Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets
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 biocat...
Main Authors: | , , , , , |
---|---|
Format: | Other/Unknown Material |
Language: | English |
Published: |
Royal Society of Chemistry
2018
|
Subjects: | |
Online Access: | https://nagasaki-u.repo.nii.ac.jp/record/1129/files/RSCA8_20347.pdf |
id |
ftnagasakiuniv:oai:nagasaki-u.repo.nii.ac.jp:00001129 |
---|---|
record_format |
openpolar |
spelling |
ftnagasakiuniv:oai:nagasaki-u.repo.nii.ac.jp:00001129 2024-09-15T17:48:45+00:00 Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets Yamada, Akane Kamada, Kai Ueda, Taro Hyodo, Takeo Shimizu, Yasuhiro Soh, Nobuaki 2018-06-04 application/pdf https://nagasaki-u.repo.nii.ac.jp/record/1129/files/RSCA8_20347.pdf eng eng Royal Society of Chemistry 10.1039/C8RA03558J RSC Advances 36 8 20347 20352 20462069 https://nagasaki-u.repo.nii.ac.jp/record/1129/files/RSCA8_20347.pdf c 2018 The Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. VoR 2018 ftnagasakiuniv 2024-08-23T06:19:39Z 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. RSC Advances, 8(36), pp.20347-20352; 2018 journal article Other/Unknown Material Antarc* Antarctica NAOSITE: Nagasaki University Academic Output SITE |
institution |
Open Polar |
collection |
NAOSITE: Nagasaki University Academic Output SITE |
op_collection_id |
ftnagasakiuniv |
language |
English |
description |
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. RSC Advances, 8(36), pp.20347-20352; 2018 journal article |
format |
Other/Unknown Material |
author |
Yamada, Akane Kamada, Kai Ueda, Taro Hyodo, Takeo Shimizu, Yasuhiro Soh, Nobuaki |
spellingShingle |
Yamada, Akane Kamada, Kai Ueda, Taro Hyodo, Takeo Shimizu, Yasuhiro Soh, Nobuaki Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
author_facet |
Yamada, Akane Kamada, Kai Ueda, Taro Hyodo, Takeo Shimizu, Yasuhiro Soh, Nobuaki |
author_sort |
Yamada, Akane |
title |
Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
title_short |
Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
title_full |
Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
title_fullStr |
Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
title_full_unstemmed |
Enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
title_sort |
enhanced catalytic activity and thermal stability of lipase bound to oxide nanosheets |
publisher |
Royal Society of Chemistry |
publishDate |
2018 |
url |
https://nagasaki-u.repo.nii.ac.jp/record/1129/files/RSCA8_20347.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
10.1039/C8RA03558J RSC Advances 36 8 20347 20352 20462069 https://nagasaki-u.repo.nii.ac.jp/record/1129/files/RSCA8_20347.pdf |
op_rights |
c 2018 The Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. |
_version_ |
1810290268804481024 |