Effects of magnetic fields on the enzymatic synthesis of naringin palmitate

Xia Zhang; Liting Wan; Lin Li; Zhenbo Xu; Jianyu Su; Bing Li; Jianrong Huang

doi:10.1039/c8ra01441h

Effects of magnetic fields on the enzymatic synthesis of naringin palmitate

RSC Adv. 2018 Apr 10;8(24):13364-13369. doi: 10.1039/c8ra01441h. eCollection 2018 Apr 9.

Authors

Xia Zhang^{1

2}, Liting Wan¹, Lin Li³, Zhenbo Xu^{1

4}, Jianyu Su¹, Bing Li^{1

2}, Jianrong Huang⁵

Affiliations

¹ School of Food Science and Engineering, South China University of Technology Guangzhou 510640 China bli@scut.edu.cn.
² Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety Guangzhou 510640 China.
³ School of Chemical Engineering and Energy Technology, Dongguan University of Technology College Road 1 Dongguan 523808 China.
⁴ Department of Microbial Pathogenesis, Dental School, University of Maryland Baltimore MD 21201 USA.
⁵ School of Food Science, Guangdong Pharmaceutical University Zhongshan 528458 China joanjr@126.com.

Abstract

The effects of magnetic fields on the enzymatic synthesis of naringin palmitate were studied. Both immobilized Candida Antarctica lipase B (I-CALB) and I-CALB tert-amyl alcohol solution were treated with magnetic fields of 100, 300, or 500 mT for 1, 2, or 3 h. Characteristics including the initial rate and the conversion yields after 24 h of reaction with magnetized I-CALB (M-I-CALB) and magnetized I-CALB tert-amyl alcohol solution (M-I-CALB-S) were investigated. Magnetic field application to both I-CALB and I-CALB-S influenced I-CALB activity. Enzyme activity increased for M-I-CALB and M-I-CALB-S with some intensities and durations and reached maxima at certain frequencies. Enzyme inactivation was only found with M-I-CALB exposed to a strong magnetic field (500 mT) for a long time (3 h). Unlike M-I-CALB, M-I-CALB-S exposed to a strong magnetic field for a long time (500 mT, 3 h) showed greater activity enhancement relative to I-CALB. Fourier transform infrared spectroscopy (FT-IR) results showed that the relative secondary structure content of free CALB was changed only slightly by the differing magnetic field intensities and durations. These findings should prove valuable for using magnetic fields in enzymatic reactions.