CN110195048A - The method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property - Google Patents
The method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property Download PDFInfo
- Publication number
- CN110195048A CN110195048A CN201910311397.9A CN201910311397A CN110195048A CN 110195048 A CN110195048 A CN 110195048A CN 201910311397 A CN201910311397 A CN 201910311397A CN 110195048 A CN110195048 A CN 110195048A
- Authority
- CN
- China
- Prior art keywords
- pepsin
- pressure
- static pressure
- processing
- solution
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention discloses a kind of methods that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property, the following steps are included: 1. preparing the lactoalbumin soln of 10mg/mL, 5min is kept the temperature in 30-40 DEG C of water-bath, 2min is patted with sterile homogenizer middle-grade, is subsequently placed at the high-pressure homogeneous processing carried out under 150MPa flow regime in high pressure homogenizer；2. pepsin is dissolved in the phosphate buffer solution that pH is 1.9, temperature is 47 DEG C, pressure maintaining 15min carries out high static pressure processing under processing pressure 150MPa；3. the pepsin solution of high static pressure processing is added into the lactoalbumin soln of high-pressure homogeneous processing, adjusting pH value of solution is 2.0, is hydrolyzed 6 hours at 50 DEG C in constant temperature oscillator.Degree of hydrolysis, solid yield, DPPH free radical scavenging activity, reducing power and Hydroxyl radical-scavenging power can be improved in present invention building " lactalbumin of high-pressure homogeneous processing-high static pressure processing pepsin " hydrolyzation system, improves the application potential of lactalbumin.
Description
Technical field
The invention belongs to food processing technology fields, and in particular to one kind moves/Static pressure Combined Treatment promotion pepsin
The method of enzymolysis lactoalbumin product property.
Background technique
Lactalbumin is referred to as the king of albumen, is generally acknowledged one of human body good protein replenishers.Studies have shown that whey
Containing there are many plant biologically active peptide in protein molecular.Having for these active peptides is antibacterial, removes free radical, Scavenger of ROS, exempts from
The functions such as epidemic disease adjusting, these functionality can not play under native state, after only lactalbumin is hydrolyzed, can lead at this time
It causes intramolecular amido bond to be broken, and then induces and generate some amino acid sequences for having certain bioactivity, and only
Having in this way can be released the bioactivity in albumen.
However, many because being known as of protein hydrolysis are influenced, in addition to external factor such as hydrolysis temperature, pH, enzyme concentration, enzyme
The factor of solution time etc. process conditions there are also protein digestion sensibility protein such as low, hydrolysis is not thorough itself.There is research table
It is bright, denaturation treatment appropriate is carried out to it before digesting to protein, later by relevant means to its internal junction
Structure, which carries out processing, facilitates it in conjunction with enzyme, also contributes to the change of enzymolysis property in this way.And high pressure technique is as a kind of
Physical means have very strong application potential in this respect.For example, there is scholar to point out the three-level to protein, four by research
Level structure, which carries out HIGH PRESSURE TREATMENT, can cause the change of covalent bond, and then tend to the stretching, extension of protein loosely, while on protein
Face also shows more binding sites, this facilitates going on smoothly for enzyme digestion reaction.Same Morild etc. passes through research hair
It is existing, the activated centre of protein can be caused cohesion occur in the case where lower pressure, the reason of this situation occur has
It may be because the tertiary structure of inducible protein matter changes when pressure changes, and then causes to occur in its complete tissue mutual
The matrix and enzyme of isolation are in contact, and accelerate the progress of enzymatic reaction.But HIGH PRESSURE TREATMENT is carried out simultaneously to albumen and enzyme at present,
It is also rarely reported in the method for promoting enzymolysis efficiency.
Summary of the invention
The purpose of the present invention is using the lactalbumin through dynamic high-pressure homogenization and the stomach cardia handled through high static pressure
Enzyme constructs " lactalbumin-pepsin " hydrolyzation system, provides a kind of dynamic/Static pressure Combined Treatment promotion pepsin enzymatic hydrolysis cream
The method of albumin product property.
