CN106967773A - A kind of application restructuring aminopeptidase takes off bitter method to rice peptide - Google Patents
A kind of application restructuring aminopeptidase takes off bitter method to rice peptide Download PDFInfo
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- CN106967773A CN106967773A CN201710260560.4A CN201710260560A CN106967773A CN 106967773 A CN106967773 A CN 106967773A CN 201710260560 A CN201710260560 A CN 201710260560A CN 106967773 A CN106967773 A CN 106967773A
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- aminopeptidase
- enzymolysis
- peptide
- amino acid
- rice peptide
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
Abstract
Bitter method is taken off to rice peptide the invention discloses a kind of application restructuring aminopeptidase, belongs to enzyme preparation technical field.The enzyme is strong to the hydrolysis ability of albumen and the hydrophobic amino acid of peptide termini.It is due on polypeptide chain caused by hydrophobic amino acid that albumen or polypeptide solution, which produce bitter taste, utilize leucine amino peptidase single enzymolysis rice peptide, the hydrophobic amino acid total amount dissociated in its enzymolysis liquid is 4.39 times before enzymolysis, the 1000Da of molecular weight 500 peptide content reduces 30.63% after enzymolysis, it can solve protein hydrolyzate bitterness problem, improve its local flavor and quality, utilize leucine and proline aminopeptidase synergetic hydrolysis rice peptide, its Pro content is 1.78 times after single enzymolysis, further de- bitter ability of the reinforcing to protide hydrolyzate.
Description
Technical field
Bitter method is taken off to rice peptide the present invention relates to a kind of application restructuring aminopeptidase, belongs to enzyme preparation technical field.
Background technology
Rice peptide is using rice protein as raw material, through small molecule egg obtained from a series of refinement treatments such as enzymolysis, UF membrane
White matter hydrolysate, it is mainly made up of multiple polypeptides molecule mixture, and other a small amount of free amino acids, carbohydrate and
Inorganic salts etc., with property easy to digest and easy absorbability, hypoallergenic, hypotensive, norcholesterol, rush fat metabolism and enhancing physical efficiency
With the effect of setting up etc..Therefore rice peptide can be widely applied to as the high-grade functional protein additive of nutraceutical industry
The fields such as health food, nutraceutical, bakery product, arsenic.Rice peptide can carry a certain degree of hardship in preparation
Taste can directly affect the quality of food, and its popularization and application in the food industry is limited to a certain extent.Therefore, for rice peptide
Carry out de- bitter mouthfeel and quality for improving food very necessary.
The content of the invention
First purpose of the present invention is to provide a kind of method that hardship is taken off to rice peptide, and methods described is added into rice peptide
Leucine amino peptidase, 200-300U/g substrate prolines aminopeptidase or its combination of 1600-2100U/g substrates, enter to rice peptide
Water-filling solution.
In one embodiment of the invention, the addition of the leucine amino peptidase is 1800~2100U/g substrates.
In one embodiment of the invention, the addition of the proline aminopeptidase is 200-300U/g substrates.
In one embodiment of the invention, the rice peptide concentration is 50~70g/L.
In one embodiment of the invention, the hydrolysis is carried out at 40~60 DEG C.
In one embodiment of the invention, the hydrolysis time is 3~6h.
In one embodiment of the invention, the hydrolysis is to digest 4~6h to rice peptide at 45~55 DEG C.
In one embodiment of the invention, the proline aminopeptidase is to be fermented to produce by recombined bacillus subtilis
, the recombined bacillus subtilis is using WB600 as host, using PMA5 as carrier, pap genes is expressed, in Publication No.
Disclosed in 105018407A national inventing patent application.
In one embodiment of the invention, the proline aminopeptidase is prepared as follows obtaining：Will be described
Zymotic fluid regulation pH flocculations after recombined bacillus subtilis fermentation, plate-frame filtering, 20~30KDa PES rolled film ultrafiltration is dense
Contracting, is freezed, and is crushed, and sieving obtains enzyme powder.
In one embodiment of the invention, the fermentation is carried out as follows：Recombined bacillus subtilis with 2~
5% (v/v, mL/100mL) inoculum concentration is inoculated into the fermentation tank containing fermentation medium, 200~450rpm, initial throughput：
7.0~9.0m3/ h, pH7.0, initial tank press 0.0~0.08MPa, stage temperature controlled fermentation：Preceding 18h temperature is 35~37 DEG C, 18h
Afterwards, temperature control is 30~32 DEG C；Tank under dissolved oxygen >=30%, 40~45h of culture is maintained to obtain zymotic fluid.
