder is dissolved in the A elutriant, and (4.6 * 250mm) chromatographic columns are separated, elutriant by YMC-Pack ODS-AP-303, gradient, the eluent flow rate and all same the first step of detection wavelength, collect and to produce the active elution peak of anti-ACE (elutriant between the 24-33min), lyophilize by lactoalbumin hydrolysate; The 3rd step, above-mentioned lyophilized powder is dissolved in the A elutriant, (3.9 * 150mm) chromatographic columns are separated through YSK-Octadecyl 4PW again, elutriant, gradient, eluent flow rate and all same the first step of detection wavelength, collect and to produce the active elution peak of anti-ACE (elutriant between the 24-29min), lyophilize by lactoalbumin hydrolysate; The 4th step was dissolved in the A elutriant with above-mentioned lyophilized powder, and (3.9 * 150mm) chromatographic columns are separated through YMC-Pack ODS-100S, elutriant A is an acetonitrile: water: trifluoroacetic acid (100: 900: 1, V/V), elutriant B is an acetonitrile: water: and trifluoroacetic acid (900: 100: 1, V/V); B liquid gradient is as follows, in 0～45min elution time, concentration rises to 40% from 0%, in 46～75min elution time, concentration rises to 70% from 41%, in 76～90min elution time, concentration rises to 100% from 71%, eluent flow rate is 1.0mL/min, the detection wavelength is 220nm, collect and can produce the active elution peak of anti-ACE (elutriant between 20-22min and the 23-25min) by lactoalbumin hydrolysate, lyophilize makes and has remarkable inhibitions ACE activity and active polypeptide VPP of antihypertensive and IPP.
Above-mentioned VPP that makes and IPP are carried out following experiment, verify that it suppresses the active and antihypertensive activity of ACE.
Suppress the ACE activity experiment:The method of employing Cushman etc.Hip-His-Leu is made into the solution of 5.0mM with the 0.1M borate buffer solution (pH8.3) that contains 0.3M NaCl.In the 10mL test tube, add the 5mM Hip-His-Leu solution of 200 μ L and the hydrolyzed solution that contains polypeptide of 80 μ the L polypeptide solution of distilled water (or be dissolved in) respectively, after being incubated 3 minutes under 37 ℃, adding 20 μ L ACE solution again (is dissolved in the distilled water, vigor is 0.1 μ/mL), be incubated 30 minutes down at 37 ℃ behind the mixing, the hydrochloric acid soln of 1.0N that adds 250 μ L again is with termination reaction, add the 1.7mL vinyl acetic monomer again, after 15 seconds kinds are vibrated mixing, left standstill 5 minutes, with the vinyl acetic monomer layer of pipette, extract 1.0mL, after the vacuum lyophilization, add 1.0mL distilled water, behind the mixing in 228nm place mensuration absorbancy.Under these conditions, the ACE activity (IC of inhibition 50%
50) be an activity unit of sample.
ACE inhibiting rate=[(B-A)/(B-C)] * 100%
Wherein A is the hydrolyzed solution that the contains polypeptide polypeptide solution of distilled water (or be dissolved in) and ACE solution absorbency; B is not for containing the hydrolyzed solution polypeptide solution of distilled water (or the be dissolved in) sample of polypeptide, but contains the ACE solution absorbency; C is for containing distilled water, but do not contain the ACE solution absorbency.
Empirical tests, IPP and VPP suppress the active IC of ACE
50Be respectively 5.15 and 9.13 μ M.
The antihypertensive activity experiment:Essential hypertension mouse (buying in Chinese Academy of Sciences Shanghai Experimental Animal Center Shanghai Si Laike Company of Animals Ltd.) is divided into following three groups at random by body weight: control group, IPP1.80 mg/kg body weight/day, VPP3.60 mg/kg body weight/day dosage group, every group 10 (each 5 of male and female), single cage is raised, ad lib and drinking-water, polypeptide according to dosage is dissolved in the phosphoric acid buffer of 0.2mmol/L (pH7.2), irritated stomach 3 days, only irritate the long-pending 1.0mL/ of being of body of stomach, once a day, continuous irrigation stomach 3 days, each stomach of irritating finishes back 2,4,6,8,10,12 and 24h, measure caudal artery systolic pressure (the Systolic blood pressure of essential hypertension mouse respectively, SBP), press the method for Furushiro etc., before measuring systolic pressure, mouse is incubated 5min measure again under 32 ± 5 ℃ condition, repeat to survey 3 times at every turn, be averaged clay.The result as shown in Figure 2, the maximum reducing value reaches 29 and 25mmHg respectively.
