CN106174438B - 一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 - Google Patents
一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 Download PDFInfo
- Publication number
- CN106174438B CN106174438B CN201610592086.0A CN201610592086A CN106174438B CN 106174438 B CN106174438 B CN 106174438B CN 201610592086 A CN201610592086 A CN 201610592086A CN 106174438 B CN106174438 B CN 106174438B
- Authority
- CN
- China
- Prior art keywords
- vegetable protein
- emulsion
- enzymatic hydrolysis
- low viscosity
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 239000000839 emulsion Substances 0.000 title claims abstract description 53
- 108010082495 Dietary Plant Proteins Proteins 0.000 title claims abstract description 36
- 230000007071 enzymatic hydrolysis Effects 0.000 title claims abstract description 19
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 title claims abstract description 19
- 230000002378 acidificating effect Effects 0.000 title claims abstract description 18
- 238000000034 method Methods 0.000 title claims abstract description 17
- 238000002360 preparation method Methods 0.000 title claims abstract description 12
- 150000004676 glycans Polymers 0.000 claims abstract description 8
- 150000004804 polysaccharides Polymers 0.000 claims abstract description 3
- 239000002994 raw material Substances 0.000 claims abstract description 3
- 108091008146 restriction endonucleases Proteins 0.000 claims abstract description 3
- 239000000047 product Substances 0.000 claims description 28
- 239000007859 condensation product Substances 0.000 claims description 21
- 239000007788 liquid Substances 0.000 claims description 20
- 239000001785 acacia senegal l. willd gum Substances 0.000 claims description 18
- 239000006185 dispersion Substances 0.000 claims description 18
- 235000018102 proteins Nutrition 0.000 claims description 16
- 102000004169 proteins and genes Human genes 0.000 claims description 16
- 108090000623 proteins and genes Proteins 0.000 claims description 16
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 15
- 102000004190 Enzymes Human genes 0.000 claims description 9
- 108090000790 Enzymes Proteins 0.000 claims description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- 235000010489 acacia gum Nutrition 0.000 claims description 9
- 108091005804 Peptidases Proteins 0.000 claims description 8
- 239000004365 Protease Substances 0.000 claims description 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 8
- 239000003513 alkali Substances 0.000 claims description 8
- 108010073771 Soybean Proteins Proteins 0.000 claims description 6
- 238000006243 chemical reaction Methods 0.000 claims description 6
- 239000005017 polysaccharide Substances 0.000 claims description 6
- 229920001282 polysaccharide Polymers 0.000 claims description 6
- 235000019710 soybean protein Nutrition 0.000 claims description 6
- 230000007062 hydrolysis Effects 0.000 claims description 5