In one embodiment of the invention, the fermentation medium components for fermenting and producing leucine amino peptidase are：
Starch 20g/L, dregs of beans 20g/L, yeast extract 18g/L, dipotassium hydrogen phosphate 6g/L, cobalt chloride 0.6mmol/L, glycerine 2mL/L, chlorination
Potassium 0.1mol/L, Tween-80 2.4mL/L, L-sodium 6g/L, potassium tartrate 7g/L.
In one embodiment of the invention, the regulation pH flocculations are the pH to 8.0 for adjusting zymotic fluid, are added
0.15%W/V cationic flocculant, 2.5%W/V diatomite, is stirred and evenly mixed.
In one embodiment of the invention, the plate-frame filtering is to cross sheet frame pressure with 80~100mL/min speed
Filter.
In one embodiment of the invention, the ultrafiltration is to be concentrated by ultrafiltration 7 times with 20~30KDa PES rolled films.
In one embodiment of the invention, methods described is with 1800U/g ratios addition rice peptide solution by enzyme powder
In, maintain 45~50 DEG C of temperature, pH to boil 10min after maintaining 8.3~8.5, enzymolysis 4h, be cooled to 50 DEG C, add proline
Aminopeptidase is hydrolyzed, and further takes off hardship.
The present invention also application of the protection methods described in the product containing amino acid or polypeptide is prepared.
Beneficial effects of the present invention：The invention provides a kind of recombined bacillus subtilis leucine amino peptidase system of improvement
Standby technique, the aminopeptidase rate of recovery of flocculated stage is up to 82.7%, and the ultra-filtration stage aminopeptidase rate of recovery is 78.22%, is solved
Treating capacity is few in existing extraction process, operation difficulty is big, cost is high, it is difficult to the problem of scale is applied.The preparation of the present invention
Technological operation is simple, easily amplification, is adapted to large-scale production, can provide condition for the application of follow-up aminopeptidase.The present invention is by bright ammonia
Sour aminopeptidase single enzymolysis and with proline aminopeptidase jointly applied to there is provided using two kinds of aminopeptidases in the hydrolysis of rice peptide
Leucine, arginine and free hydrophobic amino acid total amount difference in the enzymolysis process of synergetic hydrolysis rice peptide, enzymolysis liquid
It is 3.39 times, 16.48 times, 4.39 times before enzymolysis, molecular weight 500-1000Da peptide content reduces 30.63% after enzymolysis,
Pro contents are 1.78 times after single enzymolysis after double enzyme synergetic hydrolysis.The bitter taste of polypeptide can be reduced to conspicuousness, local flavor is lifted
And quality, it is de- relative to other method bitter more thoroughly safe, will be the application main trend of food protein resource deep processing from now on.
Brief description of the drawings
Fig. 1 is leucine amino peptidase preparation flow schematic diagram；
Fig. 2 is influence of the cycles of concentration to the aminopeptidase rate of recovery and membrane flux；
Fig. 3 is the distribution of polypeptide molecular weight before and after enzymolysis；
Fig. 4 is hydrophobic amino acid and two kinds of basic amino acid changes of contents after single enzyme, double enzyme synergetic hydrolysis；
The addition of Fig. 5 leucine amino peptidases is to hydrophobic amino acid and two kinds of basic amino acid changes of contents before and after enzymolysis；
The different enzyme-added orders of Fig. 6 are to hydrophobic amino acid and two kinds of basic amino acid changes of contents before and after enzymolysis；
Hydrophobic amino acid increment changes under the conditions of Fig. 7 difference enzymolysis rice peptides.
Embodiment
Enzyme activity determination (LNA methods)：2mL (Tris pH8.5) solution, 50 DEG C of preheating 3min, has sequentially added 1mL
The enzyme liquid of dilution, 1mL substrate, shakes up, 50 DEG C of water-bath 10min.Reaction terminates, and test tube is put into frozen water immediately, in 405nm
Quick determination sample absorbance, calculates enzyme activity down.Calculation formula：
In formula：The enzyme activity (U/mL) of X- samples；
N- measures absorbance at wavelength 405nm；
The multiple of Y- enzyme liquids dilution.
Enzyme activity is defined：Defining an enzyme-activity unit (U) is, under given conditions (50 DEG C, pH8.5), catalysis per minute
Decompose the enzyme amount required for leu-pNA generations 1umoL pNA.
