转谷氨酰胺酶交联对加热黑豆分离蛋白结构和乳化性能的影响

IF 3.3 2区 农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY
Yue San, Yuejiao Xing, Bailiang Li, Li Zheng
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引用次数: 0

摘要

背景:转谷氨酰胺酶(TGase)是一种耐热的生物催化剂,具有很强的催化活性,在温度和 pH 值适中的条件下也能有效发挥作用,被广泛应用于蛋白质的交联和重组。转谷氨酰胺酶交联是黑豆分离蛋白(BBPI)的一种新型特异性改性方法。本文研究了转谷氨酰胺酶交联对加热 BBPI 结构和乳化性能的影响:十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)分析表明,与不含转谷氨酰胺酶的加热BBPI相比,含转谷氨酰胺酶的加热BBPI分子量更高,而且蛋白质条带随着酶活性的增加而变宽,这表明转谷氨酰胺酶交联促进了蛋白质分子的聚集。高分子量聚合物能更好地稳定油水界面,防止乳液分层。傅立叶变换红外光谱(FTIR)显示,α-螺旋含量从 15.64% 降至 13.75%,β-片状含量从 48.13% 增至 54.08%。α-螺旋含量的减少和β-片状含量的增加可使加热后的BBPI结构更加稳定,并改善其乳化性能。当TG酶为20 U g-1时,蛋白质乳化活性指数(EAI)达到最高值1.87 m2 g-1,乳化稳定性指数(ESI)值为0.27 min (P 2 g-1,分别比未添加TG酶的样品高0.07 min:总之,转谷氨酰胺酶交联对加热 BBPI 的结构和乳化性能有积极影响,可作为改性 BBPI 的有效方法。© 2024 化学工业协会。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Effect of transglutaminase cross-linking on the structure and emulsification performance of heated black bean protein isolate

BACKGROUND

Transglutaminase (TGase) is a heat-resistant biocatalyst with strong catalytic activity, which functions effectively under moderate temperature and pH conditions, and is used widely in protein cross-linking and recombination. Transglutaminase cross-linking is a novel and specific modification method for black bean protein isolate (BBPI). This article investigates the effect of transglutaminase cross-linking on the structure and emulsification performance of heated BBPI.

RESULTS

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that heated BBPI with TGase had a higher molecular weight than heated BBPI without TGase, and the protein bands widened with increasing enzyme activity, indicating that TGase cross-linking promoted protein molecule aggregation. A high molecular weight polymer can better stabilize the oil–water interface, preventing the emulsion from layering. Fourier transform infrared (FTIR) spectroscopy showed that the α-helix content decreased from 15.64% to 13.75%, and the β-sheet content increased from 48.13% to 54.08%. The decrease in α-helix content and increase in β-sheet content could make the structure more stable and improve the emulsifying properties of heated BBPI. When TGase was 20 U g−1, the protein emulsification activity index (EAI) reached its highest value of 1.87 m2 g−1, and the emulsification stability index (ESI) value was 0.27 min (P < 0.05); these figures were 0.19 m2 g−1, and 0.07 min higher, respectively, than in the sample without added TGase.

CONCLUSION

In summary, transglutaminase cross-linking has a positive effect on the structure and emulsification performance of heated BBPI and can be used as an effective method for BBPI modification. © 2024 Society of Chemical Industry.

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来源期刊
CiteScore
8.10
自引率
4.90%
发文量
634
审稿时长
3.1 months
期刊介绍: The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface. Published for SCI by John Wiley & Sons Ltd. SCI (Society of Chemical Industry) is a unique international forum where science meets business on independent, impartial ground. Anyone can join and current Members include consumers, business people, environmentalists, industrialists, farmers, and researchers. The Society offers a chance to share information between sectors as diverse as food and agriculture, pharmaceuticals, biotechnology, materials, chemicals, environmental science and safety. As well as organising educational events, SCI awards a number of prestigious honours and scholarships each year, publishes peer-reviewed journals, and provides Members with news from their sectors in the respected magazine, Chemistry & Industry . Originally established in London in 1881 and in New York in 1894, SCI is a registered charity with Members in over 70 countries.
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