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<p>A robust and reusable <i>Rhizomucor miehei</i> lipase (RML) biocatalyst was prepared by integrating bio-imprinting with resin immobilization. RML was co-imprinted with lauric acid and polyethylene glycol (PEG600) followed by immobilization on an amine-functionalized epoxy resin (ES-103B), resulting in AE@RML-LA+PEG600. After immobilization process optimization, the AE@RML-LA + PEG 600 was verified by CD, SEM, FTIR, and XRD analysis. AE@RML-LA+PEG600 exhibited improved thermal, pH, and organic solvent stability compared with free RML. Under optimized conditions (10&#xa0;h, 62&#xa0;°C, palmitic-acid-enriched palm stearin/oleic acid = 1:10&#xa0;mol/mol, 10 wt% enzyme), AE@RML-LA+PEG600 achieved a maximum OPO content of 45.80%, and the proportion of palmitic acid at the sn-2 position relative to total palmitic acid ((sn-2, P)/P) was 54.59%, which was higher than that of the unimprinted enzyme (35.52% OPO). After five cycles, AE@RML-LA+PEG600 maintained 69.52% of its original catalytic activity, indicating its excellent operational stability. This work provides a promising imprinting-immobilization strategy for preparing durable lipases for industrial OPO production.</p>

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Preparation of an immobilized bio-imprinted Rhizomucor miehei lipase for the synthesis of 1,3-dioleoyl-2-palmitoylglycerol

  • 期刊论文

  • 发表日期：

    2026年5月21日

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  • Yuanshan Wang,
  • Ping Liu,
  • Xiaobo Yang,
  • Jiabao Xu,
  • Haibin Qin,
  • Chunyue Weng,
  • Yuguo Zheng

摘要

A robust and reusable Rhizomucor miehei lipase (RML) biocatalyst was prepared by integrating bio-imprinting with resin immobilization. RML was co-imprinted with lauric acid and polyethylene glycol (PEG600) followed by immobilization on an amine-functionalized epoxy resin (ES-103B), resulting in AE@RML-LA+PEG600. After immobilization process optimization, the AE@RML-LA + PEG 600 was verified by CD, SEM, FTIR, and XRD analysis. AE@RML-LA+PEG600 exhibited improved thermal, pH, and organic solvent stability compared with free RML. Under optimized conditions (10 h, 62 °C, palmitic-acid-enriched palm stearin/oleic acid = 1:10 mol/mol, 10 wt% enzyme), AE@RML-LA+PEG600 achieved a maximum OPO content of 45.80%, and the proportion of palmitic acid at the sn-2 position relative to total palmitic acid ((sn-2, P)/P) was 54.59%, which was higher than that of the unimprinted enzyme (35.52% OPO). After five cycles, AE@RML-LA+PEG600 maintained 69.52% of its original catalytic activity, indicating its excellent operational stability. This work provides a promising imprinting-immobilization strategy for preparing durable lipases for industrial OPO production.