- 238000006460 hydrolysis reaction Methods 0.000 claims description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 5
- 239000003292 glue Substances 0.000 claims description 4
- 235000015112 vegetable and seed oil Nutrition 0.000 claims description 4
- 239000008158 vegetable oil Substances 0.000 claims description 4
- 238000009835 boiling Methods 0.000 claims description 3
- 238000005354 coacervation Methods 0.000 claims description 3
- 230000009849 deactivation Effects 0.000 claims description 3
- 239000005457 ice water Substances 0.000 claims description 3
- 235000017060 Arachis glabrata Nutrition 0.000 claims description 2
- 244000105624 Arachis hypogaea Species 0.000 claims description 2
- 235000010777 Arachis hypogaea Nutrition 0.000 claims description 2
- 235000018262 Arachis monticola Nutrition 0.000 claims description 2
- 108010068370 Glutens Proteins 0.000 claims description 2
- 240000007594 Oryza sativa Species 0.000 claims description 2
- 235000007164 Oryza sativa Nutrition 0.000 claims description 2
- 235000021307 Triticum Nutrition 0.000 claims description 2
- 241000209140 Triticum Species 0.000 claims description 2
- 230000009471 action Effects 0.000 claims description 2
- 235000021312 gluten Nutrition 0.000 claims description 2
- 238000002156 mixing Methods 0.000 claims description 2
- 235000020232 peanut Nutrition 0.000 claims description 2
- 235000009566 rice Nutrition 0.000 claims description 2
- 239000002253 acid Substances 0.000 abstract description 11
- 239000006210 lotion Substances 0.000 abstract description 2
- 238000004519 manufacturing process Methods 0.000 abstract description 2
- 235000013365 dairy product Nutrition 0.000 abstract 1
- 244000068988 Glycine max Species 0.000 description 8
- 235000010469 Glycine max Nutrition 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 7
- 239000006071 cream Substances 0.000 description 5
- 235000005979 Citrus limon Nutrition 0.000 description 4
- 244000131522 Citrus pyriformis Species 0.000 description 4
- 235000013305 food Nutrition 0.000 description 4
- 235000012424 soybean oil Nutrition 0.000 description 4
- 239000003549 soybean oil Substances 0.000 description 4
- 230000007423 decrease Effects 0.000 description 3
- 230000001804 emulsifying effect Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 108010009736 Protein Hydrolysates Proteins 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 230000009881 electrostatic interaction Effects 0.000 description 2
- 239000000413 hydrolysate Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 239000003531 protein hydrolysate Substances 0.000 description 2
- 238000010008 shearing Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 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 description 1
- 102100034613 Annexin A2 Human genes 0.000 description 1
- 108090000668 Annexin A2 Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 239000006057 Non-nutritive feed additive Substances 0.000 description 1
- 230000010718 Oxidation Activity Effects 0.000 description 1
- 101710093543 Probable non-specific lipid-transfer protein Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 229930003779 Vitamin B12 Natural products 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000000991 chicken egg Anatomy 0.000 description 1
- FDJOLVPMNUYSCM-WZHZPDAFSA-L cobalt(3+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+3].N#[C-].N([C@@H]([C@]1(C)[N-]\C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C(\C)/C1=N/C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C\C1=N\C([C@H](C1(C)C)CCC(N)=O)=C/1C)[C@@H]2CC(N)=O)=C\1[C@]2(C)CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@H]1[C@@H](O)[C@@H](N2C3=CC(C)=C(C)C=C3N=C2)O[C@@H]1CO FDJOLVPMNUYSCM-WZHZPDAFSA-L 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000004945 emulsification Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 108010074605 gamma-Globulins Proteins 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000003475 lamination Methods 0.000 description 1
- 239000008268 mayonnaise Substances 0.000 description 1
- 235000010746 mayonnaise Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 235000020124 milk-based beverage Nutrition 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 230000029983 protein stabilization Effects 0.000 description 1
- 238000013139 quantization Methods 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 239000011715 vitamin B12 Substances 0.000 description 1
- 235000019163 vitamin B12 Nutrition 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Landscapes
- Cosmetics (AREA)
- Seasonings (AREA)
- General Preparation And Processing Of Foods (AREA)
Abstract
一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,属于植物蛋白加工领域。本发明是以植物蛋白为原料,通过限制性酶水解,得到的低限度酶解产物与多糖形成复凝聚产物,然后制备乳状液获得的一种以植物蛋白酶解物制备的低粘度高稳定性的酸性乳状液。本发明所用方法简单,操作条件温和,有效的改善了植物蛋白制备的乳液在酸性条件下的稳定性,有利于植物蛋白在酸性稀乳制品中的应用。
Description
技术领域
本发明涉及一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,属于植物蛋白加工领域。
背景技术
植物蛋白的乳化性质利用主要是作为浓缩乳状液中的加工助剂,例如肉糜乳化剂,而作为乳化剂应用于稀的乳状液制品中(如含乳饮料)非常有限,并且由于植物蛋白的豆腥味,或可能导致过敏,有一部分人并不喜欢含有植物蛋白的食品。蛋白质稳定的乳状液的稳定性对pH值较为敏感,在靠近蛋白质等电点附近制备的乳液,由于体系静电斥力的减少,造成乳状液液滴絮凝,絮凝的形成加速植物乳状液体系的分层,破坏乳状液的稳定性,这对植物蛋白稳定的乳状液在酸性条件下的应用是不利的,例如在酸性乳饮料、沙拉酱等方面的应用。对于食品体系,酶解改性是改善蛋白功能性质的一种有效方法。酶解相比于化学处理是一种较为温和的处理方法。限制性酶解能够改善蛋白的乳化性、酸溶性及提高抗氧化活性,但如果水解不是限制性的,通常将会导致不好的功能性质和感官特性出现。酶解通常会破坏蛋白质的三级结构,降低蛋白质的分子量,影响肽段之间的相互作用力以及肽段与外围环境的相互作用力,因此酶解产物的水解程度会直接影响其在气水或油水界面的性质。值得注意的是,较高的水解度(DH)会产生大量导致乳化性质下降的自由氨基酸和短链肽,相反的,较低的DH暴露的疏水性和亲水性残基会加强蛋白质两亲性特征,改善乳化性。
碱性蛋白酶是一种丝氨酸内源性酶,具有广泛的底物特异性,能水解底物中大部分的肽键。由于碱性蛋白酶在低浓度条件下能够有效水解蛋白产生肽片段,并且得到的酶解产物相比于未水解蛋白有较好的功能性质,特别是乳化性质,因此本发明选择碱性蛋白酶用于水解植物蛋白。
对于复杂的食品体系,单一的酶解改性或许不能满足加工需要,有时需要多种改性相互结合来改善食品体系良好的功能性质。已有研究发现蛋白质糖基化后酶解处理得到的产物能够明显改善乳状液稳定性。另外,也有研究发现在蛋白体系中添加多糖,通过调节pH使两者带相反的电荷,促使蛋白和多糖通过静电相互作用形成复凝聚物,此复凝聚物用以制备乳状液可以改善稳定性。很明显,后者的操作较为温和。但是目前对酶解产物-多糖复凝聚物在酸性条件下稳定的乳状液的性质研究不多,通过本发明希望填补国内这方面研究的空白,同时获得一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法。
发明内容
本发明的目的是提供一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法。