To achieve the above object, the technical solution adopted by the present invention is that, one kind moving/Static pressure Combined Treatment promotion stomach cardia
The method of enzyme enzymolysis lactoalbumin product property, comprising the following steps:
1. preparing the lactoalbumin soln of high-pressure homogeneous processing: the lactoalbumin soln of 10mg/mL is prepared with deionized water,
5min is kept the temperature in 30-40 DEG C of water-bath, patting 2min with sterile homogenizer middle-grade makes lactalbumin be well-dispersed in deionized water
In, it is subsequently placed at the high-pressure homogeneous processing carried out under 150 MPa flow regimes in high pressure homogenizer；
2. preparing the pepsin solution of high static pressure processing: it is 1.9 that the phosphate buffer solution of pH7.0, which is adjusted pH, with hydrochloric acid,
Then pepsin is dissolved in the phosphate buffer solution of pH1.9, temperature be 47 DEG C, pressure maintaining under 150 MPa of processing pressure
15min carries out high static pressure processing；
3. the step pepsin solution that 2. high static pressure is handled is added into the step 1. lactoalbumin soln of high-pressure homogeneous processing,
Adjusting pH value of solution is 2.0, obtains lactalbumin-pepsin system mixed solution, and hydrolysis 6 is small at 50 DEG C in constant temperature oscillator
When.
Preferably, 3. the lactoalbumin soln of mesohigh homogenization and the pepsin of high static pressure processing are molten for the step
The volume ratio of liquid is 5:1；The concentration of pepsin is 2.0mg/mL in the lactalbumin-pepsin system mixed solution.
The beneficial effect comprise that: lactalbumin can be significantly improved using the dynamic high-pressure homogenization of 150MPa
Dissolubility, foaming characteristic, emulsion stability and other function property；Using high static pressure processing porcine pepsin solution, it can be achieved that mentioning
The purpose of high peptic activity of stomach；Building " lactalbumin of high-pressure homogeneous processing-high static pressure processing pepsin " hydrolysis body
Degree of hydrolysis, solid yield, DPPH free radical scavenging activity, reducing power and Hydroxyl radical-scavenging power can be improved in system, improves cream
Albuminised application potential.
Detailed description of the invention
Fig. 1 is the influence of different enzyme concentrations (a), pH (b), temperature (c), enzymolysis time (d) to enzymolysis product degree of hydrolysis；
Fig. 2 is influence of the different disposal method to degree of hydrolysis；
Fig. 3 is influence of the different disposal method to solid yield；
Fig. 4 is influence of the different disposal method to enzymolysis product DPPH radicals scavenging power；
Fig. 5 is influence of the different disposal method to enzymolysis product reducing power；
Fig. 6 is the influence of different disposal method enzymolysis product Hydroxyl radical-scavenging power.
Specific embodiment
1.1 test materials and equipment
1.1.1 material and reagent porcine pepsin are purchased from Sigma-Aldrich；Lactalbumin is purchased from Shanghai source Ye Sheng
Object Science and Technology Ltd., it is other this experiment used in reagent grade be AR grades.
1.1.2 instrument and equipment
FPG5620YHL ultra high pressure treatment device, FPG12805 high pressure homogenizer: SFP company；Sterile homogenizer: Ningbo Xin Zhisheng
Object Science and Technology Co., Ltd.；Alpha1-2 LD plus vacuum freeze drier: German SIGMA company；TU-1810 type is ultraviolet
Spectrophotometer: Beijing Puxi General Instrument Co., Ltd；SHA-C digital display water-bath constant temperature oscillator: Jintan City, Jiangsu Province
Hua Feng Instrument Ltd.；PHS-3C type precision pH meter: Shanghai Lei Ci instrument plant.
1.2 test method
1.2.1 the measurement of peptic activity of stomach selects Folin phenol method to protease according to the method for SB/T 10317-1999
Enzyme activity is measured, wherein level of tyrosine y (μ g/mL) is used as ordinate, absorbance x is abscissa, carries out junket ammonia whereby
The drafting of acidity scale directrix curve, standard curve regression equation are y=103.33x-0.1181 (μ g/mL), R2It is 0.9979.
1.2.2 sample solution prepares the lactoalbumin soln of high-pressure homogeneous processing: the cream of 10mg/mL is prepared with deionized water
Albumin soln keeps the temperature 5min in 30-40 DEG C of water-bath, and patting 2min with sterile homogenizer middle-grade divides lactalbumin sufficiently
It dissipates in deionized water.It is subsequently placed at the high-pressure homogeneous processing that 150 MPa are carried out in high pressure homogenizer.
The porcine pepsin solution of high static pressure processing: it is 1.9 that the phosphate buffer solution of pH7.0, which is adjusted pH, with hydrochloric acid,
Then porcine pepsin is dissolved in after hydrochloric acid adjusts in the phosphate buffer solution of pH1.9, is 47 DEG C, processing pressure in temperature
Pressure maintaining 15min carries out high static pressure processing under 150MPa.
1.2.3 hydrolyzed whey protein process flow learn from else's experience high-pressure homogeneous processing lactoalbumin soln → addition through high static pressure
The pepsin solution of processing → adjusting pH value of solution → → 100 DEG C of water-bath enzyme deactivation 10min are hydrolyzed in constant temperature oscillator → is cooled to
Room temperature → freeze-drying process → collection enzymolysis liquid powder → index determining.
1.2.4 single factor experiment probes into enzyme additive amount (lactalbumin-pepsin system using degree of hydrolysis as testing index
The concentration of porcine pepsin in mixed solution, 0.5,1.0,1.5,2.0,2.5mg/ml), enzymolysis time (2,4,6,8,10h), enzyme
The influence of temperature (40,45,50,55,60 DEG C) and pH (1.0,1.5,2.0,2.5,3.0) to enzymolysis efficiency is solved, it is suitable to determine
Enzymatic hydrolysis condition.
1.2.5 the measurement of degree of hydrolysis takes 1mL lactalbumin enzymolysis liquid to be added in beaker, continues that 60ml is added to the inside later
Distilled water selects 0.05 M sodium hydroxide solution to titrate sample, while adjusting solution ph equal to 8.2.Continue to sample
Formalin 10ml is added in product, selects the sodium hydroxide solution of comparable sodium to be adjusted to solution ph after being mixed uniformly
9.2.Select distilled water that blank control experimental group is set at this time.The volume of sodium hydroxide consumed by recording, carries out according to following formula
The calculating (DH) of degree of hydrolysis.
In formula: V1: indicate that formaldehyde is added in sample carries out the volume (ml) that titration is the sodium hydroxide expended later
V2: indicate that formaldehyde is added in control group carries out the volume (ml) that titration is the sodium hydroxide expended later
C: the concentration (mol/L) of standardised sodium hydroxide is indicated
S: the concentration of substrate is represented
W: expression be the protein contained in sample content (being measured via Kjeldahl's method) (W=85.30)
Htot: indicate the peptide bond sum (H contained in proteintot=8.8 × 10meqv/g)
1.2.6 the measurement of lactalbumin enzymatic hydrolysis solid yield will be by pepsin-lactalbumin of different pre-treatments
It is hydrolyzed, the operation such as enzyme deactivation, centrifugation and filtering is then carried out to it, freeze-drying process is carried out to it after the completion, is taken at this time
Its enzymolysis liquid dry powder carries out the calculating of lactalbumin enzymatic hydrolysis yield.
1.2.7DPPH the enzymolysis liquid dry powder that the measurement of radicals scavenging power will prepare, is successively prepared into 2mg/
The enzymolysis liquid of ml.2ml enzymolysis liquid is weighed, DPPH (2 × 10 is added to the inside-4Mol/L) solution 2ml.It is set after mixing
In dark place 30min, its natural reaction is allowed, while selecting dehydrated alcohol as control.Solution is placed in progress sample suction at 517nm
Measurement (the A of light valueSample).At the same time, 2ml sample is selected, it is mixed with 2ml ethanol solution, is set 517nm item
Measurement (the A of blank control group light absorption value is carried out under partBlank).In addition, it is equal to take 2mlDPPH solution and 2ml ethanol solution to carry out
Even mixing places it at 517nm and carries out the measurement (A of control group absorbanceControl)。
1.2.8 the enzymolysis liquid dry powder 0.2mol/L phosphate buffer (pH6.6) produced is distinguished in the measurement of reducing power
The enzymolysis liquid for preparing 2mg/ml takes the potassium ferricyanide solution mixing of 2ml lactalbumin enzymolysis product solution, 2ml mass fraction 1%
It is cooled down rapidly after reacting 20min in 50 DEG C of water-baths after uniformly, while TCA solution (5%) 2ml is added to the inside.In r=
Centrifugally operated is carried out under the action of 3000r/min, takes 0.1% ferric chloride solution 0.5ml after solution centrifugation 10min.Continue later
2.5ml distilled water is added to the inside, solution stands 10min after mixing, and measures the light absorption value of solution, under the conditions of 700nm to inhale
Luminance representation reducing power.