Amino acid and polypeptide molecular weight are determined：Enzymolysis liquid 12000rpm centrifuges 10min, takes supernatant sample presentation to detect peptide molecule
Amount distribution, takes supernatant sample presentation to add 10% isometric TCA solution, stands 3h, 15000rpm, centrifuges 10min, takes supernatant to send
Sample surveys the amino acid content dissociated in enzymolysis liquid.
The separating technology of the recombined bacillus subtilis leucine amino peptidase of embodiment 1
Zymotic fluid：Recombined bacillus subtilis (WB600) is inoculated into containing fermented and cultured with 2~5% (v/v) inoculum concentration
Base (starch 20g/L, dregs of beans 20g/L, yeast extract 18g/L, dipotassium hydrogen phosphate 6g/L, cobalt chloride 0.6mmol/L, glycerine 0.2%,
Potassium chloride 0.1mol/L, Tween-80 0.24%, L-sodium 0.6%, potassium tartrate 0.7%) fermentation tank in, 200~
450rpm, initial throughput：7.0~9.0m3/ h, pH7.0, initial tank press 0.06~0.08MPa, stage temperature controlled fermentation：Preceding 18h
Temperature is 35~37 DEG C, after 18h, and temperature control is 30~32 DEG C；By first rising tank pressure, throughput is increased, the strategies such as speed are turned
Minimum dissolved oxygen tank under 30%, 40~45h of culture is maintained to obtain the zymotic fluid containing leucine amino peptidase.
(1) by into recombined bacillus subtilis zymotic fluid add 2.5%W/V (g/100mL) diatomite, 0.15~
0.2%W/V cationic flocculant, is added dropwise 0.5mol/L NaOH regulations pH to 8.0.By the zymotic fluid after flocculation, stirring is equal
It is even, filtered with 80~100mL/min speed, collect time of leucine amino peptidase in the bright zymotic fluid of clarification, whole process
Yield is 82.7%.
(2) 2L FILTECH-UF101 type ultrafiltration system (PES rolled films) system is recycled to carry out ultrafiltration, operating pressure
0.25Mpa, concentrates 7 times, the leucine amino peptidase rate of recovery is 78.22%, membrane flux is 11.54L/ (m2H), finally will concentration
Liquid is freezed, and is crushed, and sieving obtains homogeneous enzyme powder, as a result sees Fig. 2.
Application of the leucine amino peptidase of embodiment 2 in the de- hardship of rice peptide.
Rice peptide 2.5g accurately is weighed, concentration is configured to for 50g/L rice peptide solution 50mL, utilizes constant temperature blender with magnetic force
It is 50 DEG C to maintain hydrolysis temperature, is 1800U/g by the amount ratio of leucine amino peptidase and substrate, adds 0.5g enzyme powder (enzyme activities
9000U/g) in rice peptide solution, increase speed of agitator, be added dropwise 0.5mol/L NaOH regulation pH, maintain pH8.3~
8.5,4h, boiling water bath 10min are digested, cooling a period of time, enzymolysis liquid 12000rpm 10min is centrifuged into, takes supernatant 2mL to survey enzyme
The polypeptide molecular weight distribution of liquid is solved, takes supernatant 3mL to add 10% isometric TCA solution, 3h, 15000rpm, centrifugation is stood
30min, takes supernatant to cross 0.22um microfiltration membranes, takes 400uL to survey the free aminoacid content of enzymolysis liquid.
Polypeptide molecular weight distribution (Fig. 3 and Fig. 4) result is shown：Content of peptides less than 180Da adds 102.04%,
The peptide content that 500-1000Da peptide content reduces 30.63%, 1000-2000Da reduces 35.60%, 2000-5000Da
Peptide content reduce 32.80%, the research of prior art shows that generally higher than 5000Da peptide does not have bitter taste, and between 500-
1000Da small peptide bitter taste is most strong, therefore, and significant de-bittering effect can be reached by carrying out enzymolysis using leucine.
Amino acid analysis (Fig. 4) can be seen that：Leucine, arginine content and free hydrophobic amino in enzymolysis liquid
Sour total amount is 3.39 times, 16.48 times, 4.39 times before enzymolysis respectively, and other amino acid increments are as shown in table 1.
