Insight into the Stabilization Mechanism of Succinylation Modification on Black Bean Protein Gels: Molecular Conformation, Microstructure, and Gel Properties

琥珀酰化 微观结构 化学 机制(生物学) 化学改性 生物化学 生物物理学 赖氨酸 氨基酸 生物 结晶学 哲学 认识论
作者
NULL AUTHOR_ID,Wenkang Li,NULL AUTHOR_ID,Yan Chen,Sixian Mu,Lifan Cui,NULL AUTHOR_ID,NULL AUTHOR_ID,Jing Xu,Lianzhou Jiang
出处
期刊:Journal of Agricultural and Food Chemistry [American Chemical Society]
标识
DOI:10.1021/acs.jafc.4c02232
摘要

The objective of this work was to investigate the effect of succinylation treatment on the physicochemical properties of black bean proteins (BBPI), and the relationship mechanism between BBPI structure and gel properties was further analyzed. The results demonstrated that the covalent formation of higher-molecular-weight complexes with BBPI could be achieved by succinic anhydride (SA). With the addition of SA at 10% (v/v), the acylation of proteins amounted to 92.53 ± 1.10%, at which point there was a minimized particle size of the system (300.90 ± 9.57 nm). Meanwhile, the protein structure was stretched with an irregular curl content of 34.30% and the greatest processable flexibility (0.381 ± 0.004). The dense three-dimensional mesh structure of the hydrogel as revealed by scanning electron microscopy was the fundamental prerequisite for the ability to resist external extrusion. The thermally induced hydrogels of acylated proteins with 10% (v/v) addition of SA showed excellent gel elastic behavior (1.44 ± 0.002 nm) and support capacity. Correlation analysis showed that the hydrogel strength and stability of hydrogels were closely related to the changes in protein conformation. This study provides theoretical guidance for the discovery of flexible proteins and their application in hydrogels.
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