CN104982646A - Method for improving emulsibility of ovalbumin by succinylated modification - Google Patents
Method for improving emulsibility of ovalbumin by succinylated modification Download PDFInfo
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- CN104982646A CN104982646A CN201510430598.2A CN201510430598A CN104982646A CN 104982646 A CN104982646 A CN 104982646A CN 201510430598 A CN201510430598 A CN 201510430598A CN 104982646 A CN104982646 A CN 104982646A
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Abstract
The invention provides a method for improving emulsibility of ovalbumin by succinylated modification. The method comprises the steps: adding water into ovalbumin to prepare a 6.0% protein solution by mass; then adding succinic anhydride into the protein solution in a mass ratio of succinic anhydride and ovalbumin: 0.11: 1.0, and adjusting the pH value to 9.0; then carrying out acylation reaction in a mixed solution at 52 DEG C for 50 minutes; and after reaction, collecting the supernate and freezing and drying the supernate to obtain the modified ovalbumin. Compared to unmodified ovalbumin, the emulsibility of ovalbumin can be remarkably improved by modification by the method, the emulsifying activity can reach 0.966, and the treatment method is simple, so that application of the ovalbumin in an emulsification system is facilitated.
Description
Technical field
The present invention is specifically related to a kind of method that succinylation modification improves ovalbumin emulsibility.
Background technology
At present, the method improving protein function characteristic mainly contains: chemical method, Physical and enzyme process.Wherein chemical modification is owing to having, cost lower, reaction time short and effect the most obvious etc. advantage not high to equipment requirement, has become protein modified important means.Method conventional in chemical modification is acylation reaction, and its effect improving different albumin milk voltinism has obtained certainly from large quantity research.The research that Yao Yu waits quietly confirms under different acyl degree, different pH value, carries out the effect that acylation reaction improves albumin milk voltinism be better than acetic anhydride with succinyl oxide.Nowadays, the research utilizing succinylation method to improve protein performance gets more and more, and most scholar concentrates research soybean protein isolate, wheat gluten protein etc., and the modification also rare report to ovalbumin.
Egg is the food that nutritive value is very high, and containing good protein, amino acid, lecithin, fat, cholesterol, the vitamins and other nutritious components of needed by human body, digestibility is high, and especially the absorptivity of protein can up to 98%.Ovalbumin in egg is mainly present in egg white, accounts for albumen more than 56%.Ovalbumin is phosphoglucoprotein, be the ball shape structure with height secondary structure, relative molecular mass is 43.0kDa, and isoelectric point is 4.5, more than 50% is hydrophobic amino acid residue, containing 3.5% glycosyl and bury 1 disulfide bond in hydrophobic centers inside, 4 free sulfhydryl groups.Ovalbumin is higher relative to the degree of order, and structure is comparatively fine and close, and natural ovalbumin can be converted into the S-ovalbumin configuration of heat endurance in storage and transport process.Structure uniqueness just because of ovalbumin determines that it is when molecular modification is to improve its functional characteristic, presents the mechanism different from other common food albumen and condition.Along with the research of egg product deep processing, comprehensive utilization is goed deep into, the multistage coproduction purification technique development and perfection increasingly of egg bioactive ingredients, ovalbumin as the maximum protein component of content in egg, the object that must first be separated when being other functional active components of various Methods For Purification.Ovalbumin has good functional characteristic, as foaming characteristic, gelling, retentiveness and emulsibility etc., it is the important supplementary material of food processing, but current most research concentrates in the foaming characteristic of ovalbumin, little report, for the research of its emulsibility, makes its application in emulsification system be restricted.Therefore, deepen the research to ovalbumin, adopt biology, physics or chemical method to improve the emulsibility of ovalbumin, significant to its high-efficiency comprehensive utilization of promotion.
Summary of the invention
The object of the present invention is to provide a kind of succinylation modification to improve the method for ovalbumin emulsibility, it can significantly improve the emulsibility of gained ovalbumin, is conducive to promoting the application of ovalbumin in emulsification system.