Claims (1)
1. a lactobacterium helveticus protease hydrolysis milk-protein is produced the method for antihypertensive active peptide, may further comprise the steps:
(1) separation and purification of lactobacterium helveticus (Lactobacillus helveticus) ATCC15019 proteolytic enzyme Q: with centrifugal behind lactobacillus helveticus atcc-15019 bacterial cell disruptions of cultivating, collect its supernatant liquor, supernatant liquor is centrifugal after sulfate of ammoniac is saltoutd, taking precipitate is dissolved in distilled water, separate with DEAE Sephadex A-25 chromatography column by Sephadex G-100, Sepharose CL-6B again, collect the elution peak that the energy lactoalbumin hydrolysate produces the antiangiotensin invertase activity, obtain lactobacillus helveticus atcc-15019 proteolytic enzyme Q;
(2) proteolytic enzyme Q lactoalbumin hydrolysate: with lactobacillus helveticus atcc-15019 proteolytic enzyme Q lactoalbumin hydrolysates; Hydrolysising condition is: milk-protein liquid initial pH value is 6.25-6.80, and proteolytic enzyme Q addition 0.10-0.20mg/mL is at 40 ℃ of following hydrolysis 2-4h;
(3) separation and purification of antihypertensive peptide:
A, elder generation are that the ceramic membrane of 10nm carries out ultrafiltration to remove macromolecular substance to milk protein hydrolysate with the aperture, collect ultrafiltrated, lyophilize;
B, above-mentioned lyophilized powder is dissolved in aquae destillata, centrifugal, collect supernatant liquor, behind Sephadex G-25 ion exchange chromatography, separate through following four step reversed-phase liquid chromatographies again,
The first step: μ Bondasphere C
183.9 * 150mm chromatographic column is separated, elutriant A is 100: 900: 1 a acetonitrile of volume ratio, water, three fluoroacetic acid mixed solutions, elutriant B is 900: 100: 1 a acetonitrile of volume ratio, water, three fluoroacetic acid mixed solutions, adopt linear gradient elution method, in 0～40min elution time, B liquid concentration rises to 45% from 0%, in 41～70min elution time, B liquid concentration rises to 75% from 45%, and in 71～90min elution time, B liquid concentration rises to 100% from 75%, the flow velocity of each stepwise elution liquid is 1.0mL/min, the detection wavelength is 220nm, collects the elutriant between the 21-26min, lyophilize;
Second step, the previous step lyophilized powder is dissolved in elutriant A, separates, elutriant, gradient, eluent flow rate and all same the first step of detection wavelength by YMC-Pack ODS-AP-303,4.6 * 250mm chromatographic column, collect the elutriant between the 24-33min, lyophilize;
The 3rd step, the previous step lyophilized powder is dissolved in elutriant A, separates through YSK-Octadecyl 4PW 3.9 * 150mm chromatographic column again, elutriant, gradient, eluent flow rate and all same the first step of detection wavelength, collect the elutriant between the 24-29min, lyophilize;
The 4th step, the previous step lyophilized powder is dissolved in elutriant A, separate through YMC-Pack ODS-100S 3.9 * 150mm chromatographic column, elutriant A is 100: 900: 1 acetonitrile of volume ratio, water, trifluoroacetic acid mixed solution, and elutriant B is 900: 100: 1 acetonitriles of volume ratio, water, trifluoroacetic acid mixed solution; B liquid gradient is as follows, in 0～45min elution time, concentration rises to 40% from 0%, and in 46～75min elution time, concentration rises to 70% from 41%, in 76～90min elution time, concentration rises to 100% from 71%, and eluent flow rate is 1.0mL/min, and the detection wavelength is 220nm, collect the elutriant lyophilize between 20-22min and the 23-25min, get polypeptide ILE-PRO-PRO and VAL-PRO-PRO.
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| CN102816822A (en) * | 2012-09-13 | 2012-12-12 | 东北农业大学 | Lactalbumin cholesterol-reducing peptide and preparation method thereof |
| CN103146674A (en) * | 2013-03-15 | 2013-06-12 | 南京师范大学 | Method for synergetically immobilizing swiss lactobacillus protease by sodium alga acid-glutaraldehyde |
| CN104342473A (en) * | 2013-08-06 | 2015-02-11 | 北京市农林科学院 | Preparation and purification method of amaranth seed antihypertensive bioactive peptide |
| JP6940305B2 (en) * | 2017-06-01 | 2021-09-22 | 株式会社明治 | How to make cheese flavored ingredients |
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| CN1552891A (en) * | 2003-11-10 | 2004-12-08 | 东北农业大学 | Preparation of dairy ACE inhibitory peptide |
| CN1782091A (en) * | 2004-11-29 | 2006-06-07 | 中国农业大学 | Method for producing angiotonin converzyme inhibiting peptide by whey proteinase method |
| CN1858230A (en) * | 2006-03-03 | 2006-11-08 | 中国海洋大学 | Process for preparing oligomeric peptide capable of inhibiting angiotonase activity |
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