Effects of magnetic fields on the enzymatic synthesis of naringin palmitate. Issue 24 (10th April 2018)

• Record Type: Journal Article
• Authors: Zhang, Xia; Wan, Liting; Li, Lin; Xu, Zhenbo; Su, Jianyu; Li, Bing; Huang, Jianrong
• Is Part Of: RSC advances. Volume 8:Issue 24(2018)
• Page Start: 13364
• Page End: 13369
• Publication Date: 2018-04-10
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c8ra01441h
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Immobilized CALB (I-CALB) and I-CALB solution was treated by magnetic fields and enzymatic reactions with them were compared. 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.