Abstract
Candida antarctica lipase B (CALB) was immobilized on Fe3O4/SiOx-g-P(GMA) polymer carrier to catalyzed the transesterification of soybean oil and phytosterol. The enzyme loading of the obtained particles was 98.7 mg/g supports and the enzyme activity was 1226.5 U/g. The average particle size was 100.5 ± 1.30 nm and the magnetization was 15.80 emu/g. The immobilized enzyme showed higher activities at a wider range of pH and temperatures. Its optimum reaction temperature was up to 50 °C; increased by 5 °C compared to the free enzyme. The obtained magnetic immobilized Fe3O4/SiOx-g-P(GMA) lipase was nanoscale. First-grade soybean oils were used as a substrate. System pH was adjusted to 7.0. The optimal reaction temperature was 50 °C and the reaction time was 3 h. The phytosterol concentration of 5% and immobilized CALB of 2% were obtained. The conversion rate of transesterification reaction between soybean oil and phytosterol was 86.2%. The use of magnets can quickly separate the immobilized enzymes from the substrates. The relative activity of the immobilized enzymes was 83.0% when reused seven times. The prepared immobilized CALB can improve efficiently enzyme activity and reutilization.
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Acknowledgements
This work was supported by a grant from the National Natural Science Foundation of China (NSFC): Study on the mechanism of nanomagnetic enzyme hydrolysis of soybean oil by multi-effect orientation and biosynthesis of functional lipids (No: 31571880).
This work was supported by a grant from the Province Natural Science Foundation of Heilong Jang: Study on the Mechanism of Continuous Orientation Esterification of Nanometer Magnetic Lipase (No: C2017019).
This work was also supported by a grant from the National Research Project in 13th Five-Year: Research on Key Technologies of green soybean oil production and large scale intelligent equipment. (No: 2016YFD0401402).
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Yu, D., Zhang, X., Zou, D. et al. Immobilized CALB Catalyzed Transesterification of Soybean Oil and Phytosterol. Food Biophysics 13, 208–215 (2018). https://doi.org/10.1007/s11483-018-9526-7
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DOI: https://doi.org/10.1007/s11483-018-9526-7