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Immobilization for Lipase: Enhanced Activity and Stability by Flexible Combination and Solid Support

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Abstract

In this study, an enhanced activity and stability method for immobilizing porcine pancreatic lipase (PPL) was developed based on ZIF-8 encapsulated supramolecular-modified gold nanoparticle complexes (pSC4-AuNPs@ZIF-8). Supramolecular calix[4]arene (pSC4) can recognize the amino group of PPL through non-covalent force, and this flexible binding method protected the structure of PPL during the immobilization process. Due to the hydrophilic of pSC4-AuNPs and hydrophobic of ZIF-8, PPL can maintain a “lid open” conformation, which can enhance the stability of PPL structure and reduce PPL activity loss. ZIF-8 was used to immobilize PPL to avoid the difficult recovery of free PPL. Compared with the native form of PPL, it exhibited 70.6% maintained activity with terrific pH and temperature stability, and had good performance in thermal stability, time stability, and reusability. In addition, three immobilized PPL methods were designed to further clarify the influence of synthetic methods and additives on the activity and stability of PPL. Importantly, the loading rate of pSC4-AuNPs@ZIF-8@PPL was up to 51.2% among these immobilized PPL systems. Therefore, pSC4-AuNPs@ZIF-8 may serve as a versatile and promising immobilization system for enzymes.

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Data sharing is not applicable to this article as no datasets were generated or analyzed during the current study.

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Funding

This work was supported by the National Natural Science Foundation of China (grant no. 61875114 and 62005156).

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Authors and Affiliations

  1. School of Life Sciences, Shanghai University, Shanghai, 200444, People’s Republic of China

    Ruhui Hu, Yongkai Lu, Han Zhu, Xiaojun Hu & Hongxia Chen

  2. Guangdong Provincial Key Laboratory of Environmental Pollution Control and Remediation Technology, School of Environmental Science and Engineering, Sun Yat-Sen University, Guangzhou, 510275, People’s Republic of China

    Zhijuan Niu & Kai Yan

  3. School of Environmental and Chemical Engineering, Shanghai University, Shanghai, 200444, People’s Republic of China

    Zhihui Mao

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  1. Ruhui Hu
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Contributions

RH, ZN, and YL: data curation, formal analysis, validation, writing—original draft. HZ, ZM, and KY: formal analysis, writing—original draft. XH and HC: conceptualization, resources, funding acquisition, writing—review and editing.

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Correspondence to Xiaojun Hu or Hongxia Chen.

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Hu, R., Niu, Z., Lu, Y. et al. Immobilization for Lipase: Enhanced Activity and Stability by Flexible Combination and Solid Support. Appl Biochem Biotechnol 194, 5963–5976 (2022). https://doi.org/10.1007/s12010-022-04026-z

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