Abstract
In this study, Candida antarctica lipase B was immobilized on silica (SiO2) nanoparticles by physical adsorption, and then cross-linked with glutaraldehyde (GA) to prepare cross-linked immobilized lipase (CLIL). During the condition of 1.28 mg/mL lipase concentration, 25 ℃ temperature, 2 h adsorption time, 0.01% GA (V/V) 7.5 mL and 2 h cross-linking time, the highest recovery activity of CLIL reached 87.82 ± 0.07% (22.55 ± 0.025 U/mg). Scanning electron microscope (SEM) and confocal laser scanning microscope (CLSM) confirmed that lipase was immobilized on the surface of SiO2 nanoparticles. The changes in secondary structures of CLIL indicated that cross-linking changed the secondary structure of lipase protein, which made the structure of CLIL more stable. Compared with the free lipase, the thermal stability and storage stability of CLIL was significantly improved, and the t1/2 at 60 °C was extended. Studies had shown that it was a feasible method to obtain CLIL by cross-linking after adsorbing lipase on SiO2 nanoparticles.
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Acknowledgements
This work was supported by the China National Key R&D Program during the 13th Five-year Plan Period [grant numbers 2016YFD0400803] and the Project of Zhejiang University of Technology, China [grant numbers KYY-HX-20210856].
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QJQ conceptualization, funding acquisition, investigation, writing—review and editing, and methodology; HAM writing—original draft, investigation, and data analysis; ZHX writing—original draft, investigation, and data analysis; DJ writing—original draft and data analysis; ZW visualization and investigation; CY methodology and investigation.
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Qian, J., Huang, A., Zhu, H. et al. Immobilization of lipase on silica nanoparticles by adsorption followed by glutaraldehyde cross-linking. Bioprocess Biosyst Eng 46, 25–38 (2023). https://doi.org/10.1007/s00449-022-02810-z
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DOI: https://doi.org/10.1007/s00449-022-02810-z