CN104957357A - Method for improving ovalbumin emulsibility by moist-heat method glycosylation modification - Google Patents
Method for improving ovalbumin emulsibility by moist-heat method glycosylation modification Download PDFInfo
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Abstract
The invention discloses a method for improving ovalbumin emulsibility by moist-heat method glycosylation modification, wherein the influences of a substrate proportion (ovalbumin: glucose), a reaction temperature, a reaction time and a reaction pH value on the ovalbumin emulsibility are inspected; on the basis of a single-factor experiment, the conditions of improving the ovalbumin emulsibility by the glycosylation modification are optimized by a response surface; a result indicates that the optimal conditions of the glycosylation modification are as follows: the substrate proportion is 1:1.15, the reaction temperature is 56 DEG C, the reaction time is 4.0h, and the pH value is 10.0. The ovalbumin emulsifying activity measured under the conditions is 0.62, and is double of the unmodified ovalbumin emulsifying activity.
Description
Technical field
The invention belongs to protein emulsifying technology field, be specifically related to a kind of method that wet heating glycosylation modification improves ovalbumin emulsibility.
Background technology
Protein is the important composition composition of biological cell, not only plays an important role in the 26S Proteasome Structure and Function of cell, also has abundant nutritive value, for human body provides energy and essential amino acid.Protein has the characteristic of amphiphilic, its except can with water effect, can also interact with lipid, so in oil/water system, good emulsifiability can be had.Emulsifying activity and emulsion stability are protein emulsibility two data targets, and emulsifying activity refers to that protein is when promoting oil/water mixing, and unit mass protein (g) can stablize oil-water interfaces area (m
2)
[1].Protein is also one of most important constituent in food, considerable influence is had to the matter structure of food, local flavor and processing trait, this is mainly because protein has several functions character, as gelatification, dissolubility, foaming characteristic, emulsification and viscosity etc. play a significant role in food
[2].Current numerous protein does not reach the requirement of expection because of emulsibility, so fail to obtain extensive use in the food industry, it is necessary for therefore improving protein emulsibility by method of modifying.
Acidylate is mainly contained at present for food protein method of modifying
[3], remove acid amides
[4-5], phosphorylation, glycosylation
[6-7], covalent cross-linking, the method such as proteolysis; Wherein, protein glycosylation modification is the process being connected to form glycosylated protein by reducing sugar and protein molecule free lysine α or ε amino covalence mostly
[8].Do not need artificially to add any chemical reagent in this reaction, just spontaneously can be carried out by heating, belong to " friendly process "; Therefore be conducive to it to use in the food industry.Glycosylation modification mainly contains two kinds of methods: namely based on solid system dry heating method with based on aqueous phase system wet heating.
Ovalbumin has another name called ovalbumin, as protein topmost in egg white, accounts for 54% ~ 69% of total protein in egg white.The functional character of ovalbumin is excellent, can be used as emulsifying agent, NMF, edible packing membrane, gel etc., play a part to improve in food the mouthfeel of food and quality, raising product stability and extend the shelf life.The present invention adopts glucose to carry out glycosylation modification to ovalbumin to improve its emulsibility, with Responds Surface Methodology, determines that glycosylation modification improves the optimum preparating condition of ovalbumin emulsibility, for its application in related industries provides foundation.
Ovalbumin is phosphoglucoprotein, there is the ball shape structure of height secondary structure, relative molecular mass is 43.0 kDa, isoelectric point is 4.5,50 more than % are hydrophobic amino acid residue, containing 3.5 % glycosyls and bury 1 disulfide bond in hydrophobic centers inside, 4 free sulfhydryl groups, sulfydryl is all embedded in the hydrophobic core part of protein.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.When the structure uniqueness of ovalbumin determines its molecular modification to improve its functional characteristic, present 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 is 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, biology, physics or chemical method is adopted to improve the functional characteristic 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 wet heating glycosylation modification to improve the method for ovalbumin emulsibility, the emulsifying activity of actual glycation product can be predicted, there is certain using value.
For achieving the above object, the present invention adopts following technical scheme:
A kind of wet heating glycosylation modification improves the method for ovalbumin emulsibility: by concentration be the ovalbumin of 15.0mg/mL with glucose in mass ratio for 1:1.15 mixes, be dissolved in 20mL phosphate buffer, adjust ph=10.0, after 56 DEG C of isothermal reaction 4.0h, reactant liquor ice bath is cooled to room temperature rapidly, obtains modified ovalbumin.
Remarkable advantage of the present invention is: the present invention can predict the emulsifying activity of actual glycation product, has certain using value.
Accompanying drawing explanation
Fig. 1 is the impact of substrate proportioning on emulsibility.
Fig. 2 is the impact of temperature on emulsibility.
Fig. 3 is the impact of time on emulsibility.