The hydrophobic amino acid free before and after digesting of table 1 and two kinds of basic amino acid changes of contents
The application of the leucine of embodiment 3 and the double enzyme collaborations of proline in the de- hardship of rice peptide
Rice peptide 2.5g accurately is weighed, concentration is configured to for 50g/L rice peptide solution 50mL, controls 50 DEG C of hydrolysis temperature,
0.5g leucine amino peptidase enzyme powders (enzyme activity 9000U/g) are added in rice peptide solution, speed of agitator is increased, are added dropwise
0.5mol/L NaOH regulation pH, maintain pH8.3~8.5, digest 4h, boiling water bath 10min, cooling a period of time, adjust pH
To 7.5, proline aminopeptidase 800U is added, temperature 50 C, control pH7.3~7.5 is maintained, accurately hydrolyzes 3h, boiling water bath
10min, cooling, free amino acid and polypeptide molecular weight distribution are surveyed in sampling after processing.
Polypeptide molecular weight distribution (Fig. 3) can be seen that：Double enzyme collaborations are compared with single enzymolysis, 180-500Da peptide content
0.97% is added, molecular weight reduces 1.35% for 500~1000Da content of peptides.Amino acid analysis (Fig. 4) can be seen
Go out：Pro contents are 1.78 times after single enzymolysis, other hydrophobic aminos after leucine and proline aminopeptidase synergetic hydrolysis
Sour amplification is smaller, meets the hydrolysis specificity of the enzyme, relative to single enzymolysis rice peptide, and double enzyme synergies can more strengthen de- hardship
The local flavor and quality of effect, further lifting rice peptide.
Embodiment 4
Embodiment be the same as Example 2, its difference is, leucine amino peptidase is added with 900U/g addition, corresponding
Free hydrophobic amino acid content is as shown in figure 5, leucine, arginine content and free hydrophobic amino in enzymolysis liquid
Sour total amount is below with 30%~40% of content of peptides in the hydrolyzate of 1800U/g addition addition leucine amino peptidase.
Embodiment 5
First to add proline aminopeptidase, the order for adding leucine amino peptidase carries out enzyme digestion reaction, and other conditions are same
Embodiment 2.Amino acid content before and after enzymolysis is detected, and contrasted with the hydrolysis result of embodiment 2, as a result as schemed
Shown in 6, the water that phenylalanine and proline in the polypeptide solution of proline are below first adding leucine amino peptidase is first added
Liquid is solved, phenylalanine content is only 0.287mg/mL, and proline content is only 7.87 × 10-4mg/mL
Embodiment 6
Enzyme digestion reaction is carried out using different concentration of substrate, reaction temperature and enzymolysis time, as shown in Figure 7a, in aminopeptidase
Hydrophobic amino acid total amount of dissociating before enzymolysis in polypeptide is 0.4396mg/mL, adds hydrophobicity ammonia after leucine amino peptidase enzymolysis
Base acid is improved largely, and is reacted with 900~2100U/g enzyme concentration, when aminopeptidase amount addition less than 1800U/g or
During more than 2100U/g, hydrophobic amino acid content increase is slower.From Fig. 7 b, hydrophobic amino acid content is dense with substrate
Substantially, in the reaction when concentration of substrate is more than 50g/L, hydrophobic amino acid increment is 0.8mg/mL to the different differences of degree,
And concentration of substrate be 20g/L when, hydrophobic amino acid increment only 0.7mg/mL.From Fig. 7 c, hydrolysis temperature is 45~55 DEG C
When, clearly, when hydrolysis temperature is 50 DEG C, hydrophobic amino acid incrementss reach the increase of hydrophobic amino acid content
1.002mg/mL.When can be seen that enzymolysis time from Fig. 7 d for 3~6h, hydrophobic amino acid increment is all higher than 0.82mg/mL,
In 5~6h enzymolysis process, hydrophobic amino acid increment is more than 1.1mg/mL.
Although the present invention is disclosed as above with preferred embodiment, it is not limited to the present invention, any to be familiar with this skill
The people of art, without departing from the spirit and scope of the present invention, can do various changes and modification, therefore the protection model of the present invention
Enclose being defined of being defined by claims.
Claims (10)
1. a kind of take off bitter method to rice peptide, it is characterised in that the bright ammonia of 1600-2100U/g substrates is added into rice peptide
Sour aminopeptidase, 200-300U/g substrate prolines aminopeptidase or its combination, rice peptide is hydrolyzed.
2. according to the method described in claim 1, it is characterised in that the addition of the leucine amino peptidase is 1800~
2100U/g substrates；The addition of the proline aminopeptidase is 200-300U/g substrates.
