CN104982646B - A kind of succinylation is modified the method for improving ovalbumin emulsibility - Google Patents
A kind of succinylation is modified the method for improving ovalbumin emulsibility Download PDFInfo
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Abstract
The method for improving ovalbumin emulsibility is modified the present invention provides a kind of succinylation, is water to be added to be made into the protein solution that mass concentration is 6.0% ovalbumin, is then 0.11 by succinic anhydride and ovalbumin mass ratio:1.0, succinic anhydride is added in protein solution, and it is 9.0 to adjust pH value, then mixed liquor is subjected to acylation reaction in 52 DEG C, reaction time 50min collects supernatant after reaction, freeze-dried to obtain modified ovalbumin.Compared with non-modified ovalbumin, the emulsibility for being remarkably improved ovalbumin is modified by the method for the present invention, emulsifying activity is up to 0.966, and its processing method is simple, may advantageously facilitate application of the ovalbumin in emulsification system.
Description
Technical field
The method for improving ovalbumin emulsibility is modified present invention relates particularly to a kind of succinylation.
Background technology
At present, the method for improving protein function characteristic mainly has：Chemical method, Physical and enzyme process.Wherein chemical modification by
In having many advantages, such as that not high to equipment requirement, cost is relatively low, the reaction time is short and effect is the most apparent, it has also become protein modified
Important means.Common method is acylation reaction in chemical modification, improves the effect of different protein emulsifyings from a large amount of
It is affirmed in research.The research that Yao Yu waits quietly is confirmed under different acyl degree, different pH value, is carried out with succinic anhydride
The effect that acylation reaction improves protein emulsifying is better than acetic anhydride.Nowadays, improve protein performance using succinylation method
Study more and more, most scholar concentrates research soybean protein isolate, wheat gluten protein etc., and to the modification of ovalbumin also
Rare report.
Egg is the very high food of nutritive value, good protein, amino acid, lecithin, fat, courage containing needed by human body
Sterol, vitamins and other nutritious components, digestibility is high, and the absorptivity of especially protein may be up to 98%.Albumen in egg
Albumen is primarily present in egg white, accounts for more than 56% albumen.Ovalbumin is phosphoglucoprotein, is with height two level knot
The ball shape structure of structure, relative molecular mass 43.0kDa, isoelectric point 4.5, more than 50% is hydrophobic amino acid residue, containing 3.5%
Glycosyl and bury 1 disulfide bond, 4 free sulfhydryl groups inside hydrophobic centers.Ovalbumin is higher with respect to the degree of order, structure compared with
For densification, natural ovalbumin can be converted into the S- ovalbumin configurations of thermal stability in storage and transport process.Just because of albumen
The unique structure of albumen determines that it, when molecular modification is to improve its functional characteristic, is showed with other common food albumen not
Same mechanism and condition.Research with egg product deep processing, comprehensive utilization is goed deep into, and the multistage coproduction of egg bioactive ingredients carries
The development and perfection increasingly of pure technology, protein component of the ovalbumin as content maximum in egg white, be various Methods For Purifications its
The object that must be detached first during its functional active components.Ovalbumin has good functional characteristic, such as foaming characteristic, gelling
Property, retentiveness and emulsibility etc., be food processing important supplementary material, but most of research concentrates on ovalbumin at present
In foaming characteristic, seldom research of the report for its emulsibility is restricted its application in emulsification system.Therefore, deepen
Research to ovalbumin, using emulsibility that is biological, either physically or chemically improving ovalbumin, to it is promoted efficiently to integrate
Using being of great significance.
Invention content
The method for improving ovalbumin emulsibility is modified the purpose of the present invention is to provide a kind of succinylation, it can be notable
The emulsibility of gained ovalbumin is improved, may advantageously facilitate application of the ovalbumin in emulsification system.
To achieve the above object, the present invention adopts the following technical scheme that：
A kind of succinylation is modified the method for improving ovalbumin emulsibility, is water to be added to be made into mass concentration ovalbumin
For 6.0% protein solution, then by succinic anhydride and the mass ratio 0.11 of ovalbumin:1.0, amber is added in protein solution
Amber acid anhydrides, and it is 9.0, then mixed liquor is placed in 52 DEG C of water-baths and carries out acylation reaction to adjust pH value, reaction time 50min,
Supernatant is collected after reaction, it is freeze-dried to obtain modified ovalbumin.