Fig. 4 is the impact of pH value on emulsibility.
Fig. 5 response surface that to be substrate proportioning (A) affect ovalbumin emulsifying activity (EA) with the reaction time (B) and isopleth.
Fig. 6 response surface that to be substrate proportioning (A) affect ovalbumin emulsifying activity (EA) with reaction temperature (C) and isopleth.
Fig. 7 response surface that to be the reaction time (B) affect ovalbumin emulsifying activity (EA) with reaction temperature (C) and isopleth.
Detailed description of the invention
1 materials and methods
1.1 experiment materials and reagent
Fresh hen egg: Jishou City sunlight supermarket is purchased; The imperial fish edible blend oil of gold: Jishou City sunlight supermarket is purchased; It is pure that PEG8000, NaOH, glucose, hydrochloric acid, dipotassium hydrogen phosphate, potassium dihydrogen phosphate, lauryl sodium sulfate etc. are analysis.
1.2 instrument and equipment
722 type visible spectrophotometers, the limited public affairs of the permanent flat scientific instrument of Shanghai Shun's space; FA2004 electronic balance, Shanghai Sunny Hengping Scientific Instrument Co., Ltd.; HJ-3 digital display constant temperature blender with magnetic force, Changzhou Ao Hua Instrument Ltd.; PHS-4A laboratory pH meter, Shanghai faces south scientific instrument factory; HH-S2 thermostat water bath, Cheng Hui instrument plant of Jintan City; FJ200-SH type digital display high speed dispersion homogenizer, Shanghai sample model manufacturing factory; LXJ-IIB flying pigeon board centrifuge, Anting Scientific Instrument Factory, Shanghai; FD5-2.5 freeze dryer, Xi Meng life technology Co., Ltd of the U.S..
1.3 experimental technique
1.3.1 the extraction of ovalbumin
Adopt polyethylene glycol precipitation
[15]the method combined with isoelectric precipitation extracts ovalbumin.Select fresh egg, albumen is separated with yolk, albumen and deionized water are according to the dilution proportion of 1:1,10min is stirred at 25 DEG C of lower magnetic forces, by filtered through gauze, then limit magnetic agitation, limit slowly adds PEG8000 (consumption is mixed liquor mass fraction 15%), adds rear stirring 1-2 h.Mixed liquor is centrifugal 20 min under the condition of 5000r/min, get supernatant limit magnetic agitation, while with 1mol/L HCl adjust pH to 4.5, produce precipitation after leaving standstill 30 min, collecting precipitation is ovalbumin sterling, refrigerates for subsequent use after freeze drying.
1.3.2 ovalbumin glycosylation modification
Be that ovalbumin and the glucose of 15.0mg/mL mixes with certain proportion (w/w) and is dissolved in 20mL phosphate buffer by concentration, after adjust ph to a certain determined value, in closed container, after isothermal reaction certain hour, reactant liquor ice bath is cooled to room temperature rapidly, obtain the modification white of an egg, freeze-dried back.
1.3.3 emulsifying activity and Stability Determination
By the ovalbumin after different condition phosphatizing treatment, being dissolved in pH value is respectively in the phosphate buffer of 7.4,0.1 mol/L, is mixed with the protein solution sample of 0.5 mg/mL.Then in l0mL ready-mixed oil, add 20 mL samples respectively, with 10000 r/min homogeneous 1 min under room temperature, then draw 100 from bottom immediately
μemulsion after L homogeneous, adds the SDS that 5 mL mass fractions are 0.1 %, fully after mixing, does blank, survey its absorbance A at 500 nm places with the SDS solution of equivalent 0.1 %
1, be emulsifying activity E
a; After leaving standstill 15 min, again measure absorbance A
2, calculate emulsion stability Es.The computational methods of emulsion stability are: E
s=A
1× t/ (A
1-A
2), wherein, t is time of repose.
2 results and analysis
2.1 substrate proportionings are on the impact of ovalbumin emulsibility
At reaction time 3.0h, reaction temperature 45 DEG C, reaction pH7.4, investigate different substrate proportioning to the impact of ovalbumin emulsibility, to determine its factor span.
As shown in Figure 1, the emulsifying activity of ovalbumin is in rising trend before ovalbumin and glucose quality ratio reach 1:1, reaches maximum when 1:1, after this on a declining curve.May be the increase of the ratio due to sugar, the contact probability between the carbonyl of free amino groups of protein and glycan molecule reduction end be obtained and improves, emulsifying activity raises, but, along with the continuation of sugared content increases, obviously, emulsifying activity reduces for solution viscosity increase and space steric effect
[17].Emulsion stability increases along with the increase of glucose quality, reaches maximum, present downward trend afterwards when substrate proportioning is 1:3.Consider cost, and too much glucose can increase the viscosity of solution
[18], be unfavorable for the application in food, so determine that substrate proportioning value is 1:1.