1.2.9 the measurement precision of Hydroxyl radical-scavenging power weighs the Phen solution that 0.6ml concentration is 5mmol/L.To
The inside continuously adds the phosphate buffer solution (adjust pH=7.4) that 0.4ml concentration is 0.2mol/L, solution continue after mixing to
The EDTA solution that the enzymolysis liquid of 0.6ml various concentration is added in the inside and 0.6ml concentration is 15mmol/L, continuously adds after the completion
The hydrogen peroxide that 0.8ml mass fraction is 0.1%.Solution mixing is placed at 37 DEG C and keeps the temperature 1h, selects centrifuge (r=later
Centrifugation 10min 6000r/min) is carried out, a certain amount of supernatant is taken to place it at 536nm the measurement for carrying out sample absorbance
(ASample).The enzymolysis liquid of 0.6ml is successively substituted for 0.6ml distilled water also according to above-mentioned same step, carries out control group suction
Measurement (the A of luminosityControl).In addition by 0.8ml concentration be 0.1% hydrogen peroxide and 0.6ml by test solution select 1.4ml distilled water
It is replaced, measures the absorbance (A of blank sample groupBlank)。
1.3 results and analysis
1.3.1 pepsin enzymolysis lactoalbumin single factor experiment Fig. 1 is enzyme concentration, hydrolysis temperature, pH and enzymolysis time to enzyme
Solve product degree of hydrolysis influence (note:a-dDifferent letters indicate that there are significant difference (P < 0.05)).As shown in Figure 1, in enzyme concentration
When 2.0mg/ml, hydrolyzed whey protein degree is high value, and it is smaller to further increase influence of the enzyme concentration to degree of hydrolysis；When pH is
Hydrolyzed whey protein degree shows maximum value when 2.0, and when being more than this pH value, hydrolyzed whey protein degree declines rapidly；Certain
Temperature can promote the hydrolysis of lactalbumin, and with the raising of hydrolysis temperature, degree of hydrolysis is also increased, and when temperature is greater than 50
DEG C when, degree of hydrolysis declines rapidly；Enzymolysis time is more than after six hours, and the variation of hydrolyzed whey protein degree is not significant, it is possible thereby to point
It is precipitated, the convenient hydrolysising condition of pepsin enzymolysis lactoalbumin are as follows: enzyme concentration 2.0mg/ml, pH2.0, hydrolysis temperature 50
DEG C, enzymolysis time 6h.
1.3.2 move/Static pressure Combined Treatment to the influence diagram 2 of degree of hydrolysis be HIGH PRESSURE TREATMENT to degree of hydrolysis influence (note:a-d
Different letters indicate that there are significant difference (P < 0.05)), high-pressure homogeneous (P) only respectively is carried out to lactalbumin, only to stomach egg
White enzyme carries out high static pressure processing (E), high-pressure homogeneous to lactalbumin progress, while carrying out high static pressure processing (P+ to pepsin
E).As seen from the figure, with do not pressurize (0.1 MPa) sample compared with, the degree of hydrolysis of each sample has significantly after HIGH PRESSURE TREATMENT
It is promoted, and using the Combined Treatment group of two kinds of high pressure modes compared with single treatment group, degree of hydrolysis is obviously improved, reason
May be: (1) high static pressure processing directly affects the secondary structure and tertiary structure of pepsin, becomes its molecular structure
Change, changes the active site of enzyme, and the conformation change that the activated centre of enzyme molecule generates makes it easier for Binding Capacity；(2)
Lactalbumin is reaching the broken of height after high-pressure homogeneous processing, and partial size reduces, solubility improves, structure has occurred
Variation, to expose more pepsin binding sites.And dynamic/quiet Combined Treatment can be seen that by test result can
Effectively to promote the degree of hydrolysis of lactalbumin, effect is more preferable compared with for single treatment group.