The ovalbumin derives from egg, and specific extracting method is：Pollution-free, fissureless Fresh Egg is selected,
After broken shell protein isolate and yolk, by albumen and water in mass ratio 2:1 mixing is diluted, under the conditions of 25 DEG C, magnetic agitation,
It is slowly added to (NH4)2SO4To saturation degree 0.65, continue to stir 1-2h；Then mixed liquor is centrifuged under conditions of 4500r/min
20min, gained precipitation are ovalbumin crude protein；Then crude protein is packed into bag filter, is placed in distilled water and dialyses for 24 hours,
A water is changed per 2h, then by after the solution vacuum freeze drying in bag filter, it is ovalbumin to collect powder.
The remarkable advantage of the present invention is：Ovalbumin is modified using the method for the present invention, emulsifying activity is reachable
0.966, compared with unmodified ovalbumin, emulsibility significantly improves, and its processing method is simple, may advantageously facilitate albumen
Application of the albumen in emulsification system.
Description of the drawings
Fig. 1 is different succinic anhydrides and matching for ovalbumin to compare ovalbumin emulsifying activity and the shadow of emulsion stability
It rings.
Fig. 2 is influence of the differential responses temperature to ovalbumin emulsifying activity and emulsion stability.
Fig. 3 is influence of the different pH value to ovalbumin emulsifying activity and emulsion stability.
Fig. 4 is influence of the differential responses time to ovalbumin emulsifying activity and emulsion stability.
Fig. 5 is the response surface figure that reaction temperature influences ovalbumin emulsifying activity with pH value（a）With contour plots analysis figure
（b）.
Fig. 6 is that reaction temperature matches the response surface figure for comparing the influence of ovalbumin emulsifying activity with acid anhydride（a）And contour plots analysis
Figure（b）.
Fig. 7 is that pH value matches the response surface figure for comparing the influence of ovalbumin emulsifying activity with acid anhydride（a）With contour plots analysis figure
（b）.
Specific embodiment
In order to which content of the present invention is made to easily facilitate understanding, With reference to embodiment to of the present invention
Technical solution is described further, but the present invention is not limited only to this.
1 materials and methods
1.1 laboratory apparatus
PHSJ-4A laboratories 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 models
Factory)；LXJ-IIB flying pigeon board centrifuges (Anting Scientific Instrument Factory, Shanghai)；HJ-3 digital displays constant temperature blender with magnetic force (Changzhou Australia Hua Yi
Device Co., Ltd)；FA2003 electronic balances (the permanent flat science science Instrument Ltd. of Shanghai Shun's space)；FD5-2.5 vacuum refrigerations
Drier (SIM, U.S.A)；HH-S2Thermostat water bath (Jintan City into brightness instrument plant).
1.2 materials and reagent
Fresh hen egg (western Hunan Jishou City sunlight supermarket purchases)；Golden dragonfish edible blend oil (grain and oil in Shenzhen City, Guangdong Province is praised
(China) Co., Ltd)；Succinic anhydride (Sinopharm Chemical Reagent Co., Ltd.)；Dodecyl sodium sulfate (SDS) is chemistry
It is pure；Other reagents are that analysis is pure.
2 experimental methods
The extraction of 2.1 ovalbumins
Ovalbumin in egg is extracted using salting out method, the specific steps are：Select pollution-free, fissureless new freshly-slaughtered poultry
Egg, broken shell protein isolate and yolk, when separation, make to be selected into without yolk in albumen as possible, prevent the disturbance of protein in yolk real
It tests.Then by albumen and water in mass ratio 2:1 mixing is diluted, and under the conditions of 25 DEG C, magnetic agitation, is slowly added to (NH4)2SO4To saturation degree 0.65, continue to stir 1-2h.Mixed liquor centrifuges 20min under conditions of 4500r/min, and gained precipitation is
Ovalbumin crude protein.Then crude protein is packed into bag filter, is placed in distilled water and dialyses for 24 hours, changed a water per 2h, will dialyse
After solution vacuum freeze drying in bag, it is ovalbumin to collect powder.
