Enhancing the functional characteristics of soy protein isolate via cross-linking catalyzed by Bacillus subtilis transglutaminase
Enhancing the functional characteristics of soy protein isolate via cross-linking catalyzed by Bacillus subtilis transglutaminase
复制标题
通过枯草芽孢杆菌转谷氨酰胺酶催化交联增强大豆分离蛋白的功能特性
DOI：
10.1002/jsfa.11052
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发表时间：
2021-01-13
影响因子：
4.1
通讯作者：
Liu, Yihan
中科院分区：
文献类型：
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作者：
Liu, Yexue;Zhang, Yuanfu;Liu, Yihan
背景：虽然莫巴氏链霉菌转谷氨酰胺酶（MTG）已被广泛应用于通过交联增强大豆分离蛋白（SPI）的功能特性，但自然界中的各种转谷氨酰胺酶（tgg）可能为食品工业提供更多的选择。已有研究报道，源自枯草芽孢杆菌（Bacillus subtilis， BTG）的甘油三酯（TG）具有比mtg更好的pH稳定性和热稳定性。结果：尝试研究了BTG诱导交联对SPI性能的影响。十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）结果表明，在BTG处理下，SPI中几乎所有的蛋白质成分（α′、α、β、AS和BS）都可以交联。BTG处理也显著提高了SPI平均粒径（*P < 0.05）。经BTG处理后，6 h的乳化活性和稳定性由原SPI的0.11535 m(2) g（-1）和48.3%提高到0.13252 m(2) g（-1）和83.9%。同样，改性SPI的泡沫活性（1.32 mL）和稳定性（87.6%）优于原SPI （0.93 mL和56.8%）。SPI凝胶的持水能力随时间的增加而增加，6 h时的持水能力为95.43%。添加BTG后，SPI凝胶的质地曲线明显改善（*P < 0.05）。结论：BTG是一种很有前途的交联剂，可以改善SPI的功能特性。BTG作为MTG的替代品，有望用于食品结构工程，增强多种蛋白质的功能特性，促进食品化学的发展。(c) 2020年化学工业学会
BACKGROUND: Although Streptomyces mobaraense transglutaminase (MTG) has been extensively applied to enhance the functional characteristics of soy protein isolate (SPI) through cross-linking, various transglutaminases (TGs) in nature may provide more choice in the food industry. Previous research reported that TG derived from Bacillus subtilis (BTG) exhibited better pH stability and thermostability than MTG.RESULTS: An attempt was made to study the influence of BTG induced cross-linking on the properties of SPI. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results indicated that almost all protein constituents (alpha', alpha, beta, AS, and BS) in SPI could be cross-linked with BTG treatment. The BTG treatment also resulted in a significant increase (*P < 0.05) in SPI mean particle size. Emulsifying activity and stability were improved from 0.11535 m(2) g(-1) and 48.3% for native SPI to 0.13252 m(2) g(-1) and 83.9% for SPI treated with BTG at 6 h. Similarly, the modified SPI showed better foam activity (1.32 mL) and stability (87.6%) than the original SPI (0.93 mL and 56.8%). The water-holding capacity of SPI gel was found to increase with time, with a value of 95.43% at 6 h. Furthermore, SPI gel's texture profiles were greatly improved by adding BTG (*P < 0.05).CONCLUSION: The results of the present study indicated that BTG could be a promising cross-linking agent for improving the functional characteristics of SPI. As a substitute for MTG, BTG could thus potentially be used for food structure engineering to enhance the functional characteristics of multiple proteins to advance the development of food chemistry. (c) 2020 Society of Chemical Industry