1.3.3 influence solid yield usually quilt of the dynamic/Static pressure Combined Treatment to lactalbumin enzymatic hydrolysis solid yield
It can effectively reflect a mostly important index for protein digestion degree as one, Fig. 3 is different from processing method
To lactalbumin enzymolysis product solid yield influence (note:a-dDifferent letters indicate that there are significant difference (P < 0.05)).By
Fig. 3 is it is found that HIGH PRESSURE TREATMENT can promote the solid yield of enzymolysis product, and its effect is wanted using dynamic/Static pressure Combined Treatment
It is better than single treatment group.There is document to show the increase with protein hydrolysis degree, the small molecule contained inside enzymolysis liquid at this time
Segment can also increase with it, thus the soluble solid that includes of the lactalbumin enzymolysis product Jing Guo high pressure pre-treatment compared to
Control group is obviously improved, and dynamic/Static pressure Combined Treatment group its solid yield is also higher than single treatment group.
1.3.4/influence of the Static pressure Combined Treatment to enzymolysis product DPPH radicals scavenging power is moved
DPPH free radical usually contains 3 phenyl ring, and on phenyl ring as a kind of more stable free radical in its structure
One nitrogen-atoms has 1 lone pair electrons, and strong absorption can occur at 517nm in ethanol solution at this time.When addition free radical
After scavenger, the lone pair electrons of its DPPH can be matched at this time, and then cause its color to shoal, and solution colour
The depth and the electron number that matches in being closely related, so UV-vis is selected to carry out the inspection energy of absorbance at 517nm
It is enough effectively to reflect that there is a situation where remove for free radical.Then indicate the difference of processing method to enzymolysis product in lower Fig. 4
DPPH free radical Scavenging activity (note:a-cDifferent letters indicate that there are significant difference (P < 0.05)).In analysis chart data we
It can be found that lactalbumin enzymolysis product has stronger removing for the free radical at this time after passing through HIGH PRESSURE TREATMENT
Ability (p < 0.05).In addition, its enzymolysis product imitates the removing of DPPH free radical after selecting dynamic/venous hypertension Combined Treatment
Fruit is more preferable compared with single group of processing.As it can be seen that variation of the HIGH PRESSURE TREATMENT to lactalbumin enzymolysis product DPPH radicals scavenging power
It is more similar to degree of hydrolysis, this is because certain specific amino acid sequences of the antioxidant activity of enzymolysis product and protein itself
Very close connection is shown, as the increase of degree of hydrolysis may be such that corresponding amino acid content in enzymolysis product increases, into
And the ability for promoting DPPH to remove free radical gets a promotion.
1.3.5 dynamic/influence reducing power of the Static pressure Combined Treatment to enzymolysis product reducing power is usually by the way that enzyme is being added
According to the inside Fe after solution product system2+-Fe3+There is a situation where convert to verify.Due to the reduction meeting of enzymolysis product itself
For electron and then it is caused to play antioxidation, the reducing power that thus sample contains and its oxidation resistance are in positive
Pass relationship, and according to this characteristic, we can be tested by the reducing power to sample come the anti-oxidant work of judgement sample
Property.Fig. 5 be different disposal method to enzymolysis product reducing power influence (note:a-cDifferent letters indicate there are significant difference (P <
0.05)).As shown in Figure 5, after HIGH PRESSURE TREATMENT, the reducing power of albumen processing group is obviously improved (p < 0.05), and enzymatic treatment group
Then without significant changes, dynamic/Static pressure Combined Treatment group compares albumen processing group then small size rising.
1.3.6 dynamic/influence of the Static pressure Combined Treatment to enzymolysis product Hydroxyl radical-scavenging power is because hydroxy radical has
Very active chemical property is in known active oxygens all at present to the maximum free radical of organismal toxicity, and hydroxy radical can
In a manner of through electronics transfer, addition etc. for example with biomolecule important in organism: carbohydrate, protein, amino acid, lipid
And the substances such as nucleic acid, to cause the oxidative damage of these substances, cause bio-tissue damage or cell bad to combination
Extremely, it is mutated.From lower Fig. 6 we can be found that processing method difference can to enzymolysis product Hydroxyl radical-scavenging ability generate compared with
For significantly influence (note:a-cDifferent letters indicate that there are significant difference (P < 0.05)).We are it can be found that through excessively high from figure
After pressure processing, the Hydroxyl radical-scavenging power of lactalbumin enzymolysis product is significantly improved (p < 0.05), and uses dynamic/Static pressure
Its effect of combination processing group is better than single treatment group.It can be seen that lactalbumin enzymolysis product has stronger Hydroxyl radical-scavenging energy
Power.