2.2 succinylation modified techniques
Deionized water is added to be made into the protein solution that mass concentration is 6.0% gained ovalbumin, then add in succinic acid
Acid anhydride adjusts pH value to be placed in water-bath and carries out acylation reaction, collects supernatant after reaction.
2.3 ovalbumin emulsibilities measure
Ovalbumin is dissolved in deionized water, is configured to the protein solution of 1.0g/mL.Change by enzyme process under different condition
Property after, take 3mL samples add in 27mL deionized waters in, add in 10mL human consumption soybean ready-mixed oils, at room temperature with 10000r/min
Speed homogeneous 1min is to form emulsion.200 μ L are drawn from emulsion bottom immediately after homogeneous, adding in 10mL mass fractions is
In 0.1%SDS, after abundant mixing, blank is made with 0.1%SDS solution, its absorbance A is surveyed at 500nm1, as emulsifying activity
EA.After standing 5min, absorbance A is measured again2To get emulsion stability ES=A1×t/(A1-A2), t is expressed as time of repose.
2.4 single factor experiment
2.4.1 different succinic anhydrides and ovalbumin with the influence for comparing ovalbumin emulsifying activity and emulsion stability
In 50 DEG C of reaction temperature, pH value 8.0, under conditions of reaction time 50min, respectively by succinic anhydride and ovalbumin
Mass ratio be set as 0.05:1.0、0.10:1.0、0.15:1.0、0.20:1.0, measure the emulsification work of each protein sample after reaction
Property and emulsion stability.
2.4.2 influence of the differential responses temperature to ovalbumin emulsifying activity and emulsion stability
In succinic anhydride：Ovalbumin=0.10:1.0（g/g）, pH value 8.0, under conditions of reaction time 50min, respectively
Reaction temperature is set as 20,30,40,50,60,70 DEG C, measures the emulsifying activity and emulsion stability of each protein sample after reaction.
2.4.3 influence of the different pH value to ovalbumin emulsifying activity and emulsion stability
In succinic anhydride：Ovalbumin=0.10:1.0（g/g）, 50 DEG C of reaction temperature, under conditions of reaction time 50min,
PH value is set as 7.0,8.0,9.0,10.0,11.0 respectively, measures the emulsifying activity and stable emulsifying of each protein sample after reaction
Property.
2.4.4 influence of the differential responses time to ovalbumin emulsifying activity and emulsion stability
In succinic anhydride：Ovalbumin=0.10:1.0（g/g）, 50 DEG C of reaction temperature under conditions of pH value 8.0, respectively will
Reaction time is set as 30,40,50,60,70min, measure the emulsifying activity and emulsion stability of each protein sample after reaction.
2.5 response phase method Optimum Experiments
On the basis of experiment of single factor, choose the proportioning, reaction temperature, pH value of succinic anhydride and ovalbumin for influence because
Son using ovalbumin emulsifying activity as response, designs Box-Behnken center combination designs, carries out secondary multinomial recurrence side
Journey, which is intended merging optimizing to analyze, obtains optimum process condition, then carry out replication experiment.
3 results and analysis
3.1 single factor experiment
3.1.1 different succinic anhydrides and ovalbumin with the influence for comparing ovalbumin emulsifying activity and emulsion stability
Fig. 1 is different succinic anhydrides and matching for ovalbumin to compare ovalbumin emulsifying activity and the shadow of emulsion stability
It rings.As shown in Figure 1, with the increase of succinic anhydride additive amount, the emulsifying activity and stability of ovalbumin first rise after under
Drop, 0.10:Reach maximum value when 1.0.This is because succinic anhydride is on the increase the hydrophilic radical increase so that introducing, egg
White solution concentration increase, so as to improve emulsifying activity；Protein molecule institute band net charge increases, and intermolecular repulsive force is caused to increase
Add, molecular dispersivity enhancing, so as to improve the emulsion stability of ovalbumin.But when the proportioning of succinic anhydride and ovalbumin reaches
0.10:After 1.0, the raising of emulsifying activity and emulsion stability tends towards stability.Its reason may be the additive amount of succinic anhydride
When reaching a certain level, relative to protein molecule close to saturation state, if continuing to increase succinic anhydride, the promotion to reaction
It acts on unobvious.Therefore, consider from economy and practical operation angle, select the suitable proportion of succinic anhydride and ovalbumin for
0.10:1.0。
3.1.2 influence of the differential responses temperature to ovalbumin emulsifying activity and emulsion stability
Fig. 2 is influence of the differential responses temperature to ovalbumin emulsifying activity and emulsion stability.It is shown according to fig. 2, when
Reaction temperature gradually rises, and the emulsifying activity and stability of ovalbumin first rise to be declined afterwards, reaches maximum value at 50 DEG C.
