CN105928750B - A kind of highly dissoluble red bean protein isolate processing method - Google Patents
A kind of highly dissoluble red bean protein isolate processing method Download PDFInfo
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- CN105928750B CN105928750B CN201610224641.4A CN201610224641A CN105928750B CN 105928750 B CN105928750 B CN 105928750B CN 201610224641 A CN201610224641 A CN 201610224641A CN 105928750 B CN105928750 B CN 105928750B
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- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 186
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 186
- 240000001417 Vigna umbellata Species 0.000 title claims abstract description 184
- 235000011453 Vigna umbellata Nutrition 0.000 title claims abstract description 184
- 238000003672 processing method Methods 0.000 title claims abstract description 16
- 239000000843 powder Substances 0.000 claims abstract description 80
- 238000005259 measurement Methods 0.000 claims abstract description 48
- 238000000034 method Methods 0.000 claims abstract description 40
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 20
- 238000001506 fluorescence spectroscopy Methods 0.000 claims abstract description 19
- 230000008569 process Effects 0.000 claims abstract description 7
- 239000000523 sample Substances 0.000 claims description 72
- 239000007788 liquid Substances 0.000 claims description 40
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 22
- 239000008367 deionised water Substances 0.000 claims description 17
- 229910021641 deionized water Inorganic materials 0.000 claims description 17
- 239000000243 solution Substances 0.000 claims description 16
- 239000008363 phosphate buffer Substances 0.000 claims description 14
- 238000002360 preparation method Methods 0.000 claims description 12
- 239000006228 supernatant Substances 0.000 claims description 9
- 239000002245 particle Substances 0.000 claims description 8
- 238000012545 processing Methods 0.000 claims description 8
- 230000005284 excitation Effects 0.000 claims description 6
- 238000003756 stirring Methods 0.000 claims description 6
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 5
- 102000002322 Egg Proteins Human genes 0.000 claims description 5
- 108010000912 Egg Proteins Proteins 0.000 claims description 5
- 238000001157 Fourier transform infrared spectrum Methods 0.000 claims description 5
- 235000014103 egg white Nutrition 0.000 claims description 5
- 210000000969 egg white Anatomy 0.000 claims description 5
- MOMKYJPSVWEWPM-UHFFFAOYSA-N 4-(chloromethyl)-2-(4-methylphenyl)-1,3-thiazole Chemical compound C1=CC(C)=CC=C1C1=NC(CCl)=CS1 MOMKYJPSVWEWPM-UHFFFAOYSA-N 0.000 claims description 4
- 238000003556 assay Methods 0.000 claims description 4
- 238000004140 cleaning Methods 0.000 claims description 4
- 238000010790 dilution Methods 0.000 claims description 4
- 239000012895 dilution Substances 0.000 claims description 4
- 238000009826 distribution Methods 0.000 claims description 4
- 238000004108 freeze drying Methods 0.000 claims description 4
- 235000019983 sodium metaphosphate Nutrition 0.000 claims description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 3
- 229910019142 PO4 Inorganic materials 0.000 claims description 3
- 238000004220 aggregation Methods 0.000 claims description 3
- 230000002776 aggregation Effects 0.000 claims description 3
- 229920002301 cellulose acetate Polymers 0.000 claims description 3
- 238000001816 cooling Methods 0.000 claims description 3
- 238000002189 fluorescence spectrum Methods 0.000 claims description 3
- 239000005457 ice water Substances 0.000 claims description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 3
- 239000010452 phosphate Substances 0.000 claims description 3
- 239000008055 phosphate buffer solution Substances 0.000 claims description 3
- 239000012488 sample solution Substances 0.000 claims description 3
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N sodium azide Substances [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 claims description 3
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 3
- 229910021642 ultra pure water Inorganic materials 0.000 claims description 3
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- 238000004458 analytical method Methods 0.000 claims description 2
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- 238000000295 emission spectrum Methods 0.000 claims description 2
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- DWNBOPVKNPVNQG-LURJTMIESA-N (2s)-4-hydroxy-2-(propylamino)butanoic acid Chemical compound CCCN[C@H](C(O)=O)CCO DWNBOPVKNPVNQG-LURJTMIESA-N 0.000 claims 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 claims 1
- 238000010521 absorption reaction Methods 0.000 claims 1
- 230000031709 bromination Effects 0.000 claims 1
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- IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 description 4
- 108010073771 Soybean Proteins Proteins 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 235000013305 food Nutrition 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 235000019710 soybean protein Nutrition 0.000 description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 238000000862 absorption spectrum Methods 0.000 description 2
- 238000005187 foaming Methods 0.000 description 2
- 238000002329 infrared spectrum Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
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- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
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- 235000013601 eggs Nutrition 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000011010 flushing procedure Methods 0.000 description 1
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- 239000000203 mixture Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 208000015380 nutritional deficiency disease Diseases 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- XNGIFLGASWRNHJ-UHFFFAOYSA-L phthalate(2-) Chemical compound [O-]C(=O)C1=CC=CC=C1C([O-])=O XNGIFLGASWRNHJ-UHFFFAOYSA-L 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 238000010183 spectrum analysis Methods 0.000 description 1
- 238000002910 structure generation Methods 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
