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Enhanced Biocatalytic Esterification with Lipase-Immobilized Chitosan/Graphene Oxide Beads
http://hdl.handle.net/10228/00006589
http://hdl.handle.net/10228/000065897a2dbb93-bb4c-4501-9c4b-54b7d48dc3a5
名前 / ファイル | ライセンス | アクション |
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pone9_e104695.PDF (8.6 MB)
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Item type | 学術雑誌論文 = Journal Article(1) | |||||||||||
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公開日 | 2018-02-28 | |||||||||||
資源タイプ | ||||||||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||||
資源タイプ | journal article | |||||||||||
タイトル | ||||||||||||
タイトル | Enhanced Biocatalytic Esterification with Lipase-Immobilized Chitosan/Graphene Oxide Beads | |||||||||||
言語 | ||||||||||||
言語 | eng | |||||||||||
著者 |
Lau, Siaw Cheng
× Lau, Siaw Cheng× Lim , Hong Ngee× Basri, Mahiran× Masoumi, Hamid Reza Fard× Tajudin, Asilah Ahmad× Huang, Nay Ming× Pandikumar, Alagarsamy× Chia, Chi Hua× 安藤, 義人
WEKO
21654
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抄録 | ||||||||||||
内容記述タイプ | Abstract | |||||||||||
内容記述 | In this work, lipase from Candida rugosa was immobilized onto chitosan/graphene oxide beads. This was to provide an enzyme-immobilizing carrier with excellent enzyme immobilization activity for an enzyme group requiring hydrophilicity on the immobilizing carrier. In addition, this work involved a process for the preparation of an enzymatically active product insoluble in a reaction medium consisting of lauric acid and oleyl alcohol as reactants and hexane as a solvent. This product enabled the stability of the enzyme under the working conditions and allowed the enzyme to be readily isolated from the support. In particular, this meant that an enzymatic reaction could be stopped by the simple mechanical separation of the “insoluble” enzyme from the reaction medium. Chitosan was incorporated with graphene oxide because the latter was able to enhance the physical strength of the chitosan beads by its superior mechanical integrity and low thermal conductivity. The X-ray diffraction pattern showed that the graphene oxide was successfully embedded within the structure of the chitosan. Further, the lipase incorporation on the beads was confirmed by a thermo-gravimetric analysis. The lipase immobilization on the beads involved the functionalization with coupling agents, N-hydroxysulfosuccinimide sodium (NHS) and 1-ethyl-(3-dimethylaminopropyl) carbodiimide (EDC), and it possessed a high enzyme activity of 64 U. The overall esterification conversion of the prepared product was 78% at 60°C, and it attained conversions of 98% and 88% with commercially available lipozyme and novozyme, respectively, under similar experimental conditions. | |||||||||||
書誌情報 |
PLoS ONE 巻 9, 号 8, p. e104695-1-e104695-10, 発行日 2014-08-15 |
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出版社 | ||||||||||||
出版者 | Public Library of Science | |||||||||||
DOI | ||||||||||||
関連タイプ | isIdenticalTo | |||||||||||
識別子タイプ | DOI | |||||||||||
関連識別子 | info:doi/10.1371/journal.pone.0104695 | |||||||||||
ISSN | ||||||||||||
収録物識別子タイプ | ISSN | |||||||||||
収録物識別子 | 1932-6203 | |||||||||||
著作権関連情報 | ||||||||||||
権利情報 | Copyright (c) 2014 Lau et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited | |||||||||||
出版タイプ | ||||||||||||
出版タイプ | VoR | |||||||||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||||
査読の有無 | ||||||||||||
値 | yes | |||||||||||
連携ID | ||||||||||||
6679 |