可溶性重组型转谷氨酸酶用于交联植物蛋白水解酸
Han Liu1, Ishita Ghosh2, Corinne Nardin3
1Department of Food Science, The Pennsylvania State University, University Park, PA 16802, USA; Universite de Pau et des Pays de l'Adour, CNRS, IPREM, Pau 64053, France.
Food chemistry
|October 12, 2025
概括
研究人员从南极鱼中开发出一种冷活性转质氨酶 (TGase). 这种酶在低温下有效地交叉连接植物蛋白,改善它们在食品应用中的特性.
科学领域:
- 生物化学 生物化学
- 食品科学 食品科学 食品科学
- 蛋白质工程是指蛋白质工程.
背景情况:
- 冷活性酶在低温加工中提供了独特的优势.
- 冷活性转质氨酶 (TGase) 的商业可用性有限.
- 南极是一种新型冷活性酶的潜在来源.
研究的目的:
- 为了实现来自南极的冷活性TGas的重组表达.
- 为了评估该酶在交叉连接植物蛋白质水解盐中的有效性.
- 描述由酶引起的结构和功能变化.
主要方法:
- 南极鱼TGase在大肠杆菌中的重组表达.
- 优化诱导条件以实现高溶解度.
- 豆蛋白水解盐 (PPH) 的酶性交联.
- 使用SDS-PAGE,MALDI-TOF,光谱,FTIR和热重力测量分析进行分析.
主要成果:
- 重组TGase (rTGase) 在低温度 (4°C) 的高溶解度和活性.
- 通过rTGase成功交叉连接PPH,形成共价异酸键.
- 改善了交联PPH (CL-PPH) 的分子重量分布,结构完整性和热稳定性.
- 在CL-PPH中证明了形状重组和增加的分子紧性.
结论:
- 从南极鱼中成功生产了一种新型的冷活性RT气.
- rTGase有效地改变了植物蛋白质水解的物理化学特性.
- 这为开发用于冷加工食品和温度敏感应用的功能成分提供了有前途的战略.
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