2.2 temperature are on the impact of ovalbumin emulsibility
At substrate proportioning (ovalbumin: glucose) 1:1, reaction time 3.0h, reaction pH7.4, investigate differential responses temperature to the impact of ovalbumin emulsibility, to determine its factor span.
As shown in Figure 2, the emulsifying activity of ovalbumin and emulsion stability are all in rising trend before reaction temperature 55 DEG C, 55 DEG C time, reach maximum, after this on a declining curve, thus determine that reaction temperature value is 55 DEG C.Reason may be within the specific limits along with the rising of reaction temperature, the Maillard reaction of ovalbumin and glucose can be accelerated, protein structure launches, improve macromolecular surface-active, after introducing glucose, the hydrophily of compound increases, and its emulsibility and emulsion stability are improved, but when reaction temperature continues to increase to over to a certain degree, albumen serious degenerative, thus the emulsibility reducing ovalbumin
[19].
2.3 reaction time are on the impact of ovalbumin emulsibility
At substrate proportioning 1:1, reaction temperature 55 DEG C, reaction pH7.4, investigate the differential responses time to the impact of ovalbumin emulsibility, to determine its factor span.
As shown in Figure 3, ovalbumin emulsifying activity is in rising trend before 4.0h, reaches maximum when 4.0h, after this on a declining curve.Ovalbumin emulsion stability is in rising trend before 5.0h, reaches maximum when 5.0h, after this on a declining curve.This is due to the increase along with the reaction time, and protein structure launches, and glucose and ovalbumin react and aggravate, and therefore emulsibility obtains and improves; Along with the continuation in reaction time increases, free histone amino and alditol hydroxyl reduce in reaction system, reaction speed is slowed down, protein denaturation strengthens gradually simultaneously, albumen and glucose response product increase the impact that the produces impact lower than protein denaturation, and emulsibility and emulsion stability reduce gradually
[20].So determine that the value in reaction time is 4.0h.
2.4 pH value in reaction are on the impact of ovalbumin emulsibility
At substrate proportioning 1:1, reaction temperature 55 DEG C, reaction time 4.0h, investigate differential responses pH value to the impact of ovalbumin emulsibility, to determine its factor span.
As shown in Figure 4, in the scope of pH6-10, ovalbumin emulsibility increases with the increase of pH value.This is because the isoelectric point of ovalbumin is about 4.5, when pH value is less than 6, ovalbumin there will be sediment, and can suppress the generation of Maillard reaction under acid condition.But, when pH value is excessive, the primary structure of protein can be destroyed when alkalescence is crossed strong, as deamination, Tuo Suo and peptide bond fission, be unfavorable for carrying out further of glycosylation
[21], so in the present invention, determine that pH value in reaction is 10.0.
2.5 response phase method optimizations
2.5.1 Box-Behnken experimental design
According to above-mentioned single factor experiment result, adopt Box-Behnken center combination experimental design principle, choose substrate proportioning, reaction time, reaction temperature 3 factors (pH value 10.0), with ovalbumin emulsifying activity (E
a) be evaluation index, the Box-Behnken center combination test of design Three factors-levels, factor level is in table 1.
Table 1 response surface analysis factor and water-glass
2.5.2 the foundation of regression equation and significance analysis
According to factor level coding schedule, the response surface experimental program of design glycosylation modification ovalbumin emulsibility and result are as table 2.
Table 2 Box-Behnken center combination result of the test
Use Design-Expert 8.0.6 software to carry out regression analysis to the response of 17 experimental points, Multinomial fitting recurrence is carried out, with E to experimental data
afor dependent variable, substrate proportioning (A), reaction time (B) and reaction temperature (C) they are independent variable, set up regression equation as follows:
EA=0.6134+0.004375A+0.0015B+0.002625C-0.00025AB+0.003AC+0.0025BC-0.01645A
2-0.0117 B
2-0.01745C
2
The variance analysis of table 3 regression model
Note: * * represents that extremely significantly (p<0.01) * represents significantly (0.01<p<0.05)
Table 3 is the variance analysis of model.Analysis result shows, and the P value < 0.0001 of model, namely model is extremely remarkable.Lose the P value=0.4391>0.05 intending item, namely lose and intend item significantly, illustrate that X factor is little to result of the test interference.R
2=0.9953, illustrate that models fitting degree is good, therefore, regression equation can describe the true relation between each factor and response preferably.As shown in Table 3, A, C, AC, A
2, B
2, C
2on the impact of ovalbumin emulsifying activity extremely significantly (P<0.01), B impact significantly (P<0.05), AB, BC significantly do not adopt the method for stepwise regression analysis to its impact, show that probed into factor on response impact greatly and be not simple once linear relationship.By comparing each factor in analysis of variance table
fbe worth known, substrate proportioning, reaction time, reaction temperature reach extremely significantly and the level of signifiance respectively on the impact of ovalbumin emulsifying activity.
