数字农科院2.0

pH-Tunable gliadin-chitosan-lipase ternary complexes enabling efficient interfacial synthesis of phytosterol ester

文献类型： 外文期刊

作者： Zheng, Huanyu;Zhang, Ji;Sun, Zhouliang;Wang, Mengqi;Zhang, Yufei;Zheng, Mingming

作者机构：

关键词： Gliadin-chitosan matrix;Trinary complex;Pickering interfacial biocatalysis;Phytosterol ester

期刊名称： FOOD RESEARCH INTERNATIONAL

ISSN： 0963-9969

年卷期： 2025 年 226 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： Nature employs non-catalytic scaffold proteins to achieve precise enzyme positioning and enhanced catalysis. However, mimicking this approach with food-grade macromolecular materials remains a significant challenge. Herein, we introduce a pH-tunable gliadin-chitosan matrix designed to act as a bioinspired scaffold. It spontaneously self-assembles with lipase into stable ternary complex, gliadin-chitosan-lipase (GCL), through robust hydrogen bonding and hydrophobic interactions (Delta G_binding = -331.7 kJ.mol- 1) immobilize lipase AYS in an optimally active conformation. Upon addition to an oil-water mixture at pH 7, GCL particles adsorb at the interface, creating a highly efficient Pickering interfacial biocatalysis (PIB) system. When applied to the synthesis of sterol esters via interesterification with flaxseed oil, the GCL-stabllized PIB system achieved an 81.4 % yield within 6 h, a relative conversion rate of almost three times that of free lipase (31.8 %), and maintained 73.4 % of its initial activity after five consecutive cycles. Its compatibility extended to six commercial oils. Molecular dynamics results indicated that lipase acts as a regulatory element, suppressing global fluctuations to generate stable structures with high catalytic activity, thereby preparing the interface for biocatalysis. This work establishes a sustainable, scalable platform for functional lipid production and provides a blueprint for nextgeneration biomacromolecular enzyme carriers.

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