Claims (3)
1. the method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property, it is characterised in that including
Following steps:
1. preparing the lactoalbumin soln of high-pressure homogeneous processing: the lactoalbumin soln of 10mg/mL is prepared with deionized water,
5min is kept the temperature in 30-40 DEG C of water-bath, patting 2min with sterile homogenizer middle-grade makes lactalbumin be well-dispersed in deionized water
In, it is subsequently placed at the high-pressure homogeneous processing carried out under 150MPa flow regime in high pressure homogenizer；
2. preparing the pepsin solution of high static pressure processing: being 1.9 by phosphate buffer solution salt acid for adjusting pH, then by stomach
Protease is dissolved in phosphate buffer solution, temperature is 47 DEG C, pressure maintaining 15min is carried out at high static pressure under processing pressure 150MPa
Reason；
3. the pepsin solution of high static pressure processing is added into the lactoalbumin soln of high-pressure homogeneous processing, adjusting pH value of solution is
2.0, it obtains lactalbumin-pepsin system mixed solution, is hydrolyzed 6 hours at 50 DEG C in constant temperature oscillator.
2. the method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property as described in claim 1,
It is characterized by: the step pepsin solution that 3. lactoalbumin soln of mesohigh homogenization and high static pressure are handled
Volume ratio is 5:1.
3. the method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property as described in claim 1,
It is characterized by: the concentration of pepsin is 2.0mg/mL in the lactalbumin-pepsin system mixed solution.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910311397.9A CN110195048B (en) | 2019-04-18 | 2019-04-18 | Method for improving performance of pepsin enzymatic hydrolysis whey protein product through dynamic/static high-pressure combined treatment |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910311397.9A CN110195048B (en) | 2019-04-18 | 2019-04-18 | Method for improving performance of pepsin enzymatic hydrolysis whey protein product through dynamic/static high-pressure combined treatment |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN110195048A true CN110195048A (en) | 2019-09-03 |
| CN110195048B CN110195048B (en) | 2022-11-11 |
Family
ID=67752032
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201910311397.9A Active CN110195048B (en) | 2019-04-18 | 2019-04-18 | Method for improving performance of pepsin enzymatic hydrolysis whey protein product through dynamic/static high-pressure combined treatment |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN110195048B (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115005337A (en) * | 2022-07-08 | 2022-09-06 | 睿迪生物科技（深圳）有限公司 | Special artificial milk for piglet in sterility test and preparation method thereof |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103160558A (en) * | 2011-12-13 | 2013-06-19 | 中国农业科学院农产品加工研究所 | Method for preparing lactalbumin hydrolysate |
| CN105316305A (en) * | 2015-11-17 | 2016-02-10 | 河南科技学院 | Method for improving pepsin activity through high pressure processing |
| CN108244330A (en) * | 2018-01-16 | 2018-07-06 | 河南科技学院 | The method that high-pressure microfluidization processing is modified lactalbumin |
-
2019
- 2019-04-18 CN CN201910311397.9A patent/CN110195048B/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103160558A (en) * | 2011-12-13 | 2013-06-19 | 中国农业科学院农产品加工研究所 | Method for preparing lactalbumin hydrolysate |
| CN105316305A (en) * | 2015-11-17 | 2016-02-10 | 河南科技学院 | Method for improving pepsin activity through high pressure processing |
| CN108244330A (en) * | 2018-01-16 | 2018-07-06 | 河南科技学院 | The method that high-pressure microfluidization processing is modified lactalbumin |
Non-Patent Citations (6)
| Title |
|---|
| A. LAURENCE CURL AND EUGENE F. JANSEN: "THE EFFECT OF HIGH PRESSURES ON PEPSIN AND CHYMOTRYPSINOGEN", 《ENZYME RESEARCH DIVISION CONTRIBUTION》 * |
| BOEN YUAN ET AL.: "Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate", 《FOOD SCIENCE AND TECHNOLOGY》 * |
| BRUNO RICARDO DE CASTRO LEITE JÚNIOR ET AL.: "High Pressure Homogenization of Porcine Pepsin Protease: Effects on Enzyme Activity，Stability, Milk Coagulation Profile and Gel Development", 《PLOS ONE》 * |
| JIANANWANG ET AL.: "Effect of High-Pressure Treatment on Catalytic and Physicochemical Properties of Pepsin", 《MOLECULES》 * |
| MICHÈLE M. ISKANDAR ET AL.: "High Hydrostatic Pressure Pretreatment of Whey Protein Isolates Improves Their Digestibility and Antioxidant Capacity", 《FOODS》 * |
| 白腾辉: "高压处理促进胃蛋白酶酶解酪蛋白机制研究", 《中国优秀硕士学位论文全文数据库(电子期刊)工程科技I辑》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115005337A (en) * | 2022-07-08 | 2022-09-06 | 睿迪生物科技（深圳）有限公司 | Special artificial milk for piglet in sterility test and preparation method thereof |
| CN115005337B (en) * | 2022-07-08 | 2024-02-27 | 睿迪生物科技（深圳）有限公司 | Special artificial milk for aseptic experiment young pigs and preparation method thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| CN110195048B (en) | 2022-11-11 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Zhao et al. | Effects of collagen and casein with phenolic compounds interactions on protein in vitro digestion and antioxidation | |
| Jiang et al. | Mechanisms of change in gel water-holding capacity of myofibrillar proteins affected by lipid oxidation: The role of protein unfolding and cross-linking | |
| Xie et al. | Real meat and plant-based meat analogues have different in vitro protein digestibility properties | |
| Alizadeh-Pasdar et al. | Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes | |
| Feng et al. | Changes of in vitro digestion rate and antioxidant activity of digestion products of ethanol-modified whey protein isolates | |
| Fang et al. | Characterization and antioxidant properties of Manchurian walnut meal hydrolysates after calcium chelation | |
| CN105777865B (en) | Fish digestion-resistant peptide with antioxidant function, and preparation method and application thereof | |
| CN107557422A (en) | A kind of cottonseed protein polypeptide with high ACE inhibitory activity and preparation method thereof | |
| CN108949874A (en) | Rice gluten peptide-calcium chelate preparation method | |
| CN108276489A (en) | Collagen and preparation method thereof, application | |
| He et al. | Improved functional properties of wheat gluten hydrolysate by covalent conjugation with chlorogenic acid | |
| Li et al. | Interaction of myofibrillar proteins and epigallocatechin gallate in the presence of transglutaminase in solutions | |
| Fan et al. | Purification, identification and molecular docking of novel antioxidant peptides from walnut (Juglans regia L.) protein hydrolysates | |
| Chen et al. | Underlying mechanisms of egg white thinning in hot spring eggs during storage: Weak gel properties and quantitative proteome analysis | |
| Patil et al. | Enhancing Zinc Uptake through Dual‐Modification of Cicer arietinum Protein | |
| CN113061178A (en) | Preparation method of sika deer skin collagen and collagen peptide | |
| Chen et al. | Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation | |
| Gazikalović et al. | Synergistic effect of enzyme hydrolysis and microwave reactor pretreatment as an efficient procedure for gluten content reduction | |
| CN110195048A (en) | The method that dynamic/Static pressure Combined Treatment promotes pepsin enzymolysis lactoalbumin product property | |
| Wang et al. | Effects of glycation with chitooligosaccharide on digestion and fermentation processes of lactoferrin in vitro | |
| CN109680027A (en) | A kind of grifola frondosus small peptide iron chelate and its preparation method and application | |
| Pan et al. | Anti‐fatigue and antioxidative activities of peptides isolated from milk proteins | |
| WANG et al. | Antioxidant activity of hydrolysates and peptide fractions of porcine plasma albumin and globulin | |
| Zhang et al. | Study on the in vitro digestion process of green wheat protein: Structure characterization and product analysis | |
| Ma et al. | Yeast protein as a novel dietary protein source: Comparison with four common plant proteins in physicochemical properties |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |