结构变化对过氧化酶活性的影响,在高压结下具有不同的初始状态
Zhanhong Liang1, Yuanshan Yu2, Bo Zou2
1Sericultural & Argi-Food Research Institute, Guangdong Academy of Agricultural Sciences/Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs/Guangdong Key Laboratory of Agricultural Products Processing, No. 133 Yiheng street, Dongguanzhuang road, Tianhe District, Guangzhou 510610, China; School of Food Science, Guangdong Pharmaceutical University, Zhongshan 528400, China.
Food chemistry
|July 18, 2024
概括
高压冷 (HPF) 影响食品中的酶活性. 过氧化酶 (POD) 的较高初始度加强了蛋白质相互作用,在HPF加工过程中增加了酶激活.
科学领域:
- 食品科学 食品科学 食品科学
- 生物物理学的生物物理.
- 酶学 是一种酶学.
背景情况:
- 了解食品加工过程中的酶稳定性至关重要.
- 高压冷 (HPF) 是一种新的食品加工技术.
- HPF对过氧化酶 (POD) 活性的影响需要进一步研究.
研究的目的:
- 为了研究初始状态,压力和结对HPF期间过氧化酶变质化的影响.
- 用光谱和计算机模拟技术分析影响HPF下POD活动的结构变化.
主要方法:
- 研究了固体-液体双相过氧化酶 (低/高度).
- 利用光谱技术监测结构变化.
- 采用计算机模拟来分析分子变化.
主要成果:
- 在HPF期间的POD活动主要受到度的影响,其次是物理状态,压力和结.
- 较高的初始度增加了HL-POD分子直径和高度,增强聚合和酶激活 (6-17%).
- 胺I峰值有效地表明POD活动和结构变化.
结论:
- 初始度是影响HPF期间POD活动的最关键因素.
- 通过特定的结构修改,HPF加工可以导致酶激活.
- 结果为优化HPF技术在含酶的食品中提供了洞察力.
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