For achieving the above object, the present invention adopts following technical scheme:
A kind of succinylation modification improves the method for ovalbumin emulsibility; ovalbumin is added water be made into the protein solution that mass concentration is 6.0%; then the mass ratio 0.11:1.0 of succinyl oxide and ovalbumin is pressed; succinyl oxide is added in protein solution; and adjust pH is 9.0, then mixed liquor is placed in 52 DEG C of water-baths and carries out acylation reaction, the reaction time is 50min; reaction terminates rear collection supernatant, obtains modified ovalbumin through freeze drying.
Described ovalbumin derives from egg, its concrete extracting method is: select pollution-free, fissureless Fresh Egg, after broken shell protein isolate and yolk, by albumen and water in mass ratio 2:1 mix and dilute, 25 DEG C, under magnetic agitation condition, slowly add (NH
4)
2sO
4to saturation degree 0.65, continue to stir 1-2h; Then by mixed liquor centrifugal 20min under the condition of 4500r/min, gained precipitation is ovalbumin crude protein; Then crude protein is loaded bag filter, be placed in dialyse 24h, every 2h of distilled water and change a water, then by after the solution for vacuum freeze drying in bag filter, collect powder and be ovalbumin.
remarkable advantage of the present invention is: adopt the inventive method to carry out modification to ovalbumin, its emulsifying activity can reach 0.966, and compared with unmodified ovalbumin, its emulsibility significantly improves, and its processing method is simple, is conducive to promoting the application of ovalbumin in emulsification system.
Accompanying drawing explanation
Fig. 1 is the impact of proportioning on ovalbumin emulsifying activity and emulsion stability of different succinyl oxide and ovalbumin.
Fig. 2 is differential responses temperature on the impact of ovalbumin emulsifying activity and emulsion stability.
Fig. 3 is different pH value on the impact of ovalbumin emulsifying activity and emulsion stability.
Fig. 4 is the differential responses time on the impact of ovalbumin emulsifying activity and emulsion stability.
Fig. 5 response surface figure (a) that to be reaction temperature and pH value affect ovalbumin emulsifying activity and contour plots analysis figure (b).
Fig. 6 response surface figure (a) that to be reaction temperature and acid anhydride proportioning affect ovalbumin emulsifying activity and contour plots analysis figure (b).
Fig. 7 response surface figure (a) that to be pH value and acid anhydride proportioning affect ovalbumin emulsifying activity and contour plots analysis figure (b).
Detailed description of the invention
More being convenient to make content of the present invention understand, below in conjunction with detailed description of the invention, technical solutions according to the invention are described further, but the present invention being not limited only to this.
1 materials and methods
1.1 laboratory apparatus
PHSJ-4A laboratory pH meter (Shanghai precision scientific instrument Co., Ltd); 722 type visible spectrophotometers (the permanent flat science science Instrument Ltd. of Shanghai Shun's space); FJ200-SH type digital display high speed dispersion homogenizer (Shanghai Sample Model Factory); LXJ-IIB flying pigeon board centrifuge (Anting Scientific Instrument Factory, Shanghai); HJ-3 digital display constant temperature blender with magnetic force (Changzhou Ao Hua Instrument Ltd.); FA2003 electronic balance (the permanent flat science science Instrument Ltd. of Shanghai Shun's space); FD5-2.5 vacuum freeze dryer (SIM, U.S.A); HH-S
2thermostat water bath (Cheng Hui instrument plant of Jintan City).
1.2 materials and reagent
Fresh hen egg (Jishou City sunlight supermarket, the western Hunan is purchased); The imperial fish edible blend oil of gold (Shenzhen City, Guangdong Province good in grain and oil (China) Co., Ltd); Succinyl oxide (Chemical Reagent Co., Ltd., Sinopharm Group); Dodecyl sodium sulfate (SDS) is chemical pure; It is pure that other reagent are analysis.
2 experimental techniques
The extraction of 2.1 ovalbumins
Adopt salting out method to extract ovalbumin in egg, its concrete steps are: select pollution-free, fissureless Fresh Egg, broken shell protein isolate and yolk, make to be selected into without yolk in albumen during separation as far as possible, prevent the disturbance of protein in yolk from testing.Then by albumen and water in mass ratio 2:1 mix and dilute, 25 DEG C, under magnetic agitation condition, slowly add (NH
4)
2sO
4to saturation degree 0.65, continue to stir 1-2h.Mixed liquor is centrifugal 20min under the condition of 4500r/min, and gained precipitation is ovalbumin crude protein.Then crude protein is loaded bag filter, be placed in dialyse 24h, every 2h of distilled water and change a water, after the solution for vacuum freeze drying in bag filter, collect powder and be ovalbumin.
2.2 succinylation modified techniques
Gained ovalbumin is added deionized water and be made into the protein solution that mass concentration is 6.0%, then add succinyl oxide, adjust pH is placed in water-bath and carries out acylation reaction, and reaction terminates rear collection supernatant.
2.3 ovalbumin emulsibilities measure
Ovalbumin is dissolved in deionized water, is mixed with the protein solution of 1.0g/mL.After enzyme modification under different condition, get 3mL sample and add in 27mL deionized water, add 10mL human consumption soybean ready-mixed oil, at room temperature with 10000r/min speed homogeneous 1min to form emulsion.Bottom emulsion, draw 200 μ L immediately after homogeneous, adding 10mL mass fraction is in 0.1%SDS, fully after mixing, does blank, survey its absorbance A at 500nm place with 0.1%SDS solution
1, be emulsifying activity EA.After leaving standstill 5min, again measure absorbance A
2, obtain emulsion stability ES=A
1× t/ (A
1-A
2), t is expressed as time of repose.
2.4 single factor experiment
2.4.1 the proportioning of different succinyl oxide and ovalbumin is on the impact of ovalbumin emulsifying activity and emulsion stability
Reaction temperature 50 DEG C, pH value 8.0, under the condition of reaction time 50min, respectively the mass ratio of succinyl oxide and ovalbumin is set to 0.05:1.0,0.10:1.0,0.15:1.0,0.20:1.0, the emulsifying activity of each protein sample and emulsion stability after assaying reaction.
2.4.2 differential responses temperature is on the impact of ovalbumin emulsifying activity and emulsion stability
At succinyl oxide: ovalbumin=0.10:1.0(g/g), pH value 8.0, under the condition of reaction time 50min, is set to 20,30,40,50,60,70 DEG C by reaction temperature respectively, the emulsifying activity of each protein sample and emulsion stability after assaying reaction.
2.4.3 different pH value is on the impact of ovalbumin emulsifying activity and emulsion stability
At succinyl oxide: ovalbumin=0.10:1.0(g/g), reaction temperature 50 DEG C, under the condition of reaction time 50min, is set to 7.0,8.0,9.0,10.0,11.0 by pH value respectively, the emulsifying activity of each protein sample and emulsion stability after assaying reaction.
2.4.4 the differential responses time is on the impact of ovalbumin emulsifying activity and emulsion stability
At succinyl oxide: ovalbumin=0.10:1.0(g/g), reaction temperature 50 DEG C, under the condition of pH value 8.0,30 will be set to respectively the reaction time, 40,50,60,70min, the emulsifying activity of each protein sample and emulsion stability after assaying reaction.
2.5 response phase method Optimum Experiments
On experiment of single factor basis, choose the proportioning of succinyl oxide and ovalbumin, reaction temperature, pH value be factor of influence, with ovalbumin emulsifying activity for response, design Box-Behnken center combination design, carry out the multinomial regression equation matching of secondary and Optimization analyses obtains optimum process condition, then carry out replication experiment.
