Effects of magnetic fields on the enzymatic synthesis of naringin palmitate
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 r...
| Published in: | RSC Advances |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Royal Society of Chemistry
2018
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| Subjects: | |
| Online Access: | http://hdl.handle.net/10713/9277 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85045513143&doi=10.1039%2fc8ra01441h&partnerID=40&md5=02e717e6c0b0bff595194c4e5bdf834e https://doi.org/10.1039/c8ra01441h |
| Summary: | 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. Copyright 2018 The Royal Society of Chemistry. This work is supported by the National Key R&D Program of China (2016YFD0400203), the National Natural Science Foundation of China (No. 31401660), the Pearl River S&T Nova Program of Guangzhou (No. 201806010144) and the Fundamental Research Funds for the Central Universities, SCUT (No. 2017MS093 & 2015zp040). https://dx.doi.org/10.1039/c8ra01441h |
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