Temperature raising accelerates solution motion rate, and the stretching, extension of ovalbumin molecule is larger, and it is anti-to be conducive to succinylation for solubility increase
The progress answered, therefore emulsifying activity and emulsion stability increase；But when temperature reaches 60 DEG C, ovalbumin molecule is due to excessive
Denaturation, loses activity, emulsifying activity and emulsion stability is caused to decline.The stability of emulsion is the tension by water-oil interface
What size determined, with the raising of concentration of substrate, the chance that succinic anhydride is contacted with ovalbumin is more, acylation enhancing,
More hydrophobic groups reduce the pressure between water-oil interface towards oil phase, more hydrophilic groups towards water phase in ovalbumin so that
Water-oil interface is not easy to rise brokenly, so as to which emulsion be made to more they tend to stablize；And concentration of substrate it is excessive when, under conditions of continuous heating,
Small molecule polymerize to form soluble polymerized peptides, increases interfacial tension, is gradually reduced emulsion stability.Therefore 50 DEG C are selected
For suitable reaction temperature.
3.1.3 influence of the different pH value to ovalbumin emulsifying activity and emulsion stability
Fig. 3 is influence of the different pH value to ovalbumin emulsifying activity and emulsion stability.From figure 3, it can be seen that with
The increase of solution ph, the emulsifying activity and stability of ovalbumin show the trend of reduction after first increasing, and are 9.0 in pH value
When reach maximum value.With the increase of pH value, the net negative charge of ovalbumin molecule institute band increases, and subunit is unfolded, and makes what is formed
The sucking action of liquid pearl is less than repulsive interaction in emulsion, and liquid pearl is not easy to assemble, therefore ovalbumin dissolubility is more preferable, with succinic acid
Acid anhydride contact is more abundant, more notable so as to the acylation effect of ovalbumin, and emulsifying activity and stability improve.In the condition for crossing alkali
Under, ovalbumin is likely due to be denaturalized and polymeric precipitation；Under conditions of peracid, ovalbumin possibility is because too close to grade electricity
It puts and is precipitated.Therefore, it is Appropriate to take pH value 9.0.
3.1.4 influence of the differential responses time to ovalbumin emulsifying activity and emulsion stability
Fig. 4 is influence of the differential responses time to ovalbumin emulsifying activity and emulsion stability.It can from Fig. 4
Go out, the acylation reaction time is longer, and the emulsifying activity and stability of ovalbumin first rise to be declined afterwards, reaches maximum in 50min
Value.With the increase of modification time, acylation enhancing, concentration of substrate is reduced, and production concentration increases, and succinic anhydride acts on ovum
The time of albumin is more, and the hydrophobic group exposed to the open air is also more, a stabilization and the good film of viscoplasticity is advantageously formed, so as to increase
Add emulsion stability.The average molecular mass of hydrolyzed protein reduces, and surface hydrophobic increases, and solution viscosity declines, water oil
The tension at interface reduces so that the ovalbumin after acylation modification is combined more close with grease.Therefore, when acylation reaction is best
Between be 50min.
3.2 response surface optimizations are tested and result
On the basis of single factor experiment, according to Box-Behnken experimental design principles, matched with succinic anhydride and ovalbumin
Than, reaction temperature, pH value be independent variable, using emulsifying activity as response, design Three factors-levels totally 17 groups of response surface analysis
Experiment, studies the influence of each independent variable and its reciprocation to ovalbumin emulsifying activity and emulsion stability.Experimental factor and
Level is shown in Table 1, experimental design and the results are shown in Table 2.
