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Molecules 2013, 18(1), 1138-1149; doi:10.3390/molecules18011138

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

1,2,†, 1,3,†, 1, 1 and 1,*
1
Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China
2
College of Life Sciences and Agriculture and Forestry, Qiqihar University, Qiqihar 161006, China
3
State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, College of Chemistry, Jilin University, Changchun 130012, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 3 December 2012 / Revised: 9 January 2013 / Accepted: 10 January 2013 / Published: 16 January 2013
(This article belongs to the Section Medicinal Chemistry)
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Abstract

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.
Keywords: SBA-15 mesoporous silica; trypsin; immobilization; specific activity; hydrolysis; BAPNA SBA-15 mesoporous silica; trypsin; immobilization; specific activity; hydrolysis; BAPNA
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Li, S.; Wu, Z.; