WO2017128556A1 - 蛋白产品及其制备方法 - Google Patents
蛋白产品及其制备方法 Download PDFInfo
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- WO2017128556A1 WO2017128556A1 PCT/CN2016/081942 CN2016081942W WO2017128556A1 WO 2017128556 A1 WO2017128556 A1 WO 2017128556A1 CN 2016081942 W CN2016081942 W CN 2016081942W WO 2017128556 A1 WO2017128556 A1 WO 2017128556A1
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
- C07K14/425—Zeins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/001—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste
- A23J1/005—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste from vegetable waste materials
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable materials
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/12—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from cereals, wheat, bran, or molasses
- A23J1/125—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from cereals, wheat, bran, or molasses by treatment involving enzymes or microorganisms
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
Definitions
- the gluten is separated in the main separation step, and the starch is washed and then subjected to dehydration and drying; and the gluten is concentrated, dehydrated and dried to obtain corn yellow powder; the embryo is dehydrated and dried.
- the corn oil is extracted, the germ bud is obtained, and the fiber is dehydrated and dried, and then the corn mash is sprayed with the germ bud to obtain a fiber protein feed, a sorghum feed and the like.
- the process for preparing zein mainly utilizes the difference in solubility of different prolamin components in the extraction solvent.
- the corn gluten meal produced in the corn wet milling process has a protein dry basis content of about 65 wt%, and further comprises about 15 wt% to 20 wt% starch, 10 wt% to 13 wt% fiber, and about 6 wt% fat.
- the commercial process mainly uses the Swallen 1941 patent (US2287649A) and the Carter and Reck 1970 patent (US3535305), as shown in Figure 3.
- the corn gluten meal is treated batchwise or continuously with isopropanol or 95% ethanol (v/v) at a higher pH and temperature (50-60 ° C), the extract is filtered or centrifuged, and an excess of cold water or low temperature is used (- 10 ° C ⁇ -25 ° C) precipitation of prolamin, dried by vacuum drying to obtain the finished product.
- isopropanol or 95% ethanol v/v
- the hydrolase is selected from the group consisting of an alpha amylase, a saccharification enzyme, a cellulase, a beta-glucanase, a pullulanase, a xylanase, a pectinase, and an Arab One or more of the group consisting of a glycanase and a hemicellulase.
- the alpha amylase is a mold or bacterial alpha amylase, preferably a mold alpha amylase, more preferably an Aspergillus alpha amylase;
- the saccharification enzyme is a mold glucoamylase, preferably Aspergillus or Trichoderma glucoamylase;
- the cellulase is a mold cellulase, preferably a Trichoderma cellulase;
- the ⁇ -glucanase is a fungal or bacterial ⁇ -glucanase; and the pullulanase is a Bacillus pullulanase.
- the enzyme composition is optionally added to the reagent composition when the protease treatment or the hydrolase treatment is performed, and the reagent composition is selected from the group consisting of the following substances.
- a compound capable of opening a disulfide bond in a protein such as a phosphorus-containing compound or a sulfur-containing compound, wherein the phosphorus-containing compound is preferably tris(2-carboxyethyl)phosphine, and the sulfur-containing compound preferably contains a free sulfhydryl group.
- the hydrolase treatment is carried out under the following conditions: pH 3 to 8, preferably 3.3 to 7.5, more preferably 4 to 6.5, most preferably 4.5 to 5.5; and treatment temperature 30 to 72 ° C, It is preferably 35 ° C to 63 ° C, more preferably 40 ° C to 60 ° C, most preferably 45 ° C to 55 ° C; treatment time 0.5 h to 12 h, preferably 1 h to 10 h, more preferably 2 h to 8 h, most preferably 2 h to 7 h; more preferably
- the hydrolase treatment conditions are selected from the group consisting of: pH 5.0, 63 ° C; pH 5.5, 50 ° C; pH 3.0, 35 ° C; pH 6.5, 45 ° C; pH 4.0, 40 ° C; pH 6.5, 45 °C; pH 4.5, 60 ° C; pH 8, 45 ° C; pH 5, 55 ° C; pH 7.5, 50 ° C; pH 3.5
- the filtration is carried out using a filtration pore size of from 1 ⁇ m to 80 ⁇ m, preferably from 10 ⁇ m to 50 ⁇ m, or by a membrane filtration pore size of from 10 nm to 10 ⁇ m, preferably from 20 nm to 1 ⁇ m.
- the protein dry basis accounts for 85 wt% or more, preferably 90 wt% or more, more preferably 94 wt% or more, and most preferably 99 wt% of the protein product. the above.
- the method for preparing the prolamin product of the present invention can realize the content of ⁇ -gliadin and ⁇ -gliadin in the product in a single step while specifically retaining ⁇ -gliadin, without An aqueous solution of an organic solvent is used in the conventional preparation method, and ⁇ -gliadin, ⁇ -gliadin, and ⁇ -gliadin are separated stepwise by adjusting the concentration of the organic solvent.
- FIG. 1 is a schematic diagram of a process flow for extracting prolamin from a zein material.
- the refining 106 is performed, and the granules of suitable size are obtained by 108, and the slurry containing the granules of the material enters into the enzymatically separated and separated by the enzymatic hydrolysis system 112 and the separation system 114 by series, parallel or series-parallel respectively.
- system 110 a portion of the material, such as carbohydrates of starch, fiber, etc., is degraded at 110 and the non-gliadin component is degraded and/or modified and the components are separated.
- device 222 (which may be, for example, a microfiltration membrane device) and 224 (which may, for example, be a plate and frame filter press) may achieve a final separation of the non-gliadin component from the prolamin.
- the filter 246 may have a filter aperture of, for example, 200 mesh.
- 254 may also be two in-line enzyme reactor sets (254-1 and 254-2) in which the material is adjusted to pH 4.2 using hydrochloric acid, adding 0.8% by weight of protein.
- the 254-1 reactor was used to adjust the pH to 8.3 using potassium hydroxide, and the reaction was carried out by adding Bacillus subtilis alkaline protease and 0.1 mM Ca 2+ in an amount of 0.3% by weight at 50 ° C for 0.5 hour.
- an acid or a base acts as a pH adjuster for regulating the reaction in a suitable acid-base environment and also for adjusting the dissolved state of the components.
- Sulfur-containing compounds, phosphorus-containing compounds and metal ions are mainly used to regulate the structure of protein substrates, in particular, to open disulfide bonds in protein substrates, so theoretically any suitable one capable of opening proteins can be selected.
- Metal ions and chelating agents are used to modulate the activity or stability of enzymes such as proteases, carbohydrate enzymes and the like.
- the corn gluten containing 8.9% water and 64% protein (dry basis) was adjusted to a water content of 70%, and then introduced into a hydrolysis tank to adjust to pH 4.8, 45 ° C, and added an acid protease containing 4.8% of the protein content ( MA-SD, Amano Amano Enzyme Preparation Co., Ltd.), 60 mM tris(2-carboxyethyl)phosphine was adjusted to pH 7.5, 52 ° C after 1.2 hours, and 2.6% alkaline protease was added (2709, Pang Bo Bio Engineering Co., Ltd.) was reacted with 2% neutral protease (SUKAPro NE, Su Kehan Bioengineering Co., Ltd.), 1 mM mercaptoethanol for 0.5 hours, centrifuged, washed and collected.
- the total protein content of the obtained product was 61.1%, the prolamin content in the protein was more than 74%, and the ⁇ -gliadin content was 95%, and the ⁇ -
- the second filtrate and the retention are obtained. Liquid, dehydration and drying of the filtrate to obtain protein dry content 95.0% of the corn protein products.
- the above materials were passed through a colloid mill with a disc gap of 20 ⁇ m, and the pH of the ground material was adjusted to 3, 4 and 6.2, respectively, and a filter retentate was obtained using a membrane having a pore size of 10 ⁇ m, and the retentate was centrifuged and dried, respectively.
- the products with protein contents of 71.25%, 70.76% and 70.36% were obtained; when the filter cake was obtained by filtration using a sieve having a pore size of 48 ⁇ m, and the filter cake was dehydrated and dried, the protein contents were 77.7%, 76.8% and 76.3%, respectively. product.
- the pH of the above materials was adjusted to 6.9, 8 and 10.5, respectively, and a permeate was obtained using a filter having a pore size of 1 ⁇ m. After centrifugation and drying, the protein contents were 93.2%, 96.0% and 97.5%, respectively. Protein product; when the filter cake was obtained by filtration using a sieve having a pore size of 75 ⁇ m, and the filter cake was dehydrated and dried, a product having a protein content of 76.9%, 78.8%, and 79.7%, respectively, was obtained.
- Protease 2709, Pangbo Bioengineering Co., Ltd. and 2% neutral protease (metalloproteinase SUKAPro NE, Su Kehan Bioengineering Co., Ltd.), 1 mM mercaptoethanol were reacted for 0.5 hours, then added with 35 mM EDTA, and filtered through a 10 ⁇ m membrane.
- the second filtrate and filter cake The obtained filter cake is washed and dried to obtain a zein product having a protein dry content of 90%, and the prolamin content in the protein is more than 74%, and all are ⁇ -gliadin (100%), fat and ash.
- the dry basis content was 1.04% and 4.01%, respectively.
- the second filtrate was filtered through a 1 ⁇ m microfiltration membrane, and the retentate was refined and dehydrated to obtain a product having a protein dry content of 86%.
- WDG wet distiller's grains
- MagicLab MagneticLab, IKA company
- pulverize grinding disc gap about 30 ⁇ m
- the material first enters the first enzymolysis a can, adding 5 wt% of amylase (Liquozyme SCDS, Novozymes Co., Ltd.) and 3 wt% of saccharification enzyme (Spirizyme Ultra, Novozymes Co., Ltd.) at a pH of 3.5 and 30 ° C 2% of pullulanase (Promozyme D2 Novozymes Co., Ltd.), 10% complex amylase (Novozyme NS50013, Novozymes Co., Ltd.), 2 mM magnesium ion and 2 mM calcium ion for 1 hour; Then adjust the pH to 5.6 and add 10% by weight of the fiber-containing composite fiber hydrolase (GC
- the prolamin products of Examples 17-22 also all have direct film forming properties compared to commercially available samples.
- the tensile strength of the protein film of the sample of the invention was also slightly better than that of the reference commercial zein.
- the above zein ethanol solution was injected into an appropriate amount of high-purity water at a high-speed stirring rate of 12,000 rpm, and the alcohol-soluble protein microsphere solution was obtained by controlling the amount of the alcohol-soluble protein in the final system by membrane separation to be 1%.
- the amount of alcohol-soluble protein in the solution was about 3% after decompression and low-temperature evaporation.
- the microsphere solution was placed in a graduated container and stored under refrigerated conditions (4 ° C), and a significant settling time (ie, the precipitated layer volume was greater than 5% of the total solution volume) was recorded during storage.
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Abstract
Description
实施例17 | 实施例18 | 对比例 | 市售玉米醇溶蛋白 | |
聚沉时间(天) | 112 | 105 | 90 | 92 |
Claims (24)
- 一种从原料中富集α-醇溶蛋白的方法,所述原料包含醇溶蛋白和非醇溶蛋白,并且任选包含大分子碳水化合物和/或油脂,其特征在于,所述方法不使用有机溶剂,并包括下述步骤:(1)将所述原料粉碎并调浆;(2)采用蛋白酶处理,将原料中的至少一部分β-醇溶蛋白、γ-醇溶蛋白和非醇溶蛋白进行完全水解或部分水解,并利用粒径差异过滤去除水解产物,从而得到α-醇溶蛋白得以富集的粗产物;(3)将所述粗产物洗涤、脱水、干燥,得到最终产品。
- 如权利要求1所述的方法,其特征在于,所述原料选自于由玉米黄粉、玉米胚乳发酵醪和酒糟所组成的组。
- 如权利要求1或2所述的方法,其特征在于,所述蛋白酶为选自于由羧基蛋白酶、丝氨酸蛋白酶、金属蛋白酶、巯基蛋白酶所组成的组中的一种或多种。
- 如权利要求3所述的方法,其特征在于,所述羧基蛋白酶为霉菌羧基蛋白酶,优选曲霉羧基蛋白酶,更优选米曲霉羧基内切蛋白酶;所述丝氨酸蛋白酶为芽孢杆菌的丝氨酸蛋白酶,优选枯草杆菌的丝氨酸内切蛋白酶;所述金属蛋白酶为霉菌或芽孢杆菌的金属蛋白酶,优选米曲霉金属内切蛋白酶或枯草芽孢杆菌金属内切蛋白酶;所述巯基蛋白酶为来源于植物的巯基蛋白酶,优选菠萝蛋白酶和/或木瓜蛋白酶。
- 如权利要求1-4中任一项所述的方法,其特征在于,在进行所述蛋白酶处理时,任选加入试剂组合物对酶进行调节,所述试剂组合物为选自于由以下物质所组成的组中的一种或多种:能够打开蛋白中的二硫键的化合物,例如含磷化合物或含硫化合物,其中含磷化合物优选三(2-羧乙基)膦,含硫化合物优选含自由巯基的化合物和/或可提供亚硫酸根的化合物,更优选巯基乙醇、二硫苏糖醇、半胱氨酸及包含半胱氨酸的寡肽(由2-10个氨基酸组成的肽)、亚硫酸盐、亚硫酸、亚硫酸氢盐、焦亚硫酸盐;金属离子,优选碱金属离子、碱土金属离子、二价过渡金属离子,更优选钠离子、钾离子、镁离子、钙离子、锰离子、钴离子、锌离子;金属螯合剂,优选EDTA、EGTA。
- 如权利要求1-5中任一项所述的方法,其特征在于,所述蛋白酶处理在下述条件下进行:pH3.5~10.5,优选3.8~10;处理温度20℃~65℃,优选35℃~55℃;处理时间0.2h~10h,优选0.5h~5h;优选地,所述条件选自于:pH4.8、45℃;pH7.5、52℃;pH3.8、35℃;pH8.3、52℃;pH8.5、65℃;pH6.5、45℃;pH8.0、45℃;pH10.2、45℃;pH4.2、35℃;pH6.5、45℃;pH4.8、55℃;pH4.8、53℃;pH7.2、53℃;pH7.5、25℃;pH10.1、55℃。
- 如权利要求1-6中任一项所述的方法,其特征在于,所述过滤采用1μm~80μm、优选10μm~50μm的过滤孔径进行,或者采用10nm~10μm、优选20nm~1μm的膜过滤孔径进行。
- 如权利要求1-7中任一项所述的方法,其特征在于,在步骤(2)的同时、之前或之后,采用水解酶处理,对原料中的至少一部分大分子碳水化合物进行完全水解或部分水解,并利用粒径差异过滤去除水解产物。
- 如权利要求8所述的方法,其特征在于,所述水解酶选自于由α淀粉酶、糖化酶、纤维素酶、β-葡聚糖酶、普鲁兰酶、木聚糖酶、果胶酶、阿拉伯聚糖酶、半纤维素酶所组成的组中的一种或多种;优选地,所述α淀粉酶为霉菌或细菌的α淀粉酶,优选霉菌α淀粉酶,更优选曲霉α淀粉酶;所述糖化酶为霉菌葡萄糖淀粉酶,优选曲霉或木霉葡萄糖淀粉酶;所述纤维素酶为霉菌纤维素酶,优选木霉纤维 素酶;所述β-葡聚糖酶为真菌或细菌β-葡聚糖酶;所述普鲁兰酶为杆菌普鲁兰酶;优选地,在进行所述水解酶处理时,任选加入试剂组合物对酶进行调节,所述试剂组合物为选自于由以下物质所组成的组中的一种或多种:金属离子,优选碱金属离子、碱土金属离子、二价过渡金属离子,更优选钠离子、钾离子、镁离子、钙离子、锰离子、钴离子、锌离子;金属螯合剂,优选EDTA、EGTA;优选地,所述水解酶处理在如下条件下进行:pH3~8,优选3.3~7.5,更优选4~6.5,最优选4.5~5.5;处理温度30℃~72℃,优选35℃~63℃,更优选40℃~60℃,最优选45℃~55℃;处理时间0.5h~12h,优选1h~10h,更优选2h~8h,最优选2h~7h;更优选地,上述水解酶处理条件选自于:pH5.0、63℃;pH5.5、50℃;pH3.0、35℃;pH6.5、45℃;pH4.0、40℃;pH6.5、45℃;pH4.5、60℃;pH8、45℃;pH5、55℃;pH7.5、50℃;pH3.5、30℃;pH5.6、50℃。
- 一种从原料中提纯得到蛋白产品的方法,所述原料包含β-醇溶蛋白、γ-醇溶蛋白和非醇溶蛋白,并且任选包含大分子碳水化合物和/或油脂,其特征在于,所述方法不使用有机溶剂,并包括下述步骤:(1)将所述原料粉碎并调浆;(2)采用水解酶处理,对原料中的至少一部分大分子碳水化合物进行完全水解或部分水解,并利用粒径差异过滤去除水解产物,从而得到蛋白粗产物;(3)将所述蛋白粗产物洗涤、脱水、干燥,得到最终的蛋白产品。
- 如权利要求10所述的方法,其特征在于,所述原料选自于由玉米黄粉、玉米胚乳发酵醪和酒糟所组成的组。
- 如权利要求10或11所述的方法,其特征在于,所述水解酶选自于由α淀粉酶、糖化酶、纤维素酶、β-葡聚糖酶、普鲁兰酶、木聚糖酶、果胶酶、阿拉伯聚糖酶、半纤维素酶所组成的组中的一种或多种。
- 如权利要求12所述的方法,其特征在于,所述α淀粉酶为霉菌或细菌的α淀粉酶,优选霉菌α淀粉酶,更优选曲霉α淀粉酶;所述糖化酶为霉菌葡萄糖淀粉酶,优选曲霉或木霉葡萄糖淀粉酶;所述纤维素酶为霉菌纤维素酶,优选木霉纤维素酶;所述β-葡聚糖酶为真菌或细菌β-葡聚糖酶;所述普鲁兰酶为杆菌普鲁兰酶。
- 如权利要求10-13中任一项所述的方法,其特征在于,在进行所述水解酶处理时,任选加入试剂组合物对酶进行调节,所述试剂组合物为选自于由以下物质所组成的组中的一种或多种:金属离子,优选碱金属离子、碱土金属离子、二价过渡金属离子,更优选钠离子、钾离子、镁离子、钙离子、锰离子、钴离子、锌离子;金属螯合剂,优选EDTA、EGTA。
- 如权利要求10-14中任一项所述的方法,其特征在于,所述水解酶处理在如下条件下进行:pH3~8,优选3.3~7.5,更优选4~6.5,最优选4.5~5.5;处理温度30℃~72℃,优选35℃~63℃,更优选40℃~60℃,最优选45℃~55℃;处理时间0.5h~12h,优选1h~10h,更优选2h~8h,最优选2h~7h;优选地,上述水解酶处理条件选自于:pH5.0、63℃;pH5.5、50℃;pH3.0、35℃;pH6.5、45℃;pH4.0、40℃;pH6.5、45℃;pH4.5、60℃;pH8、45℃;pH5、55℃;pH7.5、50℃;pH3.5、30℃;pH5.6、50℃。
- 如权利要求10-15中任一项所述的方法,其特征在于,所述过滤采用1μm~80μm、优选 10μm~50μm的过滤孔径进行,或者采用10nm~10μm、优选20nm~1μm的膜过滤孔径进行。
- 如权利要求10-16中任一项所述的方法,其特征在于,在步骤(2)的同时、之前或之后,采用蛋白酶处理,对原料中的至少一部分β-醇溶蛋白、γ-醇溶蛋白和非醇溶蛋白进行完全水解或部分水解,并利用粒径差异过滤去除水解产物。
- 如权利要求17所述的方法,其特征在于,所述蛋白酶为选自于由羧基蛋白酶、丝氨酸蛋白酶、金属蛋白酶、巯基蛋白酶所组成的组中的一种或多种;优选地,所述羧基蛋白酶为霉菌羧基蛋白酶,优选曲霉羧基蛋白酶,更优选米曲霉羧基内切蛋白酶;所述丝氨酸蛋白酶为芽孢杆菌的丝氨酸蛋白酶,优选枯草杆菌的丝氨酸内切蛋白酶;所述金属蛋白酶为霉菌或芽孢杆菌的金属蛋白酶,优选米曲霉金属内切蛋白酶或枯草芽孢杆菌金属内切蛋白酶;所述巯基蛋白酶为来源于植物的巯基蛋白酶,优选菠萝蛋白酶和/或木瓜蛋白酶;优选地,在进行所述蛋白酶处理时,任选加入试剂组合物对酶进行调节,所述试剂组合物为选自于由以下物质所组成的组中的一种或多种:能够打开蛋白中的二硫键的化合物,例如含磷化合物或含硫化合物,其中含磷化合物优选三(2-羧乙基)膦,含硫化合物优选含自由巯基的化合物和/或可提供亚硫酸根的化合物,更优选巯基乙醇、二硫苏糖醇、半胱氨酸及包含半胱氨酸的寡肽(由2-10个氨基酸组成的肽)、亚硫酸盐、亚硫酸、亚硫酸氢盐、焦亚硫酸盐;金属离子,优选碱金属离子、碱土金属离子、二价过渡金属离子,更优选钠离子、钾离子、镁离子、钙离子、锰离子、钴离子、锌离子;金属螯合剂,优选EDTA、EGTA;优选地,所述蛋白酶处理在下述条件下进行:pH3.5~10.5,优选3.8~10;处理温度20℃~65℃,优选35℃~55℃;处理时间0.2h~10h,优选0.5h~5h;更优选地,所述条件选自于:pH4.8、45℃;pH7.5、52℃;pH3.8、35℃;pH8.3、52℃;pH8.5、65℃;pH6.5、45℃;pH8.0、45℃;pH10.2、45℃;pH4.2、35℃;pH6.5、45℃;pH4.8、55℃;pH4.8、53℃;pH7.2、53℃;pH7.5、25℃;pH10.1、55℃。
- 一种蛋白产品,所述蛋白产品包含醇溶蛋白和碳水化合物,其特征在于,所述醇溶蛋白占蛋白干基的70wt%以上;同时,α-醇溶蛋白占所述醇溶蛋白的75wt%以上,β-醇溶蛋白占所述醇溶蛋白的20wt%以下,γ-醇溶蛋白占所述醇溶蛋白的6wt%以下。
- 如权利要求19所述的蛋白产品,其特征在于,所述醇溶蛋白占所述蛋白干基的74wt%以上、优选80wt%以上、更优选85wt%以上、进一步优选90wt%以上、进一步更优选95wt%以上、最优选97wt%以上。
- 如权利要求19或20所述的蛋白产品,其特征在于,所述α-醇溶蛋白占所述醇溶蛋白的77wt%以上、优选85wt%以上、更优选90wt%以上、进一步优选95wt%以上、最优选100wt%。
- 如权利要求19-21中任一项所述的蛋白产品,其特征在于,所述β-醇溶蛋白占所述醇溶蛋白的10wt%以下、优选5wt%以下、更优选3wt%以下、进一步优选2wt%以下、最优选0%。
- 如权利要求19-22中任一项所述的蛋白产品,其特征在于,所述γ-醇溶蛋白占所述醇溶蛋白的10wt%以下、优选5wt%以下、更优选2wt%以下、最优选0%。
- 如权利要求19-23中任一项所述的蛋白产品,其特征在于,所述蛋白干基占所述蛋白产品的85wt%以上、优选90wt%以下、更优选94wt%以上、最优选99wt%以上。
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