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- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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- G01N1/28—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
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- G01N15/00—Investigating characteristics of particles; Investigating permeability, pore-volume, or surface-area of porous materials
- G01N15/02—Investigating particle size or size distribution
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- G01N21/31—Investigating relative effect of material at wavelengths characteristic of specific elements or molecules, e.g. atomic absorption spectrometry
- G01N21/35—Investigating relative effect of material at wavelengths characteristic of specific elements or molecules, e.g. atomic absorption spectrometry using infrared light
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- G01N21/64—Fluorescence; Phosphorescence
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Abstract
A kind of highly dissoluble red bean protein isolate processing method, the problems such as mainly solving the red bean protein isolate dissolubility difference and microwave treatment conditions not easy to control that existing red bean protein isolate processing method produces.The method comprises the steps of firstly, preparing raw samples, and then microwave treatment prepares the red bean protein isolate powder after microwave treatment;The measurement of secondary structure, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and deliquescent measurement are finally carried out to the red bean protein isolate powder after raw sample and microwave treatment, respectively to characterize red bean protein isolate dissolubility.Process of the invention is widely used, easy to operate and save process time, and red bean protein isolate obtained has compared with highly dissoluble, overcomes the defect of former protein solubility difference.
Description
Technical field
The present invention relates to a kind of highly dissoluble red bean protein isolate processing methods, belong to raw-food material application technology neck
Domain.
Background technique
With advances in technology and the improvement of people's living standards, the requirement to food material is also increasingly strict, tradition
Bean product, since nutrient composition content is lower, long-term consumption will lead to malnutrition, ask to cause serious health
Topic.In recent years, since the protein content of red bean is higher, and it has the characteristics that certain dissolubility and foaming characteristic, therefore
Red bean albumen has become one of the research hotspot of home and abroad gradually.
The fabricated product of red bean is very abundant in production and living, it can be directly used as cooking congee, and cook red bean mud, can also
To be processed into red bean paste, red bean Yoghourt, red bean fibre drink, red bean milk drink, at the same time also from red bean
It extracts natural pigment and utilizes red bean protein isolate production health care product etc..The Chinese patent of Publication No. CN103155998A
One kind is disclosed using red bean as raw material, processes the preparation method of the cool skin of edibility red bean.
The red bean protein isolate protein content with higher extracted merely, but with other modified protein isolate phases
Than dissolubility is poor.And microwave modification is current popular and easily operated method of modifying, microwave is as a kind of frequency range
In the electromagnetic wave of 300MHz~300GHz, the functional character of protein is influenced significantly, researchers at home and abroad have been done this greatly
Quantity research.Cai Jianrong etc. studies microwave treatment time to its foaming characteristic, foam stability, cream using soybean protein isolate as raw material
The influence of the property changed and emulsion stability, obtains 1000 watts of processing 40s of microwave, can improve the functional characteristic of soybean protein isolate.But
It is existing microwave technology defect is that temperature control is poor, it is the not easy to control red bean protein isolate dissolubility for leading to production of temperature, steady
The problem of qualitative difference.
Summary of the invention
The present invention proposes that a kind of highly dissoluble red bean protein isolate processing method, this method are widely used, are easy to operate
And process time is saved, red bean protein isolate obtained has compared with highly dissoluble, overcomes the defect of former protein solubility difference.
To achieve the above object, the present invention adopts the following technical solutions:
A kind of highly dissoluble red bean protein isolate processing method, includes the following steps: to prepare raw sample first, then make
Red bean protein isolate liquid after standby microwave treatment: deionized water is added in the red bean protein isolate powder that freeze-drying is obtained,
The two is mixed with mass volume ratio for the ratio of 1:10, then sodium metaphosphate is added thereto and stirs at room temperature, obtains red bean point
From mixed liquid of protein, then red bean protein isolate mixed liquor is constantly cleaned with deionized water, it will be described red small after cleaning
Beans protein isolate mixed liquor is mixed in equal volume with deionized water, obtains red bean protein isolate liquid, by the red bean
Protein isolate liquid is respectively put into micro-wave oven with 160 watts, 320 watts or 480 watts of power and time at 5 minutes or 10 minutes
Under the conditions of handled, temperature controls the red bean protein isolate liquid at 60-65 DEG C, after obtaining microwave treatment when microwave treatment
Body;Then the red bean protein isolate mixed liquor after microwave treatment is freeze-dried, is placed in 4 DEG C of refrigerators and stores, obtains
Red bean protein isolate powder after to microwave treatment;Finally to the red bean protein isolate powder after raw sample and microwave treatment
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent survey of secondary structure are carried out respectively
It is fixed, to characterize red bean protein isolate dissolubility.
