CN103122022A - Angiotensin converting enzyme inhibitory peptide derived from bitter almond protein and preparation method thereof - Google Patents

Angiotensin converting enzyme inhibitory peptide derived from bitter almond protein and preparation method thereof Download PDF

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CN103122022A
CN103122022A CN2013100395410A CN201310039541A CN103122022A CN 103122022 A CN103122022 A CN 103122022A CN 2013100395410 A CN2013100395410 A CN 2013100395410A CN 201310039541 A CN201310039541 A CN 201310039541A CN 103122022 A CN103122022 A CN 103122022A
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朱振宝
易建华
周慧江
刘旷
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Shaanxi University of Science and Technology
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Abstract

The invention provides an angiotensin converting enzyme inhibitory peptide derived from bitter almond protein and a preparation method thereof. The inhibitor is pentapeptide of which the relative molecular mass is 688 and the amino acid sequence is Thr-Tyr-Gly-Trp-Tyr. The preparation method comprises the following steps: debitterizing and detoxifying peeled bitter almond raw material, degreasing with petroleum ether, extracting and separating the protein by an alkali fusion acid precipitation method, carrying out enzymolysis with an alkaline proteinase, carrying out centrifugal separation on the enzymolysis solution, taking the supernatant, separating with an ultrafiltration membrane, and separating and purifying by gel filtration chromatography and reversed phase high performance liquid chromatography to obtain the new ACE (angiotensin converting enzyme) inhibitory peptide.

Description

The angiotensin converting enzyme-inhibiting peptide in Almond Proteins source and preparation method thereof
Technical field
The invention belongs to bio-pharmaceuticals or functional foodstuff processing technique field, relate to polypeptide structure and sequence, be specifically related to Zinc metallopeptidase Zace1 (ACE) inhibiting peptide in a kind of Almond Proteins source and preparation method thereof.
Background technology
Comprise bioactive peptides sequence in many natural protein structures, the effect through Digest enzyme in enzyme extracorporeal hydrolysis or body can discharge the biologically active peptides with various functions.Wherein, food source property ACE inhibitor peptide has very large potentiality aspect prevention and treatment hypertension.Food source property ACE inhibitor peptide has edible safety, and the advantage such as have no side effect becomes the critical function food factor of hyperpietic's assisting therapy.ACE is a kind of metallopeptidase, contains two in conjunction with Zn 2+The site, i.e. so-called " necessary binding site " contains one or several " additional binding site " in addition.Zn 2+Binding site is position, ACE catalytic reaction activity group place, and the acting in conjunction that comprises the various ACEI of ace inhibitory peptide is the Zn with the ACE reactive site 2+In conjunction with, make it inactivation.Semen Armeniacae Amarum is the seed of ansu apricot (Armeniaca vulgaris Lam), be not only the important by-products of apricot product processing, or a kind of traditional Chinese medicine has sending down abnormally ascending, relieving cough and asthma, the effect that relaxes bowel, clinically the respiratory tract disease such as multiplex, asthma many in treatment body heat, cough, phlegm.Debitterize, the Semen Armeniacae Amarum that takes off glycosides are the vegetable-protein new resources of a class high-quality, and its amino acid Compositional balance is reasonable, and nutritive value is higher.
At present, food source property ACE inhibitor peptide mainly is comprised of 2 ~ 11 amino acid, molecular weight is less than the oligopeptides of 1KDa, the preparation method is the albumen by each kind of plant of enzymolysis, animal-origin, as soybean protein, milk-protein, aquatic product protein, insect protein, also there is no the report of the ACE inhibitor peptide in Almond Proteins source.
Summary of the invention
The object of the present invention is to provide the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source and preparation method thereof.
For achieving the above object, the present invention has adopted following technical scheme:
The angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source, this inhibiting peptide has the aminoacid sequence as shown in SEQ.ID.NO.1.
