Enhanced Pickering interfacial biocatalysis in phosphatidylserine synthesis via phospholipase D immobilization with optimized bifunctional strategy

文献类型： 外文期刊

第一作者： Liu, Huihui

作者： Liu, Huihui;Zhang, Yufei;Zheng, Mingming;Liu, Yihan;Han, Zhongmu

作者机构：

关键词： Pickering interfacial biocatalysis; Transphosphatidylylation reaction; Immobilized enzyme; Bifunctional group modification; Hydrogen bond

期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）

ISSN： 0308-8146

年卷期： 2025 年 492 卷

页码：

收录情况： SCI

摘要： Phosphatidylserine (PS) is a high-value phospholipid in functional foods and pharmaceuticals. However, the lack of a suitable biocatalytic system has limited the conversion efficiency. A novel Pickering interfacial biocatalysis (PIB) system has developed for converting phosphatidylcholine (PC) to PS in this work. Three immobilized enzyme carriers were synthesized by grafting different modifying groups onto hollow mesoporous silica particles (HMSP). The combination of NQ-62 and octyl-modified groups yielded the optimal immobilized enzyme, PLD@HMSP-N3/C8. It stabilized the water-in-oil Pickering emulsion and enhanced phospholipase D (PLD) stability via hydrogen bond interactions. Under optimized conditions, a PS conversion of 93.8 % was achieved within 20 min at 40 degrees C, achieving a catalytic efficiency (CE) of 372 mmol/(g & sdot;h). The immobilized PLD demonstrated markedly enhanced thermostability, pH resistance, and protease hydrolysis stability compared to its free and homologous series counterparts. Moreover, it retained 70.9 % of the PS conversion after 10 cycles of reuse.

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