A kind of highly dissoluble red bean protein isolate processing method, is specifically realized by following steps:
A, raw sample is prepared
B, the red bean protein isolate liquid after microwave treatment is prepared
(1) deionized water, the red bean protein isolate powder is added in the red bean protein isolate powder for obtaining freeze-drying
It is mixed, is manufactured in beaker for the ratio of 1:10 with mass volume ratio with deionized water;
(2) 0.1g sodium metaphosphate is added thereto again, is stirred at room temperature for 24 hours with agitating paddle, obtains red bean separation egg
White mixed liquor;
(3) then red bean protein isolate mixed liquor is constantly cleaned with deionized water, until the red bean separates egg
White mixed liquor color and deionized water color are similar;
(4) then the red bean protein isolate mixed liquor after cleaning is mixed in equal volume with deionized water, is obtained red
Red bean protein isolate liquid;
(5) the red bean protein isolate liquid is poured into plate, is put into micro-wave oven with 160 watts, 320 watts or 480
Power and time are handled under conditions of 5 minutes or 10 minutes, guarantee that sample volume per treatment is equal, and microwave
Needs taking-up in every 5 minutes is put into ice-water bath cooling in treatment process, it is ensured that temperature is at 60-65 DEG C, after obtaining microwave treatment
Red bean protein isolate liquid;
C, the red bean protein isolate liquid after microwave treatment that the step b is obtained is freeze-dried, is placed in 4
It is stored in DEG C refrigerator, the red bean protein isolate powder after obtaining microwave treatment;
D, the measurement, interior of secondary structure is carried out to red bean protein isolate powder and the raw sample after the microwave treatment of preparation
Source property fluorescence spectrometry, partial size measuring, surface hydrophobic and deliquescent measurement;
The secondary structure measuring method are as follows: at the microwave for being handled raw sample and different microwave treatment conditions
Red bean protein isolate powder after reason, which is respectively placed in drier, uses P2O5It is sufficiently dry, respectively weigh 1mg, respectively again with 100mg
Potassium bromide is ground tabletting, measures FTIR (Fourier transform infrared spectrum), during data acquisition, steams to reduce water
Interference of the gas to Infrared spectra adsorption continues with dry N2Measuring chamber is eluted, measurement is 4000-400cm in wave-number range-1Respectively
The absorption spectrum of sample, resolution ratio 4cm when measurement-1, wave number precision 0.01cm-1, scanning times 64 times, 25 DEG C of environment temperature;
The intrinsic fluorescence spectroscopy measuring method are as follows: handled raw sample and different microwave treatment conditions
Red bean protein isolate powder sample after microwave treatment is mixed with phosphate buffer same volume ratio respectively, and the phosphate is slow
The concentration of fliud flushing is 0.01mol/L, and the red bean protein isolate concentration of pH 7.0, preparation are 0.15mg/mL, using F-4500
The intrinsic fluorescence spectroscopy of fluorescent spectrophotometer assay red bean protein isolate;
The Particle Size Determination Method are as follows: using ZetaPlus Particle Size Analyzer measurement raw sample and different microwave treatment conditions
The hydrodynamic radius and its distribution, use of red bean protein isolate powder sample after the microwave treatment handled are dense
Degree is the solution that each sample is diluted to a protein concentration of 0.2% by the phosphate buffer of 50mmol/L, pH=7.0, will
Sample after dilution crosses 0.45 μm of cellulose acetate film (water system), is measured at room temperature, takes the average value measured three times to survey
Measure result;
The surface hydrophobic measuring method are as follows: weighed at 0.025g raw sample and different microwave treatment conditions respectively
Red bean protein isolate powder sample after managing obtained microwave treatment, is dissolved in 50mL phosphate buffer, the phosphorus respectively
Phthalate buffer concentration is 0.01mol/L, pH=7.0, stirs 1h at room temperature, is then centrifuged 30 at 10000r/min
Minute, take supernatant Lowry method to measure protein concentration, and successively diluted each sample with the phosphate buffer,
Diluted concentration increases between 0.005-0.5mol/mL and in gradient, takes the sample solution 4mL of various concentration after dilution, respectively
The ANS solution that 40 μ L concentration are 8mmol/L is added, and (the ANS solution uses 0.01mol/L, the phosphate buffer solution of pH7.0
Prepare), 3 minutes are stood after shaking, then uses the fluorescence intensity of F-4500 fluorescent spectrophotometer assay sample;
The dissolubility measuring method are as follows: weigh 500mg raw sample respectively and different microwave treatment conditions handle
10ml ultrapure water is added, in magnetic stirring apparatus in red bean protein isolate powder sample after the microwave treatment arrived thereto respectively
Upper stirring 1h, dissolves it sufficiently, then, is centrifuged 30 minutes under the conditions of 4000rpm, takes 2mL supernatant, be separately added into
2mLNaN3Solution, the supernatant and NaN3The volume ratio of solution is 1:1, then as saving under the conditions of 4 DEG C of refrigerator, is used
The red bean protein isolate aggregation of Lowry method measurement solubility and insolubility.
Further, the plate in the step b (5) is use for laboratory 15mm*15mm plate.
Further, for Panasonic's controllable temperature micro-wave oven, optimum temperature is controlled in 60- the micro-wave oven that the step b (5) uses
62℃。
Further, the map in the secondary structure measuring method is soft with the Peakfit Version 4.12 of Systat
Part is handled, each sub- peak and secondary structure corresponding relationship after processing are as follows: 1610-1640cm-1For beta sheet;1640-1650cm-1For random coil;1650-1660cm-1For alpha-helix;1660-1700cm-1For β-corner.
Further, the contribution of tyrosine, fluorescent emission light are reduced in the intrinsic fluorescence spectroscopy measuring method
For spectrum analysis using the Tryptophan fluorescence group inside protein molecule as probe, fluorescence spectrum excitation wavelength is 290nm, dissipates spectrum
Scanning range is 300-400nm, and exciting slit and divergent slit width are 5nm.
Further, excitation wavelength lambda ex=370nm, emission wavelength lambda em=in the surface hydrophobic measuring method
490nm, crack 5nm map to protein concentration with fluorescence intensity, and initial slope over 10 is the surface hydrophobic of protein.
The beneficial effects of the present invention are:
(1) major ingredient that the present invention uses compensates for traditional soybean protein isolate in nutritional ingredient for red bean protein isolate
The deficiency of aspect.
(2) it is processed in the present invention using microwave phosphorylation (physics and chemistry combination method of modifying), by the red of extraction
Red bean protein isolate carries out microwave treatment, to achieve the purpose that improve red bean protein isolate solubility, convenient for it in health care
Application in terms of food, beverage.
(3) the red bean protein isolate after the processing of microwave phosphorylation, dissolubility significantly improve, and pollution-free, tool
There are preferable thermodynamics, dynamic performance and gelation, overcomes original red bean protein isolate and answered in performances such as dissolubilities
With the limitation of aspect, it has been widened in the development prospect of health care of food, manufacture field.
Detailed description of the invention:
Fig. 1 is the infrared spectrogram of the red bean albumen under different microwave condition processing of the invention;
Fig. 2 is the red bean protein fluorescence spectrogram under different microwave treatment conditions of the invention;
Red bean albumen particle size distribution measuring figure under the different microwave treatment conditions of Fig. 3 present invention;
Fig. 4 is red bean protein surface hydrophobicity measurement chart under different microwave treatment conditions of the invention;
Fig. 5 is red bean protein solubility measurement chart under different microwave treatment conditions of the invention.
Each sample serial number indicates in Fig. 1-Fig. 5: 1- raw sample;Red bean protein isolate liquid after 2- microwave treatment
A;Red bean protein isolate liquid B after 3- microwave treatment;Red bean protein isolate liquid C after 4- microwave treatment;5- microwave
Red bean protein isolate liquid D that treated;Red bean protein isolate liquid E after 6- microwave treatment;After 7- microwave treatment
Red bean protein isolate liquid F.
Specific embodiment
Embodiment 1
A kind of highly dissoluble red bean protein isolate processing method, is specifically realized by following steps:
A, raw sample is prepared
B, the red bean protein isolate liquid after microwave treatment is prepared
(1) deionized water, the red bean protein isolate powder is added in the red bean protein isolate powder for obtaining freeze-drying
It is mixed, is manufactured in beaker for the ratio of 1:10 with mass volume ratio with deionized water;
(2) 0.1g sodium metaphosphate is added thereto again, is stirred at room temperature for 24 hours with agitating paddle, obtains red bean separation egg
White mixed liquor;
(3) then red bean protein isolate mixed liquor is constantly cleaned with deionized water, until the red bean separates egg
White mixed liquor color and deionized water color are similar;
(4) then the red bean protein isolate mixed liquor after cleaning is mixed in equal volume with deionized water, is obtained red
Red bean protein isolate liquid;
(5) the red bean protein isolate liquid is poured into use for laboratory 15mm*15mm plate, be respectively put into micro-wave oven
With power for 160 watts, the time is to be handled under conditions of 5 minutes, and needs taking-up in every 5 minutes is put in microwave processing process
Enter in ice-water bath it is cooling under, it is ensured that temperature is at 60 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as red small
Beans protein isolate liquid A;The micro-wave oven used is Panasonic's controllable temperature micro-wave oven;
C, the red bean protein isolate liquid A after microwave treatment that the step b is obtained is freeze-dried, is placed in
It is stored in 4 DEG C of refrigerators, the red bean protein isolate powder after obtaining microwave treatment is labeled as the red bean separation after microwave treatment
Protein powder A;
D, to after the microwave treatment of preparation red bean protein isolate powder A and raw sample carry out secondary structure measurement,
Intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and deliquescent measurement.
Embodiment 2
A kind of highly dissoluble red bean protein isolate processing method, is specifically realized by following steps:
Difference from Example 1 is that it is 160 watts that the treatment conditions of the step b (5), which are power, and the time is 10 points
Clock, it is ensured that temperature is at 62 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as the red bean after microwave treatment
Protein isolate liquid B.
The step c obtains the red bean protein isolate powder after microwave treatment labeled as the red bean point after microwave treatment
From protein powder B.
The step d is to the red bean protein isolate powder B and raw sample progress second level knot after the microwave treatment of preparation
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of structure.
Embodiment 3
Difference from Example 1 is that it is 320 watts that the treatment conditions of the step b (5), which are power, and the time is 5 points
Clock, it is ensured that temperature is at 61 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as the red bean after microwave treatment
Protein isolate liquid C.
The step c obtains the red bean protein isolate powder after microwave treatment labeled as the red bean point after microwave treatment
From protein powder C.
The step d is to the red bean protein isolate powder C and raw sample progress second level knot after the microwave treatment of preparation
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of structure.
Embodiment 4
Difference from Example 1 is that it is 320 watts that the treatment conditions of the step b (5), which are power, and the time is 10 points
Clock, it is ensured that temperature is at 62 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as the red bean after microwave treatment
Protein isolate liquid D.
The step c obtains the red bean protein isolate powder after microwave treatment labeled as the red bean point after microwave treatment
From protein powder D.
The step d is to the red bean protein isolate powder D and raw sample progress second level knot after the microwave treatment of preparation
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of structure.
Embodiment 5
Difference from Example 1 is that it is 480 watts that the treatment conditions of the step b (5), which are power, and the time is 5 points
Clock, it is ensured that temperature is at 60 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as the red bean after microwave treatment
Protein isolate liquid E.
The step c obtains the red bean protein isolate powder after microwave treatment labeled as the red bean point after microwave treatment
From protein powder E.
The step d is to the red bean protein isolate powder E and raw sample progress second level knot after the microwave treatment of preparation
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of structure.
Embodiment 6
Difference from Example 1 is that it is 480 watts that the treatment conditions of the step b (5), which are power, and the time is 10 points
Clock, it is ensured that temperature is at 62 DEG C, red bean protein isolate liquid after obtaining microwave treatment, labeled as the red bean after microwave treatment
Protein isolate liquid F.
The step c obtains the red bean protein isolate powder after microwave treatment labeled as the red bean point after microwave treatment
From protein powder F.
The step d is to the red bean protein isolate powder F and raw sample progress second level knot after the microwave treatment of preparation
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of structure.
The red bean after red bean protein isolate powder A, microwave treatment point after the microwave treatment that embodiment 1-6 is obtained
From the red bean protein isolate powder C after protein powder B, microwave treatment, the red bean protein isolate powder D after microwave treatment,
Red bean protein isolate powder F after red bean protein isolate powder E, microwave treatment and raw sample after microwave treatment respectively into
Measurement, intrinsic fluorescence spectroscopy measurement, partial size measuring, surface hydrophobic and the deliquescent measurement of row secondary structure, tool
Body measuring method is as follows:
(1) secondary structure measuring method are as follows: at the microwave for being handled raw sample and different microwave treatment conditions
The red bean protein isolate powder B after red bean protein isolate powder A, microwave treatment, the red bean after microwave treatment after reason
The red bean protein isolate powder after red bean protein isolate powder D, microwave treatment after protein isolate powder C, microwave treatment
E, the red bean protein isolate powder F after microwave treatment, which is respectively placed in drier, uses P2O5It is sufficiently dry, 1mg is respectively weighed, respectively
Tabletting is ground with 100mg potassium bromide again, is measured FTIR (Fourier transform infrared spectrum), during data acquisition, is
Interference of the vapor to Infrared spectra adsorption is reduced, is continued with dry N2Measuring chamber is eluted, measurement is in wave-number range
4000-400cm-1The absorption spectrum of each sample, resolution ratio 4cm when measurement-1, wave number precision 0.01cm-1, scanning times 64 times, ring
25 DEG C of border temperature;Map is handled with 4.12 software of Peakfit Version of Systat, each sub- peak and second level after processing
Structure corresponding relationship are as follows: 1610-1640cm-1For beta sheet;1640-1650cm-1For random coil;1650-1660cm-1For
Alpha-helix;1660-1700cm-1For β-corner.
As shown in Figure 1, abscissa represents scanned infrared analyzer scanning wavelength range in figure, ordinate represents measurement result
The infrared absorbency of sample, thus, it can be known that the red bean separation after the microwave treatment obtained after different microwave treatment conditions processing
The secondary structure generation of protein powder is obvious to be understood, α spiral and β-bend increase, and go up high 23% and 17% respectively.
(2) intrinsic fluorescence spectroscopy measuring method are as follows: handled raw sample and different microwave treatment conditions
The red bean protein isolate powder B after red bean protein isolate powder A, microwave treatment after microwave treatment, after microwave treatment
Red bean after red bean protein isolate powder D, microwave treatment after red bean protein isolate powder C, microwave treatment separates egg
Red bean protein isolate powder F sample after white powder end E, microwave treatment is mixed with phosphate buffer same volume ratio respectively, institute
The concentration for stating phosphate buffer is 0.01mol/L, and the red bean protein isolate concentration of pH 7.0, preparation are 0.15mg/mL,
Using the intrinsic fluorescence spectroscopy of F-4500 fluorescent spectrophotometer assay red bean protein isolate;In order to reduce the tribute of tyrosine
It offers, using the Tryptophan fluorescence group inside protein molecule as probe, fluorescence spectrum excitation wavelength is for fluorescent emission spectrum analysis
290nm, diverging spectral scanning range are 300-400nm, and exciting slit and divergent slit width are 5nm.
Measurement result is as shown in Fig. 2, abscissa represents fluorescent scanning wave-length coverage in figure, and ordinate representative sample is in difference
Fluorescence length in wavelength, thus, it can be known that the raising of different condition occurs in different wavelength range for fluorescence intensity, when 320
Watt, the time be 10 minutes under conditions of when, reach maximum fluorescence intensity.
(3) Particle Size Determination Method are as follows: using ZetaPlus Particle Size Analyzer measurement raw sample and different microwave treatment conditions
The red bean protein isolate powder after red bean protein isolate powder A, microwave treatment after the microwave treatment handled
B, after the red bean protein isolate powder C after microwave treatment, the red bean protein isolate powder D after microwave treatment, microwave treatment
Red bean protein isolate powder E, red bean protein isolate powder F sample after microwave treatment hydrodynamic radius and its
Distribution, is diluted to a protein concentration of 0.2% for each sample with the phosphate buffer that concentration is 50mmol/L, pH=7.0
Solution, the sample after dilution is crossed into 0.45 μm of cellulose acetate film (water system), is measured at room temperature, take measure three times it is flat
Mean value is measurement result;
Measurement structure as shown in figure 3, in figure abscissa representative sample molecule particle size, ordinate representative sample is in list
The volume fraction of its contained partial size in the volume of position is 320 watts in power, and the time is under 10 minutes microwave treatment conditions, and partial size is most
It is small, reach 3.2 μm, with dissolubility formed it is good set off, to further illustrate that its dissolubility is improved.
(4) surface hydrophobic measuring method are as follows: weighed at 0.025g raw sample and different microwave treatment conditions respectively
Red bean protein isolate powder A, the red bean protein isolate powder B after microwave treatment, microwave after managing obtained microwave treatment
It is red small after red bean protein isolate powder D, microwave treatment after treated red bean protein isolate powder C, microwave treatment
Red bean protein isolate powder F sample after beans protein isolate powder E, microwave treatment, is dissolved in 50mL phosphate buffer respectively
In (phosphate buffering liquid concentration is 0.01mol/L, pH=7.0), 1h is stirred at room temperature, then in 10000r/
It is centrifuged 30 minutes under min, takes supernatant Lowry method to measure protein concentration, and with the phosphate buffer by each sample
Successively be diluted to 5 concentration at gradient, be 0.005mol/L, 0.05mol/L, 0.1mol/L respectively, 0.3mol/L and
Then 0.5mol/L respectively takes sample solution 4mL, being separately added into the ANS solution that 40 μ L concentration are 8mmol/L, (the ANS solution is adopted
Prepared with the phosphate buffer solution of 0.01mol/L, pH7.0), 3 minutes are stood after shaking, then using F-4500 fluorescence point
The fluorescence intensity of light photometric determination sample;Excitation wavelength lambdaex=370nm, emission wavelength lambdaem=490nm, crack 5nm, with
Fluorescence intensity maps to protein concentration, and initial slope over 10 is the surface hydrophobic of protein.
Measurement result is as shown in figure 4, abscissa representative sample label in figure, the surface hydrophobic of ordinate representative sample,
The results show that being 320 watts in power, it is 125 that the time, which is under 10 minutes microwave treatment conditions, and hydrophobic value reaches highest, with original sample
Condition ratio improves 50.3%, so that further secondary evidence microwave phosphatizing treatment is greatly improved the dissolution of red bean protein isolate
Property.
(5) dissolubility measuring method are as follows: weigh 500mg raw sample respectively and different microwave treatment conditions are handled to obtain
Microwave treatment after red bean protein isolate powder A, the red bean protein isolate powder B after microwave treatment, after microwave treatment
Red bean protein isolate powder C, the red bean protein isolate powder D after microwave treatment, the red bean separation after microwave treatment
10ml ultrapure water is added, in magnetic force in red bean protein isolate powder F sample after protein powder E, microwave treatment thereto respectively
Stir 1h on blender, dissolve it sufficiently, then, be centrifuged 30 minutes under the conditions of 4000rpm, take 2mL supernatant, respectively plus
Enter 2mLNaN3Solution, the supernatant and NaN3The volume ratio of solution is 1:1, then as saving under the conditions of 4 DEG C of refrigerator, is used
The red bean protein isolate aggregation of Lowry method measurement solubility and insolubility.
For measurement result as shown in figure 5, abscissa representative sample label in figure, ordinate represents the molten of sample in unit volume
Xie Du, thus, it can be known that the time is under the conditions of 10 minutes, and it is 44% that solubility, which is optimal value, with original when being 320 watts in power
Sample promotes 65% compared to dissolubility.
Claims (6)
1. a kind of highly dissoluble red bean protein isolate processing method, which is characterized in that specifically realized by following steps:
A, raw sample is prepared
B, the red bean protein isolate liquid after microwave treatment is prepared
(1) the obtained red bean protein isolate powder of freeze-drying is added deionized water, the red bean protein isolate powder with go
Ionized water is mixed with mass volume ratio for the ratio of 1:10, is manufactured in beaker;
(2) 0.1g sodium metaphosphate is added thereto again, is stirred at room temperature for 24 hours with agitating paddle, it is mixed to obtain red bean protein isolate
Close liquid;
(3) then red bean protein isolate mixed liquor is constantly cleaned with deionized water, until the red bean protein isolate is mixed
It closes liquid color and deionized water color is similar;
(4) then the red bean protein isolate mixed liquor after cleaning is mixed in equal volume with deionized water, obtains red bean
Protein isolate liquid;
(5) the red bean protein isolate liquid is poured into plate, is put into micro-wave oven with 160 watts, 320 watts or 480 power
It is handled under conditions of 5 minutes or 10 minutes with the time, guarantees that sample volume per treatment is equal, and microwave treatment
Needs taking-up in every 5 minutes is put into ice-water bath under cooling in the process, it is ensured that temperature is red after obtaining microwave treatment at 60-65 DEG C
Red bean protein isolate liquid;
C, the red bean protein isolate liquid after microwave treatment that the step b is obtained is freeze-dried, is placed in 4 DEG C of ice
It is stored in case, the red bean protein isolate powder after obtaining microwave treatment;
D, to measurement, the endogenous of red bean protein isolate powder and raw sample progress secondary structure after the microwave treatment of preparation
Fluorescence spectrometry, partial size measuring, surface hydrophobic and deliquescent measurement;
The secondary structure measuring method are as follows: after the microwave treatment for being handled raw sample and different microwave treatment conditions
Red bean protein isolate powder be respectively placed in drier and use P2O5It is sufficiently dry, respectively weigh 1mg, respectively again with 100mg bromination
Potassium is ground tabletting, measures Fourier transform infrared spectrum, during data acquisition, in order to reduce vapor to infrared light
The interference absorbed is composed, is continued with dry N2Measuring chamber is eluted, measurement is 4000-400cm in wave-number range-1The absorption of each sample
Spectrum, resolution ratio 4cm when measurement-1, wave number precision 0.01cm-1, scanning times 64 times, 25 DEG C of environment temperature;
The intrinsic fluorescence spectroscopy measuring method are as follows: the microwave for being handled raw sample and different microwave treatment conditions
Treated, and red bean protein isolate powder sample is mixed with phosphate buffer same volume ratio respectively, the phosphate buffer
Concentration be 0.01mol/L, the red bean protein isolate concentration of pH7.0, preparation are 0.15mg/mL, using F-4500 fluorescence
The intrinsic fluorescence spectroscopy of spectrophotometric determination red bean protein isolate;
The Particle Size Determination Method are as follows: carried out using ZetaPlus Particle Size Analyzer measurement raw sample and different microwave treatment conditions
The hydrodynamic radius of red bean protein isolate powder sample after handling obtained microwave treatment and its distribution are with concentration
Each sample is diluted to a protein concentration of 0.2% solution by the phosphate buffer of 50mmol/L, pH=7.0, will be diluted
Sample afterwards crosses 0.45 μm of cellulose acetate film, is measured at room temperature, and taking the average value measured three times is measurement result;
The surface hydrophobic measuring method are as follows: weigh 0.025g raw sample respectively and different microwave treatment conditions handle
Red bean protein isolate powder sample after the microwave treatment arrived, is dissolved in 50mL phosphate buffer, the phosphate respectively
Buffer concentration is 0.01mol/L, pH=7.0, stirs 1h at room temperature, and 30 points are then centrifuged at 10000r/min
Clock takes supernatant Lowry method to measure protein concentration, and is successively diluted each sample with the phosphate buffer, dilute
Concentration is released between 0.005-0.5mol/mL and increased in gradient, take the sample solution 4mL of various concentration after dilution, respectively plus
Enter the ANS solution that 40 μ L concentration are 8mmol/L, the ANS solution uses 0.01mol/L, and the phosphate buffer solution of pH7.0 is matched
System, stands 3 minutes after shaking, and then uses the fluorescence intensity of F-4500 fluorescent spectrophotometer assay sample;
The dissolubility measuring method are as follows: weigh 500mg raw sample respectively and different microwave treatment conditions are handled
Red bean protein isolate powder sample after microwave treatment is added 10ml ultrapure water thereto respectively, stirs on magnetic stirring apparatus
1h is mixed, dissolves it sufficiently, then, is centrifuged 30 minutes under the conditions of 4000rpm, takes 2mL supernatant, be separately added into 2mLNaN3
Solution, the supernatant and NaN3The volume ratio of solution is 1:1, then as saving under the conditions of 4 DEG C of refrigerator, using Lowry method
The red bean protein isolate aggregation of measurement solubility and insolubility.