本发明的技术方案,一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其以植物蛋白为原料,通过限制性酶水解,得到的低限度酶解产物与多糖形成复凝聚产物,最后制备乳状液,具体步骤为:
(1)植物蛋白在碱性蛋白酶的作用下低限度水解:取质量浓度为5%-10%的植物蛋白溶液在50-60℃下保温30min,用1M NaOH溶液将预热的植物蛋白溶液调至pH7-8,加入碱性蛋白酶150-900U/g蛋白,反应30-180min,反应过程保持温度50-60℃;反应结束迅速在沸水浴灭酶10min,取出迅速放入冰水浴中冷却至室温,得到酶解产物;
(2)酶解产物与多糖复凝聚反应:取步骤(1)所得酶解产物与阿拉伯胶以质量比1︰0.5-6混合,用质量浓度为50%的柠檬酸将混合液的pH调至3-5,不断搅拌1h,得酶解产物-阿拉伯胶复凝聚物分散液;
(3)制备乳状液:按植物油︰酶解产物-阿拉伯胶复凝聚物分散液的体积比为1︰2-10将植物油加入到步骤(2)得到的分散液中,以10000rpm高速剪切1min,30-40MPa下高压均质两次,即得到产品酸性乳状液。
步骤(1)中采用碱性蛋白酶进行水解,加酶量为450U/g蛋白,酶解时间180min,最终水解程度控制为5%。
步骤(1)所述植物蛋白具体为大豆蛋白、花生蛋白、小麦蛋白或大米蛋白。
步骤(2)中酶解产物与阿拉伯胶质量比为1︰1。
步骤(3)中植物油与复凝聚物分散液的体积比为1︰10。
分析方法:
1、水解产物分子量分布的确定
采用高效液相色谱法对水解产物的分子量分布进行测定。具体操作步骤为:用流动相配制样品溶液10mg/mL,经孔径0.22µm的膜过滤后,用高效液相色谱仪紫外检测器进行检测。蛋白标准品为:甲状腺球蛋白,牛血清γ-球蛋白,鸡卵清蛋白,马肌红蛋白或维生素B12(分子量范围1350-670000Da)。
色谱条件为:色谱柱:Shodex protein KW-804;流动相:50mM磷酸盐缓冲液(pH7.0);检测波长:280nm;柱温:25℃;信号采集时间30min。
2、植物蛋白酸溶性的测定
用1M HCl将0.5%(质量分数)植物蛋白溶液的pH调至3-5,搅拌1h,10000g冷冻高速离心30min,取上清液,测定上清液中蛋白浓度。测定方法采用BCA法,牛血清蛋白作为标准品。酸溶性(%)=上清液中蛋白含量(g)/总蛋白浓度(g)×100%。
3、乳状液粘度测定
用AR1000旋转流变仪测定粘度变化。测定参数:测试类型Stead State Flow,夹具50mm平板,样品间隙1mm,温度25℃,剪切速率从0s-1~250s-1. 扫描曲线拟合模型η=Kγn-1,η:粘度(Pa∙s),K:相关性系数(Pa·sn),γ:剪切速率(s-1),n:流变行为指数。
4、乳状液稳定性测定
新鲜制备的乳状液取3mL装入样品瓶(1.8cm内径×4.0cm高度),密封,室温下静置14天。观察乳状液分层情况。乳析指数(CI)用于量化表征乳状液的稳定性。乳析指数CI(%)=(样品瓶底部清层高度/乳状液总高度)×100%。乳析指数越小代表稳定性越好。
本发明的有益效果:本发明利用植物蛋白进行低限度酶解并与阿拉伯胶形成可溶性的复凝聚物,在复凝聚物分散液中添加油相,高压均质获得一种以植物蛋白酶解物制备的低粘度高稳定性的酸性乳状液。该发明对于植物蛋白在酸性条件下的应用具有重要意义。
具体实施方式
下面结合具体实施方式对本发明进一步说明,其具体实施方式应该理解为仅为举例说明,不是限定性的,不能以以下举例说明来限定本发明的保护范围。
实施例1 低限度酶解及复凝聚物分散液的制备
将7%(质量分数)大豆蛋白溶液倒入酶解反应器中,连接恒温循环水浴锅,控制温度50℃保温大豆蛋白溶液30min,用1M NaOH溶液将预热的大豆蛋白溶液的pH调至8,加入碱性蛋白酶450U/g蛋白,反应180min,反应过程保持温度50℃。反应结束迅速在沸水浴灭酶10min,取出迅速放入冰水浴冷却至室温。
酶解产物与阿拉伯胶以质量浓度比1︰1混合,用50%质量分数(质量分数)柠檬酸将混合液的pH调至4,不断搅拌1h。酶解产物与多糖通过静电相互作用力发生复凝聚反应,形成复凝聚物。
实施例2 植物蛋白在酸性条件下制备乳状液
0.5%(质量分数)大豆蛋白溶液,用50%(质量分数)柠檬酸将其pH调至4,不断搅拌1h,按大豆油︰大豆蛋白分散液体积比1︰10将大豆油加入到大豆蛋白分散液中,10000rpm高速剪切1min,然后通过高压均质机40MPa下高压均质两次,得到大豆蛋白稳定的乳状液。
实施例3 低限度酶解产物在酸性条件下制备乳状液
0.5%(质量分数)酶解产物溶液,用50%(质量分数)柠檬酸将其pH调至4,不断搅拌1h,按大豆油︰酶解产物分散液体积比1︰10将大豆油加入到酶解产物分散液中,10000rpm高速剪切1min,然后通过高压均质机40MPa下高压均质两次,得到酶解产物稳定的乳状液。
实施例4 植物蛋白-阿拉伯胶复凝聚物在酸性条件下制备乳状液
0.5%(质量分数)大豆蛋白与阿拉伯胶以质量浓度比1︰1混合,用50%(质量分数)柠檬酸将大豆蛋白-阿拉伯胶混合液的pH调至4,不断搅拌1h,按大豆油︰大豆蛋白-阿拉伯胶复凝聚物分散液体积比1︰10将大豆油加入到大豆蛋白-阿拉伯胶复凝聚物分散液中,10000rpm高速剪切1min,然后通过高压均质机40MPa下高压均质两次,得到大豆蛋白-阿拉伯胶复凝聚物稳定的乳状液。
实施例5 酶解产物与阿拉伯胶复凝聚物在酸性条件下制备乳状液
0.5%(质量分数)酶解产物与阿拉伯胶以质量浓度比1︰1混合,用50%(质量分数)柠檬酸将酶解产物-阿拉伯胶混合液的pH调至4,不断搅拌1h,按大豆油︰酶解产物-阿拉伯胶复凝聚物分散液体积比1︰10将大豆油加入到酶解产物-阿拉伯胶复凝聚物分散液中,10000rpm高速剪切1min,然后通过高压均质机40MPa下高压均质两次,得到酶解产物-阿拉伯胶复凝聚物稳定的乳状液。
与实施例2相比,实施例3乳状液的粘度明显降低,相关性系数K由0.410 Pa·sn下降为0.021Pa·sn,但是静置14天后,分层高度增高,乳状液稳定性下降。
与实施例2相比,实施例4的乳状液的粘度降低,相关性系数K由0.410 Pa·sn下降为0.250Pa·sn,但高于实施例3乳状液的粘度,分层高度下降,乳状液稳定性有所改善。
与实施例2-4相比,实施例5乳状液的粘度略高于实施例3,但仍处于较小数值,K值为0.069 Pa·sn;静置14天后,乳状液基本没有出现明显分层现象。
不同乳状液的流变性质(相关性系数)和静置14天后的乳析指数见表1。
表1 乳状液的粘度和乳析指数
。
Claims (5)
1.一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其特征在于:以植物蛋白为原料,通过限制性酶水解,得到的低限度酶解产物与多糖形成复凝聚产物,最后制备乳状液,具体步骤为:
