CN107212151A - A kind of method of deamidation modification of wheat flour gluten protein - Google Patents
A kind of method of deamidation modification of wheat flour gluten protein Download PDFInfo
- Publication number
- CN107212151A CN107212151A CN201710499594.9A CN201710499594A CN107212151A CN 107212151 A CN107212151 A CN 107212151A CN 201710499594 A CN201710499594 A CN 201710499594A CN 107212151 A CN107212151 A CN 107212151A
- Authority
- CN
- China
- Prior art keywords
- deamidation
- gluten protein
- protein
- wheat
- modification
- 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.)
- Pending
Links
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
- A23J3/18—Vegetable proteins from wheat
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Cereal-Derived Products (AREA)
Abstract
The invention belongs to wheat gluten protein processing technique field, it is related to a kind of method of utilization food grade protein glutaminase deamidation modification of wheat flour gluten protein, wheat gluten protein is added while stirring 3% 12% are configured into phosphate buffer（w/v）Protein suspending liquid, adds the deamidation modification under PH neutrallty conditions of food-grade glutaminase, and ice bath cooling removes salt ion, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein through acetum dialysis.The method of the food grade protein glutaminase deamidation modification of wheat flour gluten protein of the present invention, technique is simple, production cost is significantly reduced, can large-scale industrial production application, and low compared with albuminous degeneration degree, product solubility is significantly improved, surface hydrophobic makes moderate progress, deamidation degree is up to 40%, and solubility reaches 27.30%, and degree of hydrolysis is 6.67%.
Description
Technical field
The invention belongs to wheat gluten processing technique field, and in particular to a kind of food-grade glutaminase deamidation is modified
The method of wheat gluten protein.
Background technology
Wheat gluten protein is commonly called as Gluten, is byproduct when producing wheaten starch.Wheat gluten protein abundance,
It is of high nutritive value, has a wide range of application, with higher economic value.Because wheat gluten protein has one disadvantage in that itself, i.e.,
Low-solubility.And it is electric charge rate to control the main factor of solubility（charge frequeney）And hydrophobicity
（hydrophobicity）.Deamidation modification can change protein charge distribution, obtain protein molecule space structure
To stretching, extension, improve its hydrophobicity, the dissolubility of final increase protein makes protein obtain good functional characteristic, so as to open up
Its wide application.
It is change wheat gluten protein dissolubility and surface characteristic most promising that Matsudomi, which points out that deamidation is modified,
Method.At present, the method that protein deamidation is modified mainly has non-enzyme process, enzyme process, mixing deamidation method.The non-enzyme process of protein
Deamidation, which is modified, includes Physical and chemical method, wherein, Physical can be divided into wet heating and twin-screw extruder method, and chemical method has temperature
It is modified with acid, alkali, salt.Being used for the enzyme of enzymatic deamidation in report at present mainly has transglutaminase（TG enzymes）, protease, peptide
Glutaminase and glutaminase（PG enzymes）.Initially with transglutaminase（TG enzymes）, protease and peptide glutamine
Enzyme carries out deamidation, protein is also produced some side effects while occurring deamidation reaction, and PG enzyme deamidations
It is modified more advantageous in terms of selectivity, mildness and security compared with other enzyme deamidation method of modifying.
In recent years, domestic and foreign scholars carried out deamidation modification using protein glutaminase to protein, wherein
The protein of most study is the vegetable proteins such as soybean protein, avenin, oryzenin, wheat gluten protein, zein.
Inthawoot Suppavorasatit et al. use protein glutaminase（Amano 500）Soybean protein is taken off
Amide-treated, and have studied the influence to its functional character；Zhong-qing Jiang et al. have studied food grade protein paddy
Transglutaminase（Amano 50）Influence to avenin dissolubility and emulsibility；Yie Hui Yong et al. have studied protein
Glutaminase（Purified from Chryseobacterium proteolyticum）To α-zein structure and functional character
Influence；N.Miwa et al. is using the protein glutamine purified from Chryseobacterium proteolyticum
Enzyme studies its influence to skim milk albumen physicochemical property and functional character.Glutaminase deamidation is being carried out to protein
In the research of processing, the source of protein glutaminase substantially has three kinds：A kind of is to utilize the microorganism for producing glutaminase
（Such as Chryseobacterium proteolyticum）Extract, purifying obtains making glutaminase, the paddy ammonia that the method is obtained by oneself
Acid amides enzyme component and enzymatic activity have certain unstability, require higher to extraction process；Second is the pure level of purchase analysis
Other commercial enzyme（Such as the protein glutaminase of Sigma companies）, the enzyme is expensive, be not suitable for it is large-scale industrialized should
With；The third is purchase food-grade albumen enzyme glutaminase, compared to analysis true protein glutamine commercial enzyme, food-grade
Protein glutaminase cost is greatly reduced, and has great importance for industrialized production and application.And food is used at present
The correlative study that level protein glutaminase carries out deamidation modification to wheat gluten protein rarely has people's report.
The content of the invention
Present invention aims at provide a kind of method of deamidation modification of wheat flour gluten protein.
To achieve the above object, the technical scheme that provides of the present invention is：A kind of side of deamidation modification of wheat flour gluten protein
Method, comprises the following steps：
The first step：Prepare protein dispersion
Wheat gluten protein is scattered in the wheat gluten protein suspension for obtaining that mass volume ratio is 3 ~ 12% in phosphate buffer
Liquid；
Second step：Deamidation is reacted
Food-grade glutaminase is added into the wheat gluten protein dispersion liquid and carries out deamidation processing, then cooling is obtained
Wheat gluten protein deamidation treatment fluid；
3rd step：Dialysis
The wheat gluten protein deamidation treatment fluid is dialysed in acetum and obtains wheat gluten protein to remove salt ion
Deamidation refined solution；
4th step：It is lyophilized
Vacuum freeze drying is carried out to the wheat gluten protein deamidation refined solution and obtains deamidation modification of wheat flour gluten protein.
It is preferred that technical scheme be：In second step, the deamidation processing is carried out in the case where pH value is neutrallty condition, described
Cooling is that 10-15min is carried out in ice bath.
It is preferred that technical scheme be：In second step, the enzyme food-grade glutaminase is with wheat gluten protein ratio
10U/g-40U/g。
It is preferred that technical scheme be：The dialysis is carried out in 0.1M acetum, and dialyse 12h at 4 DEG C, is changed per 2h
The once acetum.
It is preferred that technical scheme be：In second step, the temperature conditionss of the deamidation processing are 30-60 DEG C, described de-
Amide-treated is carried out on shaking table, and the rotating speed of the shaking table is 80rpm-110rpm, and the reaction time of the deamidation processing is
6-30h。
It is preferred that technical scheme be：In the first step, delay in wheat gluten protein is scattered in into phosphate under stirring condition
Fliud flushing, the concentration of the phosphate buffer is 200mmol/L, and the time of the stirring is 20-30min.
It is preferred that technical scheme be：In the 4th step, the condition of the vacuum freeze drying is：Temperature is -55 DEG C, vacuum
Spend for 42Pa, drying time is 30h.
Because above-mentioned technical proposal is used, the present invention this have the advantage that compared with prior art：
1st, the raw material system wheat gluten protein that present invention process is used, accessory substance when it is production wheaten starch, wide material sources,
It is cheap, it is a kind of nutritious, edible safety plant protein source.
2nd, the present invention carries out deamidation processing using the protein glutaminase of food-grade to wheat gluten protein, compares
Compared with other enzymes, on the premise of glutaminase deamidation effect is ensured, cost is reduced, wheat gluten protein is accelerated in food
The industrialized production and application in product field.
3rd, prior art is modified to wheat gluten protein deamidation and uses physical chemistry method more, there is physical modification method modification
Effect is not notable；Chemical modification method reaction condition is violent, it is more difficult to control, and product it is dangerous the problems such as, glutaminase compared with
Other enzyme deamidation method of modifying are more advantageous in terms of selectivity, mildness and security.
4th, method of the invention, which is adopted, is cooled with an ice bath 10-15min to suppress PG enzymatic activitys, and albumen is made compared with conventional method
Denaturation degrees minimumization.
5th, protein glutaminase deamidation makes wheat gluten protein structure become loose, is hidden in inside protein molecule
Hydrophobic region exposure, protein structure become more flexibly, surface hydrophobic is dramatically increased.
6th, the wheat gluten protein product that this method is obtained, solubility is significantly improved, and deamidation is handled in neutral conditions
18h wheat gluten protein sample solubilities reach 27.27%, are 3 times of original untreated wheat gluten protein sample solubility
（Original untreated wheat gluten protein sample solubility is 9%）.
7th, the wheat gluten protein product that this method is obtained, surface hydrophobic significantly improves, during deamidation processing 24h
Surface hydrophobic is 3 times of untreated samples, is 2.3 times of blank group（Wherein deamidation processing 24h sample surfaces hydrophobicitys be
362.9, untreated blank group sample surfaces hydrophobicity is 121.8, and control sample surface hydrophobic is 158）.
8th, whole technological operation is simple, it is easy to grasp, relatively low to equipment requirement, it is easy to industrialization production.
Embodiment
Embodiments of the present invention are illustrated by particular specific embodiment below, those skilled in the art can be by this explanation
Content disclosed by book understands other advantages and effect of the present invention easily.
The detection method of the present invention includes：
1st, the measure of deamidation degree：Micro disperse ware method
The content for the ammonia that the complete deamidation of sample is produced：The accurate 0.5g wheat gluten proteins that weigh are placed in hydrolysis pipe, then to its
5ml 2mol/L HCl is added, sealing is vacuumized, 4h is hydrolyzed under the conditions of 115 DEG C -121 DEG C, cooling is taken out after having hydrolyzed, beats
Glass tube is driven, with 20g/L boric acid absorbed nitrogen and acid amides nitrogen content is determined.
The content of the ammonia produced during sample deamidation：3ml 20g/L boron is added in the center of health Wei Shi diffusion boats
Simultaneously 10 drop left and right coeruleum bromocresolis-methyl red comprehensive indicators are added dropwise in acid, and ware periphery adds 1ml protein samples, and ware edge is uniformly applied
Vaseline is smeared, glass cover is covered, and leaves a fixed gap, saturation is added to the ware periphery for having added sample by the space that reserves
NaOH solution 3ml, immediately seals up glass cover and avoids gas leakage, places after 12h, is titrated to 0.02M HCl mixed at room temperature
Close indicator terminal.
2nd, the measure of solubility：Forint phenol reagent process
Accurately weigh lyophilized wheat gluten protein sample 1mg to be placed in micro centrifugal pipe, be scattered in the buffering of 1ml different PHs
In liquid（10mmol/L, PH=3 acetate buffer；10mmol/L, PH=5 acetate buffer；10mmol/L, PH=7
Phosphate buffer）, every group of sample solution be placed in 20 DEG C under the conditions of overnight, after 10 DEG C, under the conditions of 3000rpm centrifuge
10min, collects soluble fraction, the protein content in supernatant is measured using Forint phenol method.
Forint phenol reagent process sample is determined：Take 1ml sample solutions to add 5ml reagents first to mix, in 20-25 DEG C of placement
10min, then add 0.5ml reagent second, shake up immediately, 30min is incubated at 20-25 DEG C, then the colorimetric at 500nm wavelength, with 1ml
Distilled water does blank control instead of sample.
3rd, the measure of degree of hydrolysis：Formol titration
Take the wheat gluten protein hydrolyzates of 2ml after modified to be marked in 3 in number 100ml triangular flasks respectively, add respectively
Enter 5ml distilled water and 1% phenolphthalein solution 3 drips, shake up.It is extremely in micro- red that solution in No. three bottle is titrated with 0.1mol/L NaOH solutions
Color, is used as endpoint criterion and the V that takes reading2, the mixing of 2ml neutral formalins solution is separately added into No. first and second bottles, then
With standard NaOH solution be titrated to it is identical with solution colour in No. three bottles untill, take reading, obtain average value V1, count as the following formula
Calculate degree of hydrolysis.
Free amino nitrogen（mg/ml）=NNaOH×(V1- V2) ×14/2
Hydrolysis degree DH（%）=free amino nitrogen × supernatant volume × 10-3/（Sample size × total nitrogen content）×100%
The measure of surface hydrophobic：Accurately 400mg PG ferment treatment wheat gluten protein sample dispersions are weighed in 15ml's
In the phosphate buffer of 10mmol/L PH=7, centrifuge 10min under the conditions of 8000rpm, 15 DEG C, Supernatant protein concentration by
Coomassie Brilliant Blue is measured.Supernatant is diluted to several different concentration gradients（1 times, 0.75 times, 0.5 times, 0.25 times,
0.125 times）, then take 40 μ L ANS reagents（8mmol/L）It is added in 4ml protein solution, selective exitation wavelength 365nm, sends out
The long 484nm of ejected wave, curve is done with fluorescence intensity to protein concentration, and the slope that most starts of curve is defined as being detected sample
Surface hydrophobicity degree.
4th, the measure of Supernatant protein concentration：Coomassie Brilliant Blue
Pipette samples solution 1ml is put into test tube, is added 5ml Coomassie Brillant Blue solutions, is shaken up, and is placed 3min or so, is waited reaction
After the completion of, absorbance is determined at 595nm, sample solution protein content is obtained by bovine serum albumin standard curve.
Embodiment one：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 7% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 30min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=10U/g, are placed in shaking table, rotating speed 80rpm, change in 40 DEG C of deamidations
Property reaction 12h, reaction terminate after immediately ice bath cooling 10min, PG ferment treatments liquid through 0.1M acetums dialyse 12h, per 2h more
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein sample.
Vacuum freeze drying condition is：- 55 DEG C, vacuum 42Pa, drying time is 30h.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 52.48%, and degree of hydrolysis is 3.64%.
Embodiment two：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 5% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 20min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=40U/g, are placed in shaking table, rotating speed 80rpm, change in 40 DEG C of deamidations
Property reaction 30h, reaction terminates rear ice bath cooling 10min, and PG ferment treatments liquid is dialysed 12h through 0.1M acetums, and one is changed per 2h
Secondary dialyzate, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 53.40%, and degree of hydrolysis is 8.34%.
Embodiment three：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 5% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 20min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=20U/g, are placed in shaking table, rotating speed 110rpm, de- in 40 DEG C of conditions
Amide modifications react 12h, and reaction terminates rear ice bath cooling 15min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, per 2h
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 29.59%, and degree of hydrolysis is 3.20%.
Example IV：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 12% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 30min after formed protein suspending liquid, add
Food-grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=10U/g, are placed in shaking table, rotating speed 110rpm, in 40 DEG C of conditions
Deamidation modified-reaction 1h, reaction terminates rear ice bath cooling 10min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, per 2h
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 15.97%, and degree of hydrolysis is 1.79%.
Embodiment five：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 7% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 20min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=10U/g, are placed in shaking table, rotating speed 80rpm, in 60 DEG C of condition deacylations
Amine modified-reaction 12h, reaction terminates rear ice bath cooling 15min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, and every 2h is more
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 78.40%, and degree of hydrolysis is 7.28%.
Embodiment six：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 7% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 20min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=10U/g, are placed in shaking table, rotating speed 80rpm, in 30 DEG C of condition deacylations
Amine modified-reaction 12h, reaction terminates rear ice bath cooling 10min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, and every 2h is more
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 38.71%, and degree of hydrolysis is 1.49%.
Embodiment seven：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 5% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 30min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=20U/g, are placed in shaking table, rotating speed 110rpm, de- in 40 DEG C of conditions
Amide modifications react 24h, and reaction terminates rear ice bath cooling 15min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, per 2h
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 41.84%, and degree of hydrolysis is 7.23%, surface hydrophobic
For 362.9（Wherein original untreated wheat gluten protein surface hydrophobic is 121.8, control group wheat gluten protein sample table
Face hydrophobicity is 158）.
Embodiment eight：A kind of method of deamidation modification of wheat flour gluten protein
A certain amount of wheat gluten protein is weighed, adds fill phosphate buffer while stirring（200 mmol/L, PH=7）'s
In reactor, it is 5% to be configured to concentration（w/v）Wheat gluten protein liquid, stirring 30min after formed protein suspending liquid, add food
Grade PG enzymes stir to form system of the enzyme-to-substrate than E/S=20U/g, are placed in shaking table, rotating speed 110rpm, de- in 40 DEG C of conditions
Amide modifications react 18h, and reaction terminates rear ice bath cooling 15min, and PG ferment treatments liquid is through 0.1M acetums dialysis 12h, per 2h
A dialyzate is changed, vacuum freeze drying obtains deamidation modification of wheat flour gluten protein.
Vacuum freeze drying condition be the same as Example 1.
The deamidation degree for detecting deamidation modification of wheat flour gluten protein is 38.20%, and degree of hydrolysis is 6.67%, and solubility is
27.30%, surface hydrophobic is 374.9（Wherein original untreated wheat gluten protein solubility is 11.43%, surface hydrophobic
For 121.8；Control group wheat gluten protein sample solubility is 9%, and surface hydrophobic is 158）.
Embodiment nine：A kind of method of deamidation modification of wheat flour gluten protein
A kind of method of deamidation modification of wheat flour gluten protein, it is characterised in that：Comprise the following steps：
The first step：Prepare protein dispersion
Wheat gluten protein is scattered in the wheat gluten protein suspension for obtaining that mass volume ratio is 8% in phosphate buffer；
Second step：Deamidation is reacted
Food-grade glutaminase is added into the wheat gluten protein dispersion liquid and carries out deamidation processing, then cooling is obtained
Wheat gluten protein deamidation treatment fluid；
3rd step：Dialysis
The wheat gluten protein deamidation treatment fluid is dialysed in acetum and obtains wheat gluten protein to remove salt ion
Deamidation refined solution；
4th step：It is lyophilized
Vacuum freeze drying is carried out to the wheat gluten protein deamidation refined solution and obtains deamidation modification of wheat flour gluten protein.
In second step, the deamidation processing is carried out in the case where pH value is neutrallty condition, and the cooling is entered in ice bath
Row 10min.
In second step, the enzyme food-grade glutaminase is 40U/g with wheat gluten protein ratio.
4th, the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：The dialysis
Carried out in 0.1M acetum, dialysed 12h at 4 DEG C, and the once acetum is changed per 2h.
5th, the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In second step
In, the temperature conditionss of the deamidation processing are 60 DEG C, and the deamidation processing is carried out on shaking table, and the rotating speed of the shaking table is
100rpm, the reaction time of the deamidation processing is 20h.
6th, the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In the first step
In, in wheat gluten protein is scattered in into phosphate buffer under stirring condition, the concentration of the phosphate buffer is
200mmol/L, the time of the stirring is 25min.
7th, the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In the 4th step
In, the condition of the vacuum freeze drying is：Temperature is -55 DEG C, and vacuum is 42Pa, and drying time is 30h.
Embodiment ten：A kind of method of deamidation modification of wheat flour gluten protein
A kind of method of deamidation modification of wheat flour gluten protein, it is characterised in that：Comprise the following steps：
The first step：Prepare protein dispersion
Wheat gluten protein is scattered in the wheat gluten protein suspension for obtaining that mass volume ratio is 12% in phosphate buffer
Liquid；
Second step：Deamidation is reacted
Food-grade glutaminase is added into the wheat gluten protein dispersion liquid and carries out deamidation processing, then cooling is obtained
Wheat gluten protein deamidation treatment fluid；
3rd step：Dialysis
The wheat gluten protein deamidation treatment fluid is dialysed in acetum and obtains wheat gluten protein to remove salt ion
Deamidation refined solution；
4th step：It is lyophilized
Vacuum freeze drying is carried out to the wheat gluten protein deamidation refined solution and obtains deamidation modification of wheat flour gluten protein.
In second step, the deamidation processing is carried out in the case where pH value is neutrallty condition, and the cooling is entered in ice bath
Row 12min.
In second step, the enzyme food-grade glutaminase is 25U/g with wheat gluten protein ratio.
The dialysis is carried out in 0.1M acetum, and dialysed 12h at 4 DEG C, and the once acetum is changed per 2h.
In second step, the temperature conditionss of the deamidation processing are 45 DEG C, and the deamidation processing is carried out on shaking table,
The rotating speed of the shaking table is 80, and the reaction time of the deamidation processing is 30h.
In the first step, in wheat gluten protein is scattered in into phosphate buffer under stirring condition, the phosphate-buffered
The concentration of liquid is 200mmol/L, and the time of the stirring is 25min.
In the 4th step, the condition of the vacuum freeze drying is：Temperature is -55 DEG C, and vacuum is 42Pa, drying time
For 30h.
The above-described embodiments merely illustrate the principles and effects of the present invention, not for the limitation present invention.It is any ripe
Know the personage of this technology all can carry out modifications and changes under the spirit and scope without prejudice to the present invention to above-described embodiment.Cause
This, those of ordinary skill in the art is complete without departing from disclosed spirit and institute under technological thought such as
Into all equivalent modifications or change, should by the present invention claim be covered.
Claims (7)
1. a kind of method of deamidation modification of wheat flour gluten protein, it is characterised in that：Comprise the following steps：
The first step：Prepare protein dispersion
Wheat gluten protein is scattered in the wheat gluten protein suspension for obtaining that mass volume ratio is 3 ~ 12% in phosphate buffer
Liquid；
Second step：Deamidation is reacted
Food-grade glutaminase is added into the wheat gluten protein dispersion liquid and carries out deamidation processing, then cooling is obtained
Wheat gluten protein deamidation treatment fluid；
3rd step：Dialysis
The wheat gluten protein deamidation treatment fluid is dialysed in acetum and obtains wheat gluten protein to remove salt ion
Deamidation refined solution；
4th step：It is lyophilized
Vacuum freeze drying is carried out to the wheat gluten protein deamidation refined solution and obtains deamidation modification of wheat flour gluten protein.
2. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In second step,
The deamidation processing is carried out in the case where pH value is neutrallty condition, and the cooling is that 10-15min is carried out in ice bath.
3. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In second step,
The enzyme food-grade glutaminase is 10U/g-40U/g with wheat gluten protein ratio.
4. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：The dialysis exists
Carried out in 0.1M acetum, dialysed 12h at 4 DEG C, and the once acetum is changed per 2h.
5. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In second step,
The temperature conditionss of the deamidation processing are 30-60 DEG C, and the deamidation processing is carried out on shaking table, and the rotating speed of the shaking table is
80rpm-110rpm, the reaction time of the deamidation processing is 6-30h.
6. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In the first step,
In wheat gluten protein is scattered in into phosphate buffer under stirring condition, the concentration of the phosphate buffer is 200mmol/L,
The time of the stirring is 20-30min.
7. the method for deamidation modification of wheat flour gluten protein according to claim 1, it is characterised in that：In the 4th step,
The condition of the vacuum freeze drying is：Temperature is -55 DEG C, and vacuum is 42Pa, and drying time is 30h.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201710499594.9A CN107212151A (en) | 2017-06-27 | 2017-06-27 | A kind of method of deamidation modification of wheat flour gluten protein |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201710499594.9A CN107212151A (en) | 2017-06-27 | 2017-06-27 | A kind of method of deamidation modification of wheat flour gluten protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN107212151A true CN107212151A (en) | 2017-09-29 |
Family
ID=59950436
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201710499594.9A Pending CN107212151A (en) | 2017-06-27 | 2017-06-27 | A kind of method of deamidation modification of wheat flour gluten protein |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN107212151A (en) |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109463526A (en) * | 2018-04-25 | 2019-03-15 | 福州大学 | A method of the rush efficient deamidation of wheat gluten drops quick |
| CN113100387A (en) * | 2021-04-01 | 2021-07-13 | 湖南聚宝金昊生物科技有限公司 | Special flour for pure rice steamed vermicelli roll and preparation method thereof |
| CN114304368A (en) * | 2021-12-22 | 2022-04-12 | 华东师范大学 | Method for modifying pea protein by using protein glutaminase |
| CN114686162A (en) * | 2022-04-19 | 2022-07-01 | 河南工业大学 | Environment-friendly wheat gluten protein adhesive and preparation method thereof |
| CN114982861A (en) * | 2022-06-16 | 2022-09-02 | 西南大学 | Thick sensory peptide and preparation method and application thereof |
| CN115553375A (en) * | 2022-10-17 | 2023-01-03 | 江南大学 | Method for modifying wheat gluten protein through lactic acid hydrolysis |
| CN116235895A (en) * | 2023-03-14 | 2023-06-09 | 西南科技大学 | Method for preparing food emulsifier based on cottonseed protein isolate |
-
2017
- 2017-06-27 CN CN201710499594.9A patent/CN107212151A/en active Pending
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109463526A (en) * | 2018-04-25 | 2019-03-15 | 福州大学 | A method of the rush efficient deamidation of wheat gluten drops quick |
| CN113100387A (en) * | 2021-04-01 | 2021-07-13 | 湖南聚宝金昊生物科技有限公司 | Special flour for pure rice steamed vermicelli roll and preparation method thereof |
| CN114304368A (en) * | 2021-12-22 | 2022-04-12 | 华东师范大学 | Method for modifying pea protein by using protein glutaminase |
| CN114686162A (en) * | 2022-04-19 | 2022-07-01 | 河南工业大学 | Environment-friendly wheat gluten protein adhesive and preparation method thereof |
| CN114686162B (en) * | 2022-04-19 | 2023-11-03 | 河南工业大学 | Environment-friendly wheat gluten protein adhesive and preparation method thereof |
| CN114982861A (en) * | 2022-06-16 | 2022-09-02 | 西南大学 | Thick sensory peptide and preparation method and application thereof |
| CN115553375A (en) * | 2022-10-17 | 2023-01-03 | 江南大学 | Method for modifying wheat gluten protein through lactic acid hydrolysis |
| CN115553375B (en) * | 2022-10-17 | 2024-03-01 | 江南大学 | Method for modifying wheat gluten protein by lactic acid |
| CN116235895A (en) * | 2023-03-14 | 2023-06-09 | 西南科技大学 | Method for preparing food emulsifier based on cottonseed protein isolate |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN107212151A (en) | A kind of method of deamidation modification of wheat flour gluten protein | |
| CN105462950B (en) | A kind of liquid enzyme formulation and preparation method | |
| CN106455625A (en) | Hypoallergenic, bitterness-reduced soybean oligopeptide, preparation method for same, and applications thereof | |
| CN101569344B (en) | High-dispersity soybean protein isolate and preparation method thereof | |
| CN104448405B (en) | A kind of polysaccharide/alcohol soluble protein composite membrane and preparation method thereof | |
| CN105558259B (en) | The method that enzymolyzed wheat mucedin prepares low bitter taste Gly-His-Lys | |
| JP2012507265A (en) | Glutamic acid-rich yeast extract and method for producing the same | |
| CN104798983A (en) | TG enzyme modification high-intensity mixed gel and preparing method thereof | |
| CN102771749A (en) | Method for preparing thermal reaction meat flavor by utilizing wheat gluten | |
| CN110115348A (en) | A kind of preparation method of highly dissoluble and low irritability egg-white powder | |
| CN107568410A (en) | A kind of method for the rice protein for preparing the common frame structure of high dissolubility | |
| CN107304436A (en) | A kind of xylose improves the preparation method of casein hydrolysate peptides antioxidation activity | |
| CN104757138B (en) | A kind of preparation and its method using prebiotics and WPC as the microencapsulation lactalbumin hydrolysate of wall material | |
| CN108669287A (en) | A kind of method of soybean protein hydrolyate and products thereof preparing acidproof high foaming | |
| CN101361532A (en) | Preparation method of compound protein effervescing agent | |
| CN109938156A (en) | The method for preparing low antigenicity lactalbumin enzymolysis product using ultrasound-ionic liquid processing | |
| CN106480137B (en) | A kind of endogenous sugar improves the method and products thereof of rice residue protein functional characteristic | |
| CN113647602A (en) | Soy sauce and preparation method thereof | |
| CN104531815B (en) | A method of preparing the rich peptide product of high glutamine-bound peptides content | |
| CN105316305A (en) | Method for improving pepsin activity through high pressure processing | |
| CN106841362A (en) | The method of dehydrated potato powder content in detection potato staple food powder or potato staple food | |
| CN110693033A (en) | Walnut peptide calcium chelate and preparation method thereof | |
| CN109536420B (en) | Bacillus subtilis and application thereof | |
| CN113151382B (en) | Method for producing wheat oligopeptide by precipitation method | |
| CN109507247A (en) | Identify the method in the millet place of production based on nonlinear chemical fingerprint |
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 | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20170929 |
|
| RJ01 | Rejection of invention patent application after publication |