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Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets

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タイトル: Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets
著者: Yamada, Akane / Kamada, Kai / Ueda, Taro / Hyodo, Takeo / Shimizu, Yasuhiro / Soh, Nobuaki
発行日: 2018年 6月 4日
出版者: Royal Society of Chemistry
引用: RSC Advances, 8(36), pp.20347-20352; 2018
抄録: The present study reports the effects of binding of lipase, which is an inexpensive digestive enzyme (candida antarctica lipase) that catalyzes the hydrolysis reaction and is frequently utilized for artificial synthesis of a variety of organic molecules, to titanate nanosheets (TNSs) on their biocatalytic activities and stabilities under several lipase concentrations. TNSs were prepared through a hydrolysis reaction of titanium tetraisopropoxide (TTIP) with tetrabutylammonium hydroxide (TBAOH), resulting in formation of a colorless and transparent colloidal solution including TNSs with nanometric dimensions (hydrodynamic diameter: ca. 5.6 nm). TNSs were bound to lipase molecules through electrostatic interaction in an aqueous phase at an appropriate pH, forming inorganic-bio nanohybrids (lipase-TNSs). The enzymatic reaction rate for hydrolysis of p-nitrophenyl acetate (pNPA) catalyzed by the lipase-TNSs, especially in diluted lipase concentrations, was significantly improved more than 8 times as compared with free lipase. On the other hand, it was confirmed that heat tolerance of lipase was also improved by binding to TNSs. These results suggest that the novel lipase-TNSs proposed here have combined enhancements of the catalytic activity and the anti-denaturation stability of lipase.
URI: http://hdl.handle.net/10069/38375
DOI: 10.1039/C8RA03558J
権利: © 2018 The Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence.
資料タイプ: Journal Article
原稿種類: publisher
出現コレクション:060 学術雑誌論文

引用URI : http://hdl.handle.net/10069/38375



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