2. a kind of highly dissoluble red bean protein isolate processing method as described in claim 1, which is characterized in that the step
Plate in b (5) is use for laboratory 15mm*15mm plate.
3. a kind of highly dissoluble red bean protein isolate processing method as described in claim 1, which is characterized in that the step
For Panasonic's controllable temperature micro-wave oven, optimum temperature is controlled at 60-62 DEG C the micro-wave oven that b (5) is used.
4. a kind of highly dissoluble red bean protein isolate processing method as described in claim 1, which is characterized in that the second level
Map in structure determination method is handled with 4.12 software of Peakfit Version of Systat, after processing each sub- peak with
Secondary structure corresponding relationship are as follows: 1610-1640cm-1For beta sheet;1640-1650cm-1For random coil;1650-1660cm-1For alpha-helix;1660-1700cm-1For β-corner.
5. a kind of highly dissoluble red bean protein isolate processing method as described in claim 1, which is characterized in that described endogenous
The contribution of tyrosine is reduced in property fluorescence spectrometry method, fluorescent emission spectrum analysis is with the color inside protein molecule
Propylhomoserin fluorophor is probe, and fluorescence spectrum excitation wavelength is 290nm, and diverging spectral scanning range is 300-400nm, is excited narrow
Seam and divergent slit width are 5nm.
6. a kind of highly dissoluble red bean protein isolate processing method as described in claim 1, which is characterized in that the surface
Excitation wavelength lambda in hydrophobicity measuring methodex=370nm, emission wavelength lambdaem=490nm, crack 5nm, with fluorescence intensity to egg
White concentration mapping, initial slope over 10 is the surface hydrophobic of protein.
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Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1961706A (en) * | 2006-11-21 | 2007-05-16 | 华南理工大学 | Microwave modification method of alcohol processed soybean protein concentrate |
CN101381399A (en) * | 2008-10-09 | 2009-03-11 | 江南大学 | Microwave preparation method of rice protein glycosylation modification |
CN102334588A (en) * | 2011-08-26 | 2012-02-01 | 山东省花生研究所 | Preparation method for enzyme-modified peanut protein |
CN102422975A (en) * | 2011-11-24 | 2012-04-25 | 山东省农业科学院农产品研究所 | Method for pre-extracting peanut protein |
CN105368905A (en) * | 2015-12-09 | 2016-03-02 | 曾志亮 | Microwave-assisted method for preparing pea protein polypeptides |
-
2016
- 2016-04-11 CN CN201610224641.4A patent/CN105928750B/en active Active
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1961706A (en) * | 2006-11-21 | 2007-05-16 | 华南理工大学 | Microwave modification method of alcohol processed soybean protein concentrate |
CN101381399A (en) * | 2008-10-09 | 2009-03-11 | 江南大学 | Microwave preparation method of rice protein glycosylation modification |
CN102334588A (en) * | 2011-08-26 | 2012-02-01 | 山东省花生研究所 | Preparation method for enzyme-modified peanut protein |
CN102422975A (en) * | 2011-11-24 | 2012-04-25 | 山东省农业科学院农产品研究所 | Method for pre-extracting peanut protein |
CN105368905A (en) * | 2015-12-09 | 2016-03-02 | 曾志亮 | Microwave-assisted method for preparing pea protein polypeptides |
Non-Patent Citations (5)
Title |
---|
Microwave-Assisted Phosphorylation of Soybean Protein Isolates and their Physicochemical Properties;Xi-Bo Wang et al.;《Czech Journal of Food Science》;20121231;第30卷(第2期);正文第99-101页 |
Modication of the Soluble Protein Content of Heat-Processed Soybean Flour;Adrian Caprita et al.;《Notulae Botanicae Horti Agrobotanici Cluj-Napoca》;20101231;第38卷(第2期);第98-101页 |
不同改性方法对蛋白质溶解性的影响研究进展;任为聪 等;《中国粮油学报》;20110831;第26卷(第8期);第123-128页 |
微波辅助磷酸化改性提高大豆分离蛋白乳化性的研究;海日罕 等;《中国粮油学报》;20090630;第24卷(第6期);第36-40页 |
微波辐射对大豆浓缩蛋白溶解性的影响;熊犍 等;《食品与发酵工业》;20061231;第32卷(第1期);第107-110页 |
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