微波双酶协同水解大豆分离蛋白制备小分子肽的研究

研究微波加热条件下，用碱性蛋白酶和胰蛋白酶双酶水解大豆分离蛋白。以氨基氮为评价指标，确定了单酶水解工艺，双酶分步水解的顺序和制备小分子大豆多肽的最佳条件，并通过毛细管电泳方法对水解多肽的分子量进行测定。实验表明：双酶水解优于单酶，制得的大豆肽分子量主要集中在5000以下。     

大豆多肽Alcalase酶解法制备工艺研究及应用

以大豆分离蛋白为原料,选用Alcalase酶,分别从底物浓度、酶解温度、加酶量、酶解pH值和酶解时间等因素来研究Alcalase酶对酶解大豆分离蛋白水解度的影响,并通过正交试验优化了酶解条件,其最佳酶解条件为,底物浓度3%、酶解pH8.0、加酶量5%,酶解温度55℃,酶解时间6h,所得的大豆多肽口感好,含量高.     

大豆多肽木糖醇饮料加工工艺的探讨

以大豆分离蛋白为主要原料,采用木瓜蛋白酶水解SPI 得到大豆多肽,添加适量的功能性甜味剂进行饮料的加 工,并对酶解的最佳工艺条件和加工工艺进行了研究。     

大豆多肽硬糖的工艺研究

以大豆分离蛋白为原料,研究了大豆多肽的制备工艺及大豆多肽硬糖的生产工艺和配方。正交试验结果表明,大豆分离蛋白水解的最佳条件为:酶解温度55℃,酶量(E/S)=0.2%,酶解时间2h;硬糖的最佳配方为:0.8%大豆多肽,0.8%柠檬酸,0.2%苹果酸。     

应用固定化胰蛋白酶制备大豆肽的研究

采用固定化胰蛋白酶水解大豆分离蛋白制备大豆低肽，对固定化胰蛋白酶水解工艺参数等进行了系统研究。结果表明：固定化胰蛋白酶的最适温度为60℃，最适pH为8．7，最佳底物浓度为2．0－3．0mg/mL，大豆分离蛋白的最佳流速为0．3mL/min，大豆分离蛋白的水解率达到45．6％，酶解液中大豆肽含量为1．462mg/mL。酶解液多肽分子量大部分在10000以下。     

应用双固定化酶制备大豆肽的研究

采用固定化胰蛋白酶和固定化木瓜蛋白酶分步对大豆分离蛋白进行水解，水解后酶解液中大豆肽含量为1．628～1．702mg／mL，水解度为54．4％～57．8％。多肽分子量在180以下水解度为11．1％～13．5％，181～2000为11．5％～14．5％，2000～5700为27．1％～27．2％，5700～10000为44．7％～49．6％。结果表明：双固定化酶对大豆分离蛋白的水解作用效率高，并能有效地将大豆分离蛋白降解为分子量更小的大豆肽。     

中性蛋白酶水解大豆分离蛋白的工艺优化

以大豆分离蛋白为原料,利用中性蛋白酶水解法制备活性多肽,并对影响中性蛋白酶水解过程的各个因素进行研究.通过测定大豆分离蛋白酶解液氨基态氮含量,确定中性蛋白酶水解大豆分离蛋白制备活性多肽的的最佳工艺条件:最适pH为7.0,最适温度为45℃,最适酶量为0.80%(w/w),最适底物浓度为6.0%(w/w).在此水解条件下水解大豆分离蛋白4 h,酶解液氨基态氮含量达到1761.38 mg/kg.     

大豆生理活性肽的研究(Ⅰ)--酶法水解的工艺

研究了高水解度大豆多肽的制备和脱盐工艺,采用两种蛋白酶AS1.398和Alcalase水解大豆分离蛋白制得水解度为10%～24%的大豆多肽.结果显示在等电点沉淀分离多肽时,相同水解度下,Alcalase酶水解产物的水解得率比AS1.398酶水解产物的水解得率高20%.采用DA201-C大孔吸附树脂对水解液进行脱盐,得到了优化的吸附和解吸的条件.该条件下大孔吸附树脂对水解液的吸附率为89.71%,解吸率为72.30%.     

碱牲蛋白酶水解大豆分离蛋白的研究

采用Alcalase碱性蛋白酶水解大豆分离蛋白,利用扫描电镜观察不同预热温度对大豆分离蛋白结构的影响.研究了温度、pH、底物浓度、酶与底物比和时间对水解度的影响.通过正交实验及验证实验确定了最佳水解条件为:预热温度90℃、pH8.5、温度55℃、底物浓度为5%、酶与底物比为15%、水解时间4h,水解度为25.12%,多肽得率78.85%.     

风味蛋白酶和中性蛋白酶复合酶解大豆分离蛋白制备多肽的研究

为了改善大豆蛋白的功能性质,使其在食品工业中有更广泛的应用,用酶来水解大豆蛋白,可以提高大豆多肽的产率。本研究以大豆分离蛋白作为底物,配制不同浓度的大豆分离蛋白溶液,经预处理后,用风味蛋白酶、中性蛋白酶进行酶解,得出两种酶的酶解最佳条件,即大豆分离蛋白溶液质量分数为4%、风味蛋白酶和中性蛋白酶比例为3∶1,pH值为7.5、酶解温度为45℃、酶解时间为7h。在此条件下,溶液的水解度最高,经测定多肽含量为5.162%。     

Alcalase酶解制备大豆肽工艺条件的优化

以大豆分离蛋白为原料,研究了用Alcalase碱性蛋白酶水解制备大豆肽。以蛋白水解度和蛋白水解液等电点溶解度为指标,通过单因素试验及正交试验得出最佳水解条件为：料液比1：20,酶解pH8．5,酶解温度60℃,加酶量5400U／g蛋白。此条件下,蛋白水解度为18．79％,等电点溶解度是86．32％。     

Antioxidant activities and functional properties of soy protein isolate hydrolysates obtained using microbial proteases

Soy protein isolate (SPI) hydrolysates were prepared using microbial proteases to produce peptides with antioxidant activity. The process parameters (substrate and enzyme concentrations), hydrolysis time, functional properties and the effects of ultrafiltration were further investigated. The results showed that the soy protein isolate exhibited a 7.0‐fold increase in antioxidant activity after hydrolysis. The hydrolysis parameters, defined by the experimental design, were a substrate concentration of 90 mg mL^?1 and the addition of 70.0 U of protease per mL of reaction. The maximum antioxidant activities were observed between 120 and 180 min of hydrolysis, where the degree of hydrolysis was approximately 20.0%. The hydrolysis increased solubility of the soy protein isolate; however, the hydrolysates exhibited a tendency to decrease in the interfacial activities and the heat stability. The SPI hydrolysates fractions obtained by ultrafiltration showed that the enzymatic hydrolysis resulted in samples with homogenous size and strong antioxidant activity.     

Interaction and Functionality of Mixed Myofibrillar and Enzyme-hydrolyzed Soy Proteins

ABSTRACT Native and briefly heated (85 °C for 3 min) soy protein isolates (SPI) were partially hydrolyzed (4% DH) by Alcalase® and Flavourzyme™ before incorporation into a pork myofibril isolate (MPI) system. The hydrolysis of soy protein enhanced its interaction with MPI, leading to a decreased thermal stability of both soy and muscle proteins. Alcalase SPI hydrolysates, when compared with nonhydrolyzed SPI, improved viscoelastic properties and hardness of MPI gels, while Flavourzyme SPI hydrolysates had an adverse effect. Hydrolyzed SPI augmented emulsifying properties of MPI; the specific efficacy depended upon the type of enzymes used, the SPI:MPI ratio, and whether SPI was heated before hydrolysis.     

酶改性技术在大豆分离蛋白生产中的应用

大豆分离蛋白是一种高纯度的大豆蛋白制品，其中的蛋白质含量在90％以上。其分子量分布范围在1000—500000)道尔顿之间，而且呈非均匀分布，组成非常复杂。本文详细介绍了酶改性技术在大豆分离蛋白生产中的应用，开拓了大豆蛋白的应用范围，为研制大豆多肽打下了基础。     

酶法制备大豆多肽及在酱油发酵中的应用

以脱脂大豆粕为原料,采用复合酶解技术制取大豆多肽酶解液,将制备的大豆多肽应用于酱油发酵前期,并从酱油理化指标、感官评价及香气分析三方面归纳其对酱油主要品质的影响。结果表明,先加中性蛋白酶（温度55 ℃,pH值为6.5,酶用量为4 500 U/g蛋白,酶解3 h）后,再加入碱性蛋白酶（温度55 ℃,pH值为9.0,酶用量为3 000 U/g蛋白,酶解1 h）。此时水解度达22%,多肽得率达10.84%。添加大豆多肽的酿造酱油色泽棕红亮,醇香、酱香浓郁,整体滋味均优于普通酿造酱油。气质联用（GC-MS）鉴定出酱油中含挥发性风味化合物40种,其中主要香气化合物为醇类69.41%、酸类23.06%、醛酮类4.45%、杂环酯类2.47%等,大豆多肽提高了酿造酱油的综合品质,滋味和香气明显优于传统发酵酱油,可用于开发功能营养型酱油。     

大豆分离蛋白ACE活性抑制肽的研究

研究了预处理条件对大豆分离蛋白水解效果的影响,热处理与微波辅助处理相结合能显著提高蛋白酶的水解效率.比较了6种酶解大豆蛋白产物的ACE抑制活性,选择碱性蛋白酶为最佳水解用酶,并优化了酶解条件.研究了8种大孔树脂对水解产物精制效果,结果表明:经D3520型大孔吸附树脂精制后,水解产物脱盐率89.4%,肽回收率90.6%,ACE抑制活性达84.1%.经HPLC法测定,大豆分离蛋白ACE活性抑制肽混合物分子质量主要分布在200～800 ku之间.     

Modification of the nitrogen solubility properties of soy protein isolate following proteolysis and transglutaminase cross-linking

The effect of (a) limited hydrolysis [0.5–2.0% degree of hydrolysis (DH)] with Alcalase™, (b) cross-linking with transglutaminase (TGase) and (c) combinations of these modifications on the nitrogen solubility (pH 3–8) of soy protein isolate (SPI) was investigated. Between pH 3.0 and 5.0, SPI hydrolysates, hydrolysates of cross-linked SPI and the cross-linked products of SPI hydrolysates displayed significant (P<0.05) increases in solubility compared to unmodified SPI. Cross-linking pre- or post hydrolysis did not alter the overall trend of increased (P<0.05) solubility relative to the unmodified control at low pH. At 2% DH, cross-linking pre- or post-hydrolysis resulted in greater solubility (P<0.05) than that observed in hydrolysates per se at low pH. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS–PAGE) indicated that the 22 kDa 11S basic polypeptide was relatively resistant to Alcalase hydrolysis and that the 18 and 22 kDa 11S basic polypeptides were not susceptible to TGase cross-linking. The results demonstrate that a combination of enzymatic treatments and the order in which they are applied may have potential for creating novel food ingredients with improved functional properties, especially those properties that are dependant on high solubility at low pH.     

Physicochemical and Functional Properties of Soy Protein Substrates Modified by Low Levels of Protease Hydrolysis

ABSTRACT: Endo-protease treatments achieving low degrees of hydrolysis (DH 2% and 4%) were used to improve functional properties of hexane-extracted soy flour (HESF), extruded-expelled partially defatted soy flour (EESF), ethanol-washed soy protein concentrate (SPC), and soy protein isolate (SPI). These substrates had protein dispersibility indices ranging from 11% to 89%. Functional properties, including solubility profile (pH 3 to 7), emul-sification capacity and stability, foaming capacity and stability, and apparent viscosity were determined and related to surface hydrophobicity and peptide profiles of the hydrolysates. Protein solubilities of all substrates increased as DH increased. Emulsification capacity and hydrophobicity values of the enzyme-modified HESF and EESF decreased after hydrolysis, whereas these values increased for SPC and SPI. Emulsion stability was improved for all 4% DH hydrolysates. Hydrolyzed SPC had lower foaming capacity and stability. For substrates other than SPC, foaming properties were different depending on DH. Hydrolysis significantly decreased the apparent viscosities regardless of substrate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated differences in the molecular weight profiles of the hydrolysates. HESF and EESF, which had high proportions of native-state proteins, showed minor changes in the peptide profile due to hydrolysis compared with SPC and SPI.     

大豆分离蛋白乳化性的研究

采用蛋白质乳化容量电导法,对不同浓度、ＰＨ和酶水解条件下大豆分离蛋白乳化容量和乳化稳定性进行测定,结果表明：大豆蛋白的乳化性在低密度时随浓度上升而增加,浓度达到６％以后趋于稳定;等电点时（ＰＨ４．５）,乳化性最差,偏离等电点后尤其在偏碱性条件下,乳化性明显增加,酶水解后,乳化性变化产大,水解度１７％时,乳化性最佳。     

大豆蛋白及其水解物的界面流变学行为和搅打性质

为研究不同结构大豆蛋白在空气-水界面处的吸附行为,探究其与搅打起泡性质的关系,本文对大豆分离蛋白(SPI)、β-伴大豆球蛋白(7S)、大豆蛋白选择性水解产物(SPSH)和大豆蛋白限制性水解产物(SPLH)进行了聚丙烯酰胺凝胶电泳(SDS-PAGE)、界面剪切流变学和搅打起泡性的测定。SDS-PAGE表明SPI由7S和11S组成,SPSH选择性水解后11S亚基带消失,仅保留了7S亚基,SPLH水解度1%,仅留下分子量约10 kDa的多肽链。界面剪切流变学行为表明SPI和7S的吸附速度较慢,SPLH可快速吸附至界面上。SPSH同时存在7S和多肽,既可快速吸附至界面,又能形成粘弹性强的界面膜。搅打实验表明SPSH和SPLH的泡沫膨胀率明显增加,分别从450%增至680%和700%。水解可以降低大豆蛋白的分子量,加快蛋白质吸附至界面的速度,从而增加泡沫膨胀率。本研究为大豆蛋白在充气食品的应用提供实际意义。