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...
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Royal Society of Chemistry
2018
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ftumarylandhshsl:oai:archive.hshsl.umaryland.edu:10713/9277 2023-05-15T14:04:15+02:00 Effects of magnetic fields on the enzymatic synthesis of naringin palmitate Zhang, X. Wan, L. Li, L. 2018 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 en_US eng Royal Society of Chemistry RSC Advances https://www.scopus.com/inward/record.uri?eid=2-s2.0-85045513143&doi=10.1039%2fc8ra01441h&partnerID=40&md5=02e717e6c0b0bff595194c4e5bdf834e http://hdl.handle.net/10713/9277 doi:10.1039/c8ra01441h enzymatic synthesis Enzymes Magnetic Fields Article 2018 ftumarylandhshsl https://doi.org/10.1039/c8ra01441h 2022-06-19T17:01:32Z 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 Article in Journal/Newspaper Antarc* Antarctica UMB Digital Archive (University of Maryland, Baltimore) RSC Advances 8 24 13364 13369 |
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Open Polar |
collection |
UMB Digital Archive (University of Maryland, Baltimore) |
op_collection_id |
ftumarylandhshsl |
language |
English |
topic |
enzymatic synthesis Enzymes Magnetic Fields |
spellingShingle |
enzymatic synthesis Enzymes Magnetic Fields Zhang, X. Wan, L. Li, L. Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
topic_facet |
enzymatic synthesis Enzymes Magnetic Fields |
description |
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 |
format |
Article in Journal/Newspaper |
author |
Zhang, X. Wan, L. Li, L. |
author_facet |
Zhang, X. Wan, L. Li, L. |
author_sort |
Zhang, X. |
title |
Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
title_short |
Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
title_full |
Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
title_fullStr |
Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
title_full_unstemmed |
Effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
title_sort |
effects of magnetic fields on the enzymatic synthesis of naringin palmitate |
publisher |
Royal Society of Chemistry |
publishDate |
2018 |
url |
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 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
RSC Advances https://www.scopus.com/inward/record.uri?eid=2-s2.0-85045513143&doi=10.1039%2fc8ra01441h&partnerID=40&md5=02e717e6c0b0bff595194c4e5bdf834e http://hdl.handle.net/10713/9277 doi:10.1039/c8ra01441h |
op_doi |
https://doi.org/10.1039/c8ra01441h |
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8 |
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24 |
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13364 |
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13369 |
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1766275285417721856 |