The preparation method of the angiotensin converting enzyme-inhibiting peptide in above-mentioned Almond Proteins source comprises the following steps:
1) with Semen Armeniacae Amarum peeling, pulverize after removing amygdaloside, the Semen Armeniacae Amarum spent meal that then sieves after petroleum ether degreasing to get extracts Almond Proteins in the Semen Armeniacae Amarum spent meal with the alkali extraction and acid precipitation method, and the Almond Proteins lyophilize is got the Semen Armeniacae Amarum separated protein powder;
2) Semen Armeniacae Amarum separated protein powder and water are mixed to get protein solution, the Sumizyme MP that adds Semen Armeniacae Amarum separated protein powder quality 2% in the protein solution, then the pH that regulates protein solution is 7.0, temperature is that after 50 ℃, isothermal reaction 4h gets enzymolysis solution, enzymolysis solution is gone out in boiling water enzyme 2min, then centrifugal 20min under 4 ℃, 10000r/min;
3) get supernatant liquor after centrifugal, the ultrafiltration membrance filter that is 1KDa through molecular weight cut-off with supernatant liquor must see through liquid, will get lyophilized powder through liquid vacuum concentration, lyophilize;
4) different according to hydrophobicity, lyophilized powder is carried out the gel filtration chromatography separation obtain two components, the Zinc metallopeptidase Zace1 (ACE) of measuring respectively two components suppresses active, two component Angiotensin-Converting converting Enzymes (ACE) is suppressed active higher component be designated as component 2;
5) component 2 is carried out RPLC and separate, the component that separation obtains is determined Zinc metallopeptidase Zace1 inhibition the highest active component after the active detection of menses ACEs (ACE) inhibition respectively, be designated as component e;
6) with component e by analysis type RP-HPLC system continue separation and purification, the separation and purification obtained component is carried out Zinc metallopeptidase Zace1 (ACE) suppress active definite Zinc metallopeptidase Zace1 inhibition the highest active component that detects, be designated as component QH, component QH is the target inhibiting peptide, target inhibiting peptide aminoacid sequence is Thr-Tyr-Gly-Trp-Tyr(TYGWY), molecular weight is 668.
Described Sumizyme MP is that the Alacase2.4L(manufacturer is Novi's letter), enzyme activity is 2.4AU/g.
After ultrafiltration membrance filter, molecular weight is less than the IC of 1KDa component 50Be 0.15 ± 0.007mg/mL.
The method that described gel filtration chromatography is separated is: with Sephadex G-15, lyophilized powder is separated, before loading, lyophilized powder is dissolved in ultrapure water, loading concentration is 200mg/mL, applied sample amount is 2mL, elutriant is the trifluoroacetic acid aqueous solution of massfraction 0.1%, eluent flow rate is 0.5mL/min, collects respectively the elutriant that elution volume is 200-275mL and 280-500mL, obtains two components after merging.
Described RPLC adopts the PRC-ODS chromatographic column, and (manufacturer is Shimadzu, be of a size of 250 * 20mm, particle diameter is 5 μ m), before sample introduction, 100mg component 2 is dissolved in the ultrapure water of 100mL, sample size is 500 μ L, and mobile phase A is trifluoroacetic acid (TFA) acetonitrile solution of massfraction 0.1%, and Mobile phase B is trifluoroacetic acid (TFA) the ultrapure water solution of massfraction 0.1%; Elution requirement is: 0～30min, 90%～75% Mobile phase B; 30～40min, 75%～90% Mobile phase B, flow velocity is 14mL/min, the detection wavelength is 214nm.
Described component 2 is isolated a, b, c, d, five components of e through RPLC (RP-HPLC), and the Zinc metallopeptidase Zace1 of five components (ACE) inhibiting rate is respectively 10%, 25.6%, 25.0%, 24.3% and 41.9%.
The described analysis mode RP-HPLC employing Diamonsil of system TMC 18Chromatographic column (manufacturer is Dai An company, is of a size of 4.6 * 250mm, and particle diameter is 5 μ m); UV-detector (UV) detects wavelength 214nm; Mobile phase A is trifluoroacetic acid (TFA) the ultrapure water solution of massfraction 0.1%, and Mobile phase B is trifluoroacetic acid (TFA) acetonitrile solution of massfraction 0.07%; Flow velocity is 1.0mL/min; Sample size is 20 μ L; Column temperature is 30 ℃; Condition of gradient elution is 0 ~ 20min, 20 ~ 25% Mobile phase B; 20 ~ 30min, 25 ~ 15% Mobile phase B; 30 ~ 40min, 15 ~ 10% Mobile phase B.
The present invention adopts the Semen Armeniacae Amarum raw material of peeling through debitterize, detoxification, petroleum ether degreasing, adopt the alkali extraction and acid precipitation method to extract protein isolate, then through the Sumizyme MP enzymolysis, enzymolysis solution through centrifugal, ultra-filtration membrane separation, gel filtration chromatography separate with RPLC, purifying obtains a kind of new ace inhibitory peptide, utilizes electron spray(ES) plural serial stage mass spectrum (ESI-MS n), in conjunction with amino acid analysis, its structure is identified.
Inhibiting peptide of the present invention is 5 peptides with high ACE inhibition activity in Almond Proteins source, this peptide is that Almond Proteins obtains after hydrolysis under mild conditions through food grade enzyme, and it is safe, and can prepare in a large number, therefore, be expected to provide effective constituent for developing new Altace Ramipril.
Description of drawings
Fig. 1 is that SephadexG-15 separates Almond Proteins hydrolyzate component III (﹤ 1000Da) gel chromatography collection of illustrative plates;
Fig. 2 is that half preparation property RP-HPLC separates SephadexG-15 gel chromatography component 2(F III 2) result;
Fig. 3 is that analysis mode RP-HPLC separates preparation property liquid phase component e(F III 2e) result;
Fig. 4 is the total ion chromatogram of component e (F III 2e);
Fig. 5 is that retention time is 1.23 peak ESI mass spectrum (M+H +).
Embodiment
Below in conjunction with accompanying drawing, invention is described further.
(1) Semen Armeniacae Amarum protein isolate preparation
after the manual peeling of Semen Armeniacae Amarum raw material, salt acid soak 6h with massfraction 0.3%, then use water soaking 42h instead, every 6h changes water one time, to remove the amygdaloside in Semen Armeniacae Amarum, then 40 ℃ of dry 24h in baking oven, then the Semen Armeniacae Amarum of drying is pulverized, with petroleum ether degreasing (the mass ratio 1:6 of Semen Armeniacae Amarum and sherwood oil) three times, after degreasing, (40 ℃) oven dry removes sherwood oil, then cross 60 mesh sieves and obtain the Semen Armeniacae Amarum spent meal, extract Almond Proteins with the alkali extraction and acid precipitation method, in the alkali extraction and acid precipitation method: the molten stage of alkali, the Semen Armeniacae Amarum spent meal is added to the water, the regulation system temperature is 50 ℃, regulation system pH value is 11, magnetic agitation 2 hours, the heavy stage of acid, staticly settle 1 hour after regulating pH to 4.8.The Almond Proteins lyophilize is got the Semen Armeniacae Amarum separated protein powder.
(2) enzymolysis of Semen Armeniacae Amarum protein isolate
Semen Armeniacae Amarum separated protein powder (lipidated protein 82.5%) water is made into protein solution (every 1g Semen Armeniacae Amarum separated protein powder mixes with 50mL water), add Sumizyme MP Alacase2.4L in protein solution, the mass ratio of Sumizyme MP and Semen Armeniacae Amarum separated protein powder is 2%, the pH value of then regulating protein solution is 7.0, and get enzymolysis solution in 50 ℃ of enzymolysis 4h, enzymolysis solution is boiled the 2min enzyme that goes out in boiling water, then regulate pH to neutral, and in 4 ℃ of centrifugal 20min of lower 10000r/min, get supernatant liquor.
(3) protein enzymatic hydrolyzate separation, purifying
Ultrafiltration: the ultra-filtration membrane that centrifugal rear supernatant liquor is 5KDa and 1KDa through molecular weight cut-off respectively separates, zymolyte is divided into three components, components I (M＞5KDa), compositionⅱ (1KDa＜M＜5KDa), component III (M＜1KDa), each component is through (40 ℃ of Rotary Evaporators vacuum concentration (60 ℃), lyophilizes, 0.01MPa), then detect respectively ACE and suppress active, after testing, the inhibition activity of component III is the highest;
Gel filtration chromatography is separated: (M＜1KDa) carrying out gel filtration chromatography separates with the component III after lyophilize, separating medium is SephadexG-15, loading concentration is 200mg/mL, applied sample amount is 2mL, TFA(trifluoroacetic acid take massfraction 0.1%) aqueous solution is as elutriant, and elution speed is 0.5mL/min.The target components that the collection gel filtration chromatography flows out, different according to hydrophobicity, the component III is separated into two main ingredient (see figure 1)s, will detect respectively ACE after two component lyophilizes and suppress active, and it is active that wherein component 2 has higher ACE inhibition;
RPLC separates: collect the component (component 2) with higher ACE inhibition activity that gel filtration chromatography is separated, carry out half preparation RP-HPLC purifying.