1 response phase method experimental factor of table and level code table
2 Box-Behnken experimental designs of table and result
It is tested centered on experiment 4,7,12,13,17, to estimate experimental error, other are factorial experiment, are utilized
Design-Expert8.0.6.1 programs carry out ANOVA analyses to the data obtained, and analysis result is shown in Table 3.
3 regression model variance analysis of table
Three factors are through the regression equation that over-fitting obtains：Y=0.98+0.022 × A+0.01 × B+0.014 × C-
0.034×A×B-0.062×B×C-0.078×A2-0.09×B2-0.069×C2。
As shown in Table 3, modelP<0.0001, related coefficientR 2=0.9749, adjusted coefficient of determinationR Adj 2=0.9427, it loses and intends
P=0.1231>0.05 is notable, illustrates the model highly significant, test method is reliable, and true shadow is simulated using the equation
The analysis for ringing factor level is feasible.The Pr from table 3>F it is recognised that quadratic term A2、B2、C2And the BC in interaction item
There is pole significant impact to emulsifying activity, AB has a significant impact, and other factors influence is not notable, this shows the variation phase of response
Work as complexity, influence of each experimental factor to response is not simple linear relationship, but in secondary relationship, and three factors it
Between there are reciprocations.
On the basis of variance analysis, the Design-Expert8.0.6.1 Software on Drawing significant interaction factors are utilized
The reciprocation surface chart and contour map of AB, AC, BC, it is interactive that Fig. 5,6,7 intuitively give three impact factors
Response surface figure and circle of equal altitudes.It can be seen that in selected range that there are extreme values from the peak and isopleth of response surface, be
The central point of isopleth minimum ellipse, while be also the peak on response surface design.It is analyzed by Design-Expert 8.0.6.1
Obtain maximum response（Y）When, the optimum process condition of maximum emulsifying activity is：The proportioning of succinic anhydride and ovalbumin
0.11:1.0, pH value 8.99,51.44 DEG C of reaction temperature, theoretical maximum emulsifying activity is 0.972.
3.3 replication experiment
The verification test of succinylation modification ovalbumin is carried out with gained Optimizing Process Parameters, while in view of practical
Operation and the facility of production match 0.11 with succinic anhydride and ovalbumin:1.0, pH value 9.0,52 DEG C of reaction temperature be it is best,
3 repeated experiments are carried out, it is 0.966 to obtain ovalbumin emulsifying activity average value, and the emulsification with unmodified ovalbumin is lived
Property（0.51）Compared to improving 89.41%, show to be remarkably improved the emulsibility of ovalbumin using the method for the present invention.
The foregoing is merely presently preferred embodiments of the present invention, all equivalent changes done according to scope of the present invention patent with
Modification should all belong to the covering scope of the present invention.
Claims (1)
1. a kind of succinylation is modified the method for improving ovalbumin emulsibility, it is characterised in that：Ovalbumin plus water are made into
Mass concentration is 6.0% protein solution, is then 0.11 by the mass ratio of succinic anhydride and ovalbumin:1.0 in protein solution
Middle addition succinic anhydride, and adjust pH value as 9.0, then mixed liquor is subjected to acylation reaction in 52 DEG C, reaction time 50min,
Supernatant is collected after reaction, it is freeze-dried to be modified ovalbumin；
The ovalbumin derives from egg, and specific extracting method is：Select pollution-free, fissureless Fresh Egg, broken shell
After protein isolate and yolk, by albumen and water in mass ratio 2:1 mixing is diluted, under the conditions of 25 DEG C, magnetic agitation, slowly
Add in (NH4)2SO4To saturation degree 0.65, continue to stir 1-2h；Then mixed liquor is centrifuged under conditions of 4500r/min
20min, gained precipitation are ovalbumin crude protein；Then crude protein is packed into bag filter, is placed in distilled water and dialyses for 24 hours,
A water is changed per 2h, then by after the solution vacuum freeze drying in bag filter, it is ovalbumin to collect powder.
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