3 results and analysis
3.1 single factor experiment
3.1.1 the proportioning of different succinyl oxide and ovalbumin is on the impact of ovalbumin emulsifying activity and emulsion stability
Fig. 1 is the impact of proportioning on ovalbumin emulsifying activity and emulsion stability of different succinyl oxide and ovalbumin.As shown in Figure 1, along with the increase of succinyl oxide addition, the emulsifying activity of ovalbumin and stability all first rise and decline afterwards, reach maximum when 0.10:1.0.This is that protein solution concentration increases, thus improves emulsifying activity because the hydrophilic radical making to introduce of being on the increase of succinyl oxide increases; Net charge that protein molecule is with increases, and causes intermolecular repulsive force to increase, and molecular dispersivity strengthens, thus improves the emulsion stability of ovalbumin.But after the proportioning working as succinyl oxide and ovalbumin reaches 0.10:1.0, the raising of emulsifying activity and emulsion stability tends towards stability.Its reason may be the addition of succinyl oxide when acquiring a certain degree, and relative to protein molecule close to saturation state, increases succinyl oxide if continue, to the facilitation of reaction by not obvious.Therefore, consider from economy and practical operation angle, the suitable proportion selecting succinyl oxide and ovalbumin is 0.10:1.0.
3.1.2 differential responses temperature is on the impact of ovalbumin emulsifying activity and emulsion stability
Fig. 2 is differential responses temperature on the impact of ovalbumin emulsifying activity and emulsion stability.According to Fig. 2, when reaction temperature raises gradually, the emulsifying activity of ovalbumin and stability all first rise and decline afterwards, 50 DEG C time, reach maximum.Temperature raises and solution motion speed is accelerated, and the stretching, extension of ovalbumin molecule is comparatively large, and solubility increases, and is conducive to the carrying out of succinylation reaction, and therefore emulsifying activity and emulsion stability increase; But when temperature reaches 60 DEG C, ovalbumin molecule, due to excessive sex change, loses activity, emulsifying activity and emulsion stability is caused all to decline.The stability of emulsion is determined by the Tensity size at water oil interface, along with the rising of concentration of substrate, the chance that succinyl oxide contacts with ovalbumin is more, acylation strengthens, in ovalbumin, more hydrophobic group is towards oil phase, and more hydrophilic groups, towards aqueous phase, reduce the pressure between water oil interface, not easily risen brokenly in water oil interface, thus emulsion is more tended towards stability; And concentration of substrate excessive time, under the condition of constantly heating, Small molecular polymerization forms the polymerized peptides of solubility, increases interfacial tension, emulsion stability is reduced gradually.Therefore 50 DEG C are selected for suitable reaction temperature.
3.1.3 different pH value is on the impact of ovalbumin emulsifying activity and emulsion stability
Fig. 3 is different pH value on the impact of ovalbumin emulsifying activity and emulsion stability.As can be seen from Figure 3, along with the increase of solution ph, the emulsifying activity of ovalbumin and stability present the trend first increasing and reduce afterwards, reach maximum when pH value is 9.0.Along with the increase of pH value; ovalbumin molecule with net negative charge increase; subunit is unfolded; the sucking action of liquid pearl in the emulsion of formation is made to be less than repulsive interaction; pearl not easily assembles liquid, therefore ovalbumin dissolubility is better, contacts more abundant with succinyl oxide; thus the acidylate more remarkable effect of ovalbumin, emulsifying activity and stability improve.Under the condition crossing alkali, ovalbumin is the polymeric precipitation due to sex change likely; Under the condition of peracid, ovalbumin may because too separating out near isoelectric point.Therefore, pH value 9.0 is got for Appropriate.
3.1.4 the differential responses time is on the impact of ovalbumin emulsifying activity and emulsion stability
Fig. 4 is the differential responses time on the impact of ovalbumin emulsifying activity and emulsion stability.As can be seen from Figure 4, the acylation reaction time is longer, and the emulsifying activity of ovalbumin and stability first rise and declines afterwards, reach maximum when 50min.Along with the increase of modification time, acylation strengthens, and concentration of substrate reduces; production concentration increases, and the time that succinyl oxide acts on ovalbumin is more, and the hydrophobic group exposed to the open air is also more; be conducive to the stable and film that viscoplasticity is good of formation one, thus increase emulsion stability.The average molecular mass of hydrolyzed protein reduces, and surface hydrophobic increases, and solution viscosity declines, and the tension force at water oil interface reduces, and the ovalbumin after acylation modification is combined more tight with grease.Therefore, acylation reaction Best Times is 50min.
3.2 response surface optimization test and results
On single factor experiment basis, according to Box-Behnken experimental design principle, with succinyl oxide and ovalbumin proportioning, reaction temperature, pH value for independent variable, take emulsifying activity as response, the totally 17 groups of response surface analysises experiment of design Three factors-levels, studies the impact on ovalbumin emulsifying activity and emulsion stability of each independent variable and reciprocation thereof.Experimental factor and level in table 1, experimental design and the results are shown in Table 2.
Table 1 response phase method experimental factor and level code table
Table 2 Box-Behnken experimental design and result
Test centered by testing 4,7,12,13,17, in order to estimate experimental error, other are factorial experiment, and utilize Design-Expert8.0.6.1 program to carry out ANOVA analysis to the data obtained, analysis result is in table 3.
The variance analysis of table 3 regression model
The regression equation that three factors obtain through over-fitting is: Y=0.98+0.022 × A+0.01 × B+0.014 × C-0.034 × A × B-0.062 × B × C-0.078 × A
2-0.09 × B
2-0.069 × C
2.
As shown in Table 3, model
p<0.0001, coefficient correlation
r 2=0.9749, adjusted coefficient of determination
r adj 2=0.9427, lose and intend item
p=0.1231>0.05 is not remarkable, and this model highly significant is described, test method is reliable, and the analysis using this equation influence factor that is virtually reality like reality level is feasible.From table 3, Pr>F item can be known, quadratic term A
2, B
2, C
2and the BC in mutual item has emulsifying activity and affects extremely significantly, AB has remarkable impact, the impact of other factors is not remarkable, this shows that the change of response is quite complicated, each experimental factor is not simple linear relationship on the impact of response, but in secondary relation, and there is reciprocation between Three factors.
On the basis of variance analysis, utilize Design-Expert8.0.6.1 Software on Drawing significant interaction factors A B, the reciprocation surface chart of AC, BC and contour map, Fig. 5,6,7 gives three interactive response surface figure of factor of influence and circle of equal altitudes intuitively.As can be seen from peak and the isopleth of response surface, in selected scope, there is extreme value, is namely the central point of isopleth minimum ellipse, is also the peak on response surface design simultaneously.When obtaining maximum response (Y) by Design-Expert 8.0.6.1 analysis, the optimum process condition of its maximum emulsifying activity is: the proportioning 0.11:1.0 of succinyl oxide and ovalbumin, pH value 8.99, reaction temperature 51.44 DEG C, theoretical maximum emulsifying activity is 0.972.
3.3 replication experiment
Gained Optimizing Process Parameters is used to carry out the demonstration test of succinylation modification ovalbumin; consider the facility of practical operation and production simultaneously; with succinyl oxide and ovalbumin proportioning 0.11:1.0; pH value 9.0; reaction temperature 52 DEG C is best, and carry out 3 repeated experiments, obtaining ovalbumin emulsifying activity mean value is 0.966; improve 89.41% compared with the emulsifying activity (0.51) of unmodified ovalbumin, show to adopt the inventive method can significantly improve the emulsibility of ovalbumin.
The foregoing is only preferred embodiment of the present invention, all equalizations done according to the present patent application the scope of the claims change and modify, and all should belong to covering scope of the present invention.
Claims (1)
1. the method for a succinylation modification raising ovalbumin emulsibility; it is characterized in that: ovalbumin is added water and is made into the protein solution that mass concentration is 6.0%; then be that 0.11:1.0 adds succinyl oxide in protein solution by the mass ratio of succinyl oxide and ovalbumin; and adjust pH is 9.0; again mixed liquor is carried out acylation reaction in 52 DEG C; reaction time is 50min, and reaction terminates rear collection supernatant, obtains modification ovalbumin through freeze drying.
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| CN111621032A (en) * | 2020-04-27 | 2020-09-04 | 上海海洋大学 | Octenylsuccinic anhydride modified gelatin and preparation method and application thereof |
| CN113209005A (en) * | 2021-05-08 | 2021-08-06 | 华中农业大学 | Preparation method and application of high-stability protein nanogel delivery carrier |
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| CN113209005A (en) * | 2021-05-08 | 2021-08-06 | 华中农业大学 | Preparation method and application of high-stability protein nanogel delivery carrier |
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