(1)植物蛋白在碱性蛋白酶的作用下低限度水解:取质量浓度为5%-10%的植物蛋白溶液在50-60℃下保温30min,用1M NaOH溶液将预热的植物蛋白溶液调至pH7-8,加入碱性蛋白酶150-900U/g蛋白,反应30-180min,反应过程保持温度50-60℃;反应结束迅速在沸水浴灭酶10min,取出迅速放入冰水浴中冷却至室温,得到酶解产物;
(2)酶解产物与多糖复凝聚反应:取步骤(1)所得酶解产物与阿拉伯胶以质量比1︰0.5-6混合,用质量浓度为50%的柠檬酸将混合液的pH调至3-5,不断搅拌1h,得酶解产物-阿拉伯胶复凝聚物分散液;
(3)制备乳状液:按植物油︰酶解产物-阿拉伯胶复凝聚物分散液的体积比为1︰2-10将植物油加入到步骤(2)得到的分散液中,以10000rpm高速剪切1min,30-40MPa下高压均质两次,即得到产品酸性乳状液。
2.根据权利要求1所述以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其特征在于:步骤(1)中采用碱性蛋白酶进行水解,加酶量为450U/g蛋白,酶解时间180min,最终水解程度控制为5%。
3.根据权利要求1所述以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其特征在于:步骤(1)所述植物蛋白具体为大豆蛋白、花生蛋白、小麦蛋白或大米蛋白。
4.根据权利要求1所述以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其特征在于:步骤(2)中酶解产物与阿拉伯胶质量比为1︰1。
5.根据权利要求1所述以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法,其特征在于:步骤(3)中植物油与复凝聚物分散液的体积比为1︰10。
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201610592086.0A CN106174438B (zh) | 2016-07-26 | 2016-07-26 | 一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201610592086.0A CN106174438B (zh) | 2016-07-26 | 2016-07-26 | 一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 |
Publications (2)
Publication Number | Publication Date |
---|---|
CN106174438A CN106174438A (zh) | 2016-12-07 |
CN106174438B true CN106174438B (zh) | 2019-05-24 |
Family
ID=57494936
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201610592086.0A Active CN106174438B (zh) | 2016-07-26 | 2016-07-26 | 一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN106174438B (zh) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2017080872A1 (en) | 2015-11-13 | 2017-05-18 | Unilever N.V. | Process for the manufacture of an aqueous dispersion comprising mustard bran and oil-in-water emulsion containing such dispersion |
CN107455550B (zh) * | 2017-08-21 | 2018-10-23 | 中国农业科学院农产品加工研究所 | 一种使用花生分离蛋白制备的Pickering乳液及其制备方法 |
CN107828554B (zh) * | 2017-11-08 | 2020-05-22 | 安慕斯科技有限公司 | 婴儿抑菌洗衣皂 |
CN109122906A (zh) * | 2018-09-14 | 2019-01-04 | 南京财经大学 | 一种大米蛋白乳液及其制备方法 |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN105146051A (zh) * | 2015-07-22 | 2015-12-16 | 福建农林大学 | 一种酶法改性提高卵白蛋白乳化性的方法 |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1875749A (zh) * | 2006-07-03 | 2006-12-13 | 广东药学院 | 一种蛋白质-多糖共价聚合物天然食品乳化剂及其制备方法 |
CN104938765B (zh) * | 2015-07-17 | 2018-07-17 | 东北农业大学 | 一种高稳定性大豆蛋白乳液的制备方法 |
-
2016
- 2016-07-26 CN CN201610592086.0A patent/CN106174438B/zh active Active
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN105146051A (zh) * | 2015-07-22 | 2015-12-16 | 福建农林大学 | 一种酶法改性提高卵白蛋白乳化性的方法 |
Non-Patent Citations (3)
Title |
---|
卵白蛋白-阿拉伯胶相互作用及其在油水界面的吸附特性;牛付阁;《中国博士学位论文全文数据库 工程科技I辑》;20151115(第11期);全文 |
大豆蛋白/阿拉伯胶复合物形成机理及其功能性质研究;第6期;《中国博士学位论文全文数据库 工程科技I辑》;20160615;全文 |
大豆蛋白酶解过程中聚集行为的研究;赵沙沙 等;《中国粮油学报》;20140430;第29卷(第4期);第16-21页 |
Also Published As
Publication number | Publication date |
---|---|
CN106174438A (zh) | 2016-12-07 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN106174438B (zh) | 一种以植物蛋白酶解物制备低粘度高稳定性的酸性乳状液的方法 | |
