Effect of transglutaminase cross-linking on the structure and emulsification performance of heated black bean protein isolate

IF 3.3 2区农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY Journal of the Science of Food and Agriculture Pub Date : 2024-11-09 DOI:10.1002/jsfa.14008

Yue San, Yuejiao Xing, Bailiang Li, Li Zheng

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Abstract

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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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

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。

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来源期刊

Journal of the Science of Food and Agriculture 工程技术-农业综合

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.