Chromatographic condition: PRC-ODS chromatographic column (250 * 20mm, 5 μ m), mobile phase A: the acetonitrile that contains 0.1%TFA; Mobile phase B: contain the ultrapure water of 0.1%TFA, elution requirement: 0～30min, 90%～75% Mobile phase B; 30～40min, 75%～90% Mobile phase B, flow velocity: 14mL/min, detect wavelength: 214nm, sample size: 500 μ L, for obtaining enough analytic samples, repeated isolation 5 times, and collect and obtain different components.Through above-mentioned separation, purification step, obtain altogether a, b, c, d, five kinds of ace inhibitory peptide (see figure 2)s of e.Suppress active through ACE and detect, the Zinc metallopeptidase Zace1 of five components (ACE) inhibiting rate is respectively 10%, 25.6%, 25.0%, 24.3% and 41.9%, and wherein, it is the highest that the ACE of component e suppresses activity.
(4) ace inhibitory peptide Structural Identification
The component e that obtains through above-mentioned separation, purge process adopts to component e that analysis mode RP-HPLC system continues to separate, purifying, and analysis mode RP-HPLC system adopts Diamonsil TMC 18Chromatographic column, the manufacturer is Dai An company, is of a size of 4.6 * 250mm, particle diameter is 5 μ m; UV-detector (UV) detects wavelength 214nm; Mobile phase A: ultrapure water (containing 0.1%TFA), Mobile phase B: acetonitrile (containing 0.07%TFA); Flow velocity: 1.0mL/min; Sample size: 20 μ L; Column temperature: 30 ℃; Condition of gradient elution: 0 ~ 20min, 20 ~ 25% Mobile phase B; 20 ~ 30min, 25 ~ 15% Mobile phase B; 30 ~ 40min, 15 ~ 10% Mobile phase B.
By analysis type RP-HPLC system continue to separate, purifying, find that component e forms (see figure 3) by the peak of 4 different retention time, collect each component, carry out ACE and suppress active detection, through superelevation liquid phase-electrospray ionization mass spectrum, component e is carried out preliminary evaluation, the retention time of its 4 quasi-molecular ions is respectively 0.99,1.23,1.47,1.59min(sees Fig. 4), wherein the ACE inhibiting rate at retention time 1.23min peak is the highest, through electron spray(ES) plural serial stage mass spectrum (ESI-MS n), in conjunction with amino acid analysis, identify that its relative molecular mass is that 688(sees Fig. 5), sequence is Thr-Tyr-Gly-Trp-Tyr(TYGWY).
(5) ACE suppresses activity test method
ACE suppresses the active RP-HPLC of employing sample by direct sample introduction, and specific as follows: the freeze-drying sample is dissolved in ultrapure water (2.5mg/mL), gets supernatant liquor after the centrifugal 15min of 10000g/min and carries out ACE inhibition determination of activity.
10 μ L sample solutions add 10 μ LACE(0.25U to be dissolved in 2.5mL pH8.350mmol/L borax-borate buffer, wherein contain 300mmol/L NaCl) in 37 ℃ of insulation 10min, add 50 μ L6.15mmol/LHHL(Hip-His-Leu to be dissolved in same buffer), after reacting 30min under 37 ℃, add 85 μ L1mol/L hydrochloric acid soln termination reactions, get reaction product after being cooled to room temperature, get 20 μ L reaction product sample introductions, by the quantitative urobenzoic acid growing amount of RP-HPLC wash-out collection of illustrative plates, come calculation sample active to the inhibition of ACE with the urobenzoic acid growing amount, do simultaneously blank (replacing sample solution with borax-borate buffer).Calculation formula is as follows:
Figure BDA00002802960000071
Chromatographic condition is as follows:
Chromatographic column, Diamonsil TMC 18Post (4.6 * 250mm);
UV-detector, wavelength 228nm;
Mobile phase A: 25% acetonitrile, Mobile phase B: 75% ultrapure water (containing 0.1%TFA);
Flow velocity: 1.0mL/min; Sample size: 20 μ L; Column temperature: 30 ℃.