Thaiphanit et al. | Effects of coconut (Cocos nucifera L.) protein hydrolysates obtained from enzymatic hydrolysis on the stability and rheological properties of oil-in-water emulsions | |
Xu et al. | Effect of limited enzymatic hydrolysis on structure and emulsifying properties of rice glutelin | |
Lorieau et al. | Impact of the dairy product structure and protein nature on the proteolysis and amino acid bioaccessiblity during in vitro digestion | |
Hu et al. | Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions | |
Thaiphanit et al. | Physicochemical and emulsion properties of edible protein concentrate from coconut (Cocos nucifera L.) processing by-products and the influence of heat treatment | |
Li et al. | Improvement of emulsifying properties of soy protein through selective hydrolysis: Interfacial shear rheology of adsorption layer | |
Tamm et al. | Functional properties of pea protein hydrolysates in emulsions and spray-dried microcapsules | |
Wouters et al. | Relevance of the functional properties of enzymatic plant protein hydrolysates in food systems | |
Foegeding et al. | Advances in modifying and understanding whey protein functionality | |
Ren et al. | Structural characterization of heat-induced protein particles in soy milk | |
Zhou et al. | Effects of high hydrostatic pressure treatment on structural, allergenicity, and functional properties of proteins from ginkgo seeds | |
Jiang et al. | Oat protein solubility and emulsion properties improved by enzymatic deamidation | |
Bučko et al. | Influence of enzymatic hydrolysis on solubility, interfacial and emulsifying properties of pumpkin (Cucurbita pepo) seed protein isolate | |
van der Ven et al. | Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics | |
Ling et al. | Fabrication egg white gel hydrolysates-stabilized oil-in-water emulsion and characterization of its stability and digestibility | |
Guo et al. | Emulsifying properties of sweet potato protein: Effect of protein concentration and oil volume fraction | |
Shao et al. | Modification of foaming properties of commercial soy protein isolates and concentrates by heat treatments | |
CN104938765B (zh) | 一种高稳定性大豆蛋白乳液的制备方法 | |
Jeske et al. | Impact of protease and amylase treatment on proteins and the product quality of a quinoa-based milk substitute | |
CN102379435B (zh) | 花生蛋白多肽饮料 | |
Zhong et al. | Dynamic gastric stability and in vitro lipid digestion of soybean protein isolate and three storage protein-stabilized emulsions: Effects of ultrasonic treatment | |
Wang et al. | Effect of enzymatic hydrolysis on the physicochemical and emulsification properties of rice bran albumin and globulin fractions | |
Momen et al. | The techno-functional properties of camel whey protein compared to bovine whey protein for fabrication a model high protein emulsion | |
CN109122906A (zh) | 一种大米蛋白乳液及其制备方法 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
GR01 | Patent grant | ||
GR01 | Patent grant |