3. according to the method described in claim 1, it is characterised in that the rice peptide concentration is 50~70g/L.
4. according to the method described in claim 1, it is characterised in that the hydrolysis is carried out at 40~60 DEG C.
5. according to the method described in claim 1, it is characterised in that the hydrolysis time is 3~6h.
6. according to the method described in claim 1, it is characterised in that the proline aminopeptidase is by recombined bacillus subtilis
What fermentation was produced, the recombined bacillus subtilis is using WB600 as host, using PMA5 as carrier, expresses pap genes.
7. method according to claim 6, it is characterised in that the proline aminopeptidase is prepared as follows obtaining
：Zymotic fluid after the recombined bacillus subtilis is fermented adjusts pH, adds flocculant flocculation, then carries out plate-frame filtering,
20~30KDa PES rolled films are concentrated by ultrafiltration, and freeze, and crush, and sieving obtains enzyme powder.
8. method according to claim 7, it is characterised in that regulation pH to 8.0, adds 1.5g/L cation flocculation
Agent, 25g/L diatomite, is stirred and evenly mixed.
9. method according to claim 7, it is characterised in that the plate-frame filtering is to use flame filter press, with 80~
100mL/min speed filtering；The ultrafiltration is to be concentrated by ultrafiltration 6~7 times with 20~30KDa PES rolled films.
10. application of any methods described of claim 1~9 in the product containing amino acid or polypeptide is prepared.
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN107400666A (en) * | 2017-09-11 | 2017-11-28 | 广东轻工职业技术学院 | A kind of aminopeptidase and its encoding gene and application |
| CN107760659A (en) * | 2017-11-30 | 2018-03-06 | 江南大学 | It is a kind of to recombinate proline aminopeptidase fermentation high yield and prepare the method for taking off bitter rice peptide |
| CN113584005A (en) * | 2021-08-27 | 2021-11-02 | 江南大学 | Preparation of aminopeptidase and application of aminopeptidase in protein debittering |
| CN114246934A (en) * | 2021-12-17 | 2022-03-29 | 吉林农业大学 | Synergistic active substance composition for protecting nerves and application thereof |
| CN114350643A (en) * | 2022-01-24 | 2022-04-15 | 江南大学 | Recombinant strain for producing aminopeptidase and application of recombinant strain in efficient proteolysis |
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Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN107400666A (en) * | 2017-09-11 | 2017-11-28 | 广东轻工职业技术学院 | A kind of aminopeptidase and its encoding gene and application |
| CN107400666B (en) * | 2017-09-11 | 2019-11-22 | 广东轻工职业技术学院 | A kind of aminopeptidase and its encoding gene and application |
| CN107760659A (en) * | 2017-11-30 | 2018-03-06 | 江南大学 | It is a kind of to recombinate proline aminopeptidase fermentation high yield and prepare the method for taking off bitter rice peptide |
| WO2019104761A1 (en) * | 2017-11-30 | 2019-06-06 | 江南大学 | Method for fermenting, highly producing, and preparing debittered rice peptide from recombinant prolyl aminopeptidase |
| CN107760659B (en) * | 2017-11-30 | 2020-08-04 | 江南大学 | Method for high yield of recombinant proline aminopeptidase through fermentation and preparation of debittered rice peptide |
| US10968440B2 (en) | 2017-11-30 | 2021-04-06 | Jiangnan University | Method for high-yield fermentation of recombinant proline aminopeptidase and preparation of debittered rice peptide |
| CN113584005A (en) * | 2021-08-27 | 2021-11-02 | 江南大学 | Preparation of aminopeptidase and application of aminopeptidase in protein debittering |
| CN113584005B (en) * | 2021-08-27 | 2024-03-01 | 江南大学 | Preparation of aminopeptidase and application of aminopeptidase in protein debittering |
| CN114246934A (en) * | 2021-12-17 | 2022-03-29 | 吉林农业大学 | Synergistic active substance composition for protecting nerves and application thereof |
| CN114246934B (en) * | 2021-12-17 | 2024-03-15 | 吉林农业大学 | Active substance composition for synergistically protecting nerves and application thereof |
| CN114350643A (en) * | 2022-01-24 | 2022-04-15 | 江南大学 | Recombinant strain for producing aminopeptidase and application of recombinant strain in efficient proteolysis |
| CN114350643B (en) * | 2022-01-24 | 2023-07-25 | 江南大学 | Recombinant strain for producing aminopeptidase and application of recombinant strain in efficient proteolysis |
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