Figure IDA00002802960800011

Claims (8)

1. the angiotensin converting enzyme-inhibiting peptide in Almond Proteins source, it is characterized in that: this inhibiting peptide has the aminoacid sequence as shown in SEQ.ID.NO.1.
2. preparation method of the angiotensin converting enzyme-inhibiting peptide in Almond Proteins source as claimed in claim 1 is characterized in that: comprise the following steps:
1) Semen Armeniacae Amarum is pulverized, the Semen Armeniacae Amarum spent meal that then sieves after petroleum ether degreasing to get, the Almond Proteins with in alkali extraction and acid precipitation method extraction Semen Armeniacae Amarum spent meal gets the Semen Armeniacae Amarum separated protein powder with the Almond Proteins lyophilize;
2) Semen Armeniacae Amarum separated protein powder and water are mixed to get protein solution, the Sumizyme MP that adds Semen Armeniacae Amarum separated protein powder quality 2% in the protein solution, then the pH that regulates protein solution is 7.0, temperature is that after 50 ℃, isothermal reaction 4h gets enzymolysis solution, enzymolysis solution is gone out in boiling water enzyme, then centrifugal;
3) get supernatant liquor after centrifugal, the ultrafiltration membrance filter that is 1KDa through molecular weight cut-off with supernatant liquor must see through liquid, will get lyophilized powder through liquid vacuum concentration, lyophilize;
4) lyophilized powder is carried out the gel filtration chromatography separation and obtain two components, the Zinc metallopeptidase Zace1 of measuring respectively two components suppresses active, and two higher components of component Angiotensin-Convertings conversion enzyme inhibition activity are designated as component 2;
5) component 2 is carried out RPLC and separate, the component that separation obtains is determined Zinc metallopeptidase Zace1 inhibition the highest active component after the active detection of menses ACE inhibition respectively, be designated as component e;
6) with component e by analysis type RP-HPLC system continue separation and purification, the separation and purification obtained component is carried out Zinc metallopeptidase Zace1 suppresses active the detection and determine that Zinc metallopeptidase Zace1 suppresses the highest active component, is the target inhibiting peptide.
3. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2, it is characterized in that: described Sumizyme MP is Alacase2.4L, and enzyme activity is 2.4AU/g.
4. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2, it is characterized in that: after ultrafiltration membrance filter, molecular weight is less than the IC of 1KDa component 50Be 0.15 ± 0.007mg/mL.
5. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2, it is characterized in that: the method that described gel filtration chromatography is separated is: with Sephadex G-15, lyophilized powder is separated, before loading, lyophilized powder is dissolved in ultrapure water, loading concentration is 200mg/mL, applied sample amount is 2mL, elutriant is the trifluoroacetic acid aqueous solution of massfraction 0.1%, eluent flow rate is 0.5mL/min, collects respectively the elutriant that elution volume is 200-275mL and 280-500mL.
6. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2, it is characterized in that: described RPLC adopts the PRC-ODS chromatographic column, before sample introduction, 100mg component 2 is dissolved in the ultrapure water of 100mL, sample size is 500 μ L, mobile phase A is the trifluoroacetic acid acetonitrile solution of massfraction 0.1%, and Mobile phase B is the trifluoroacetic acid ultrapure water solution of massfraction 0.1%; Elution requirement is: 0～30min, 90%～75% Mobile phase B; 30～40min, 75%～90% Mobile phase B, flow velocity is 14mL/min, the detection wavelength is 214nm.
7. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2, it is characterized in that: described component 2 is isolated a, b, c, d, five components of e through RPLC, and the Zinc metallopeptidase Zace1 inhibiting rate of five components is respectively 10%, 25.6%, 25.0%, 24.3% and 41.9%.
8. the preparation method of the angiotensin converting enzyme-inhibiting peptide in a kind of Almond Proteins source according to claim 2 is characterized in that: described analysis mode RP-HPLC system adopts C 18Chromatographic column; UV-detector detects wavelength 214nm; Mobile phase A is the trifluoroacetic acid ultrapure water solution of massfraction 0.1%, and Mobile phase B is the trifluoroacetic acid acetonitrile solution of massfraction 0.07%; Flow velocity is 1.0mL/min; Sample size is 20 μ L; Column temperature is 30 ℃; Condition of gradient elution is 0 ~ 20min, 20 ~ 25% Mobile phase B; 20 ~ 30min, 25 ~ 15% Mobile phase B; 30 ~ 40min, 15 ~ 10% Mobile phase B.
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CN105131083A (en) * 2015-07-30 2015-12-09 陕西师范大学 Flat almond peptides capable of inhibiting activity of angiotensin converting enzyme (ACE) and preparation method thereof
CN105859868A (en) * 2016-06-08 2016-08-17 广西科技大学 Angiotensin converting enzyme inhibition peptide and preparing method thereof
CN109956995A (en) * 2017-12-14 2019-07-02 浙江工商大学 A kind of paclitaxel loaded Almond Proteins nano-carrier and preparation method thereof
CN110105430A (en) * 2019-05-23 2019-08-09 合肥工业大学 A kind of ginkgo nut protein peptides and preparation method thereof with angiotensin converting enzyme inhibition activity
CN110183516A (en) * 2019-05-23 2019-08-30 合肥工业大学 A kind of preparation method of blood pressure lowering ginkgo nut protein peptides
CN110194786A (en) * 2019-05-23 2019-09-03 合肥工业大学 A kind of ginkgo nut protein peptides and preparation method thereof with ACE inhibitory activity
CN110551704A (en) * 2019-08-30 2019-12-10 集美大学 Method for separating and purifying angiotensin converting enzyme from pig lungs
CN110746485A (en) * 2019-10-09 2020-02-04 天津科技大学 Screening of novel alkaline protease inhibitory peptides
CN111138516A (en) * 2020-01-10 2020-05-12 大理大学 Vespa mandarinia peptide and preparation method and application thereof
CN115109817A (en) * 2021-06-22 2022-09-27 国家林业和草原局泡桐研究开发中心 Almond peptide with antioxidant and immunocompetence, preparation method and application thereof

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CN105131083A (en) * 2015-07-30 2015-12-09 陕西师范大学 Flat almond peptides capable of inhibiting activity of angiotensin converting enzyme (ACE) and preparation method thereof
CN105131083B (en) * 2015-07-30 2018-07-10 陕西师范大学 Flat almond peptide with angiotensin converting enzyme inhibition activity and preparation method thereof
CN105859868A (en) * 2016-06-08 2016-08-17 广西科技大学 Angiotensin converting enzyme inhibition peptide and preparing method thereof
CN109956995A (en) * 2017-12-14 2019-07-02 浙江工商大学 A kind of paclitaxel loaded Almond Proteins nano-carrier and preparation method thereof
CN109956995B (en) * 2017-12-14 2023-07-28 浙江工商大学 Paclitaxel-loaded bitter almond protein nano-carrier and preparation method thereof
CN110194786A (en) * 2019-05-23 2019-09-03 合肥工业大学 A kind of ginkgo nut protein peptides and preparation method thereof with ACE inhibitory activity
CN110183516A (en) * 2019-05-23 2019-08-30 合肥工业大学 A kind of preparation method of blood pressure lowering ginkgo nut protein peptides
CN110105430A (en) * 2019-05-23 2019-08-09 合肥工业大学 A kind of ginkgo nut protein peptides and preparation method thereof with angiotensin converting enzyme inhibition activity
CN110551704A (en) * 2019-08-30 2019-12-10 集美大学 Method for separating and purifying angiotensin converting enzyme from pig lungs
CN110746485A (en) * 2019-10-09 2020-02-04 天津科技大学 Screening of novel alkaline protease inhibitory peptides
CN111138516A (en) * 2020-01-10 2020-05-12 大理大学 Vespa mandarinia peptide and preparation method and application thereof
CN111138516B (en) * 2020-01-10 2023-04-25 大理大学 Royal jelly peptide and preparation method and application thereof
CN115109817A (en) * 2021-06-22 2022-09-27 国家林业和草原局泡桐研究开发中心 Almond peptide with antioxidant and immunocompetence, preparation method and application thereof

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