2.5.3 response surface design analysis and technology is optimized
Fig. 5-7 is the response surface design figure of each factor interaction.As seen from the figure, in substrate proportioning one timing, the emulsibility of ovalbumin increases with the reaction time and increases, and when increasing to certain value, increasing and reduce with the reaction time; Reaction time, when certain, ovalbumin emulsibility increased with the increase of substrate proportioning, when substrate proportioning arrives certain value, increases and reduce with substrate proportioning.
In reaction temperature one timing, the emulsibility of ovalbumin increases with substrate proportioning and increases, and when increasing to certain value, increasing and reduce with substrate proportioning; When substrate proportioning is certain, ovalbumin emulsibility increases with the increase of reaction temperature, when reaction temperature arrives certain value, increases and reduce with reaction temperature.
In reaction time one timing, the emulsibility reaction temperature of ovalbumin increases and increases, and when increasing to certain value, increasing and reduce with reaction temperature; When reaction temperature is certain, ovalbumin emulsibility increases with the increase in reaction time, when arriving certain value when reacted, increases and reduce with the reaction time.
2.5.4 optimum results and demonstration test
In order to try to achieve the optimum condition combination of each factor further, Mathematical treatment is carried out to regression equation, the optimal conditions that local derviation asks the extreme value solving equations after zero to obtain glycosylation modification ovalbumin emulsibility is: substrate proportioning 1:1.141, reaction time 4.067h, reaction temperature 55.489 DEG C.Consider the practical operation of experiment, glycosylation modification ovalbumin emulsibility optimal conditions be: substrate proportioning 1:1.15, reaction time 4.0h, reaction temperature 56 DEG C.Under this condition, the emulsifying activity theoretical value of ovalbumin reaches 0.61.For the difference of testing model predicted value and test value, do 3 repeating test according to optimal conditions, the emulsifying activity of result ovalbumin is 0.62, basically identical with theoretical value.
3 conclusions
Be that raw material adds appropriate glucose and carries out modification to it with ovalbumin, and using modified ovalbumin emulsifying activity as evaluation index.Single factor test basis adopt response phase method optimize glycosylation modification ovalbumin process conditions.The optimum condition being obtained glycosylation modification by confirmatory experiment and regression analysis is: substrate proportioning (ovalbumin: glucose) 1:1.15, reaction time 4.0h, reaction temperature 56 DEG C, pH value 10.0.The emulsibility of the glycation product obtained with this understanding is 0.62, can coincide preferably with theoretical value, and this model can predict the emulsifying activity of actual glycation product, has certain using value.Modified ovalbumin such as emulsibility is significantly better than unmodified ovalbumin (0.31), improves 100%.
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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 wet heating glycosylation modification raising ovalbumin emulsibility, it is characterized in that: by concentration be the ovalbumin of 15.0mg/mL with glucose in mass ratio for 1:1.15 mixes, be dissolved in 20mL phosphate buffer, adjust ph=10.0, after 56 DEG C of isothermal reaction 4.0h, reactant liquor ice bath is cooled to room temperature rapidly, obtains modified ovalbumin.
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| CN108378193A (en) * | 2018-04-08 | 2018-08-10 | 长江大学 | A kind of composite modified method for improving ovalbumin emulsibility |
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| CN110074353A (en) * | 2019-06-04 | 2019-08-02 | 吉林大学 | A kind of preparation method of high grafting degree pectin egg white product |
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| CN102960535A (en) * | 2012-12-17 | 2013-03-13 | 东北农业大学 | Method for preparing efficient protein emulsifier by compounding and modifying |
| CN103387612A (en) * | 2013-06-25 | 2013-11-13 | 南昌大学 | Rapid glycosylation method for modifying egg white protein |
| CN103652316A (en) * | 2013-12-18 | 2014-03-26 | 东北农业大学 | Preparation method of modified isolated soy protein with high emulsibility and high solubility |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN108378193A (en) * | 2018-04-08 | 2018-08-10 | 长江大学 | A kind of composite modified method for improving ovalbumin emulsibility |
| CN108378193B (en) * | 2018-04-08 | 2021-08-20 | 长江大学 | Method for improving ovalbumin emulsibility through composite modification |
| CN109170128A (en) * | 2018-07-12 | 2019-01-11 | 安徽省碧绿春生物科技有限公司 | A kind of method of modifying of Gluten |
| CN110074353A (en) * | 2019-06-04 | 2019-08-02 | 吉林大学 | A kind of preparation method of high grafting degree pectin egg white product |
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