Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA

The enzymatic performance of trypsin in hydrolysis of N-α-benzoyl-DL-arginine-4-nitroanilide (BAPNA) was improved by adsorption on Santa Barbara Amorphous (SBA)-15 mesoporous silica. The optimal immobilization conditions were screened and the properties of immobilized enzyme have also been studied....

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Detalles Bibliográficos
Autores principales: Li, Shanshan, Wu, Zhuofu, Lu, Ming, Wang, Zhi, Li, Zhengqiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270008/
https://www.ncbi.nlm.nih.gov/pubmed/23325102
http://dx.doi.org/10.3390/molecules18011138
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author Li, Shanshan
Wu, Zhuofu
Lu, Ming
Wang, Zhi
Li, Zhengqiang
author_facet Li, Shanshan
Wu, Zhuofu
Lu, Ming
Wang, Zhi
Li, Zhengqiang
author_sort Li, Shanshan
collection PubMed
description The enzymatic performance of trypsin in hydrolysis of N-α-benzoyl-DL-arginine-4-nitroanilide (BAPNA) was improved by adsorption on Santa Barbara Amorphous (SBA)-15 mesoporous silica. The optimal immobilization conditions were screened and the properties of immobilized enzyme have also been studied. Under the optimal conditions, the immobilized trypsin displays maximum specific activity (49.8 μmol/min/g). The results also indicate that the immobilized trypsin exhibits better storage stability.
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spelling pubmed-62700082018-12-14 Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA Li, Shanshan Wu, Zhuofu Lu, Ming Wang, Zhi Li, Zhengqiang Molecules Article The enzymatic performance of trypsin in hydrolysis of N-α-benzoyl-DL-arginine-4-nitroanilide (BAPNA) was improved by adsorption on Santa Barbara Amorphous (SBA)-15 mesoporous silica. The optimal immobilization conditions were screened and the properties of immobilized enzyme have also been studied. Under the optimal conditions, the immobilized trypsin displays maximum specific activity (49.8 μmol/min/g). The results also indicate that the immobilized trypsin exhibits better storage stability. MDPI 2013-01-16 /pmc/articles/PMC6270008/ /pubmed/23325102 http://dx.doi.org/10.3390/molecules18011138 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Li, Shanshan
Wu, Zhuofu
Lu, Ming
Wang, Zhi
Li, Zhengqiang
Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title_full Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title_fullStr Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title_full_unstemmed Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title_short Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA
title_sort improvement of the enzyme performance of trypsin via adsorption in mesoporous silica sba-15: hydrolysis of bapna
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270008/
https://www.ncbi.nlm.nih.gov/pubmed/23325102
http://dx.doi.org/10.3390/molecules18011138
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AT wangzhi improvementoftheenzymeperformanceoftrypsinviaadsorptioninmesoporoussilicasba15hydrolysisofbapna
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