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对生物合成的全素在热处理后的结构恶化进行洞察

Ranran Pang ¹, Kai Zhou ², Yong Xie ¹

¹School of Food and Biological Engineering, Hefei University of Technology, Engineering Research Center of Bio-Process, Ministry of Education, Hefei 230601, Anhui, China.
²School of Food and Biological Engineering, Hefei University of Technology, Engineering Research Center of Bio-Process, Ministry of Education, Hefei 230601, Anhui, China; Key Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, China; Anhui Chem-Bright Bioengineering CO., LTD, Huaibei 235000, China.
³School of Food and Biological Engineering, Hefei University of Technology, Engineering Research Center of Bio-Process, Ministry of Education, Hefei 230601, Anhui, China; Anhui Zhongqing Inspection and Testing Co., Ltd, Hefei 230088, Anhui, China.
⁴Anhui Zhongqing Inspection and Testing Co., Ltd, Hefei 230088, Anhui, China.
⁵College of Food Science, Southwest University, Chongqing 400715, China.
⁶School of Food and Biological Engineering, Hefei University of Technology, Engineering Research Center of Bio-Process, Ministry of Education, Hefei 230601, Anhui, China; Key Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province, Hefei University of Technology, Hefei 230601, China.
⁷Anhui Chem-Bright Bioengineering CO., LTD, Huaibei 235000, China.

⁰School of Food and Biological Engineering, Hefei University of Technology, Engineering Research Center of Bio-Process, Ministry of Education, Hefei 230601, Anhui, China.

International Journal of Biological Macromolecules +

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2025年九月6日

在PubMed上查看摘要

概括

生物合成的全素 (bs-holoFt) 具有较高的铁容量. 热量会降低其结构和功能,影响铁的释放和纳米酶活性,这对于应用至关重要.

科学领域

生物化学和生物物理
蛋白质工程
纳米技术

背景情况

荷洛费里丁是一种有前途的铁补充剂,但天然提取效率低下,而体外方法可能会破坏其结构.
在生产用于治疗和工业应用的稳定,功能性的全素方面存在挑战.

研究的目的

报告大肠杆菌中高度稳定的全蛋白 (bs-holoFt) 的体内生物合成.
描述热处理对bs-holFt结构和功能的影响.
阐明化机制及其对铁释放和纳米酶活性的影响.

主要方法

在大肠杆菌中全蛋白的体内生物合成.
系统的热处理 (70-100°C) 合成的全素.
多级结构分析 (二级,三级,四级) 和功能测定 (铁释放,过氧化酶类活性).

主要成果

生物合成的全素 (bs-holoFt) 显示出高铁负载能力 (1213 Fe原子/蛋白质).
热处理诱导了一种取决于温度的降解途径:α-螺旋内容的丧失,三级展开,四级拆卸和聚合.
在100°C时,结构衰变与铁释放 (17.7%) 和纳米酶活性 (15.3%) 的显著损失直接相关.

结论

热诱导的变性导致分子通道的结构崩和阻塞,导致全素的功能受损.
这项研究提供了一种稳定的全素生产方法,并为其变性提供了基本的见解.
这些发现为优化铁补充剂和纳米技术中的全素使用提供了理论基础.

关键词:

活动下降铁素铁补充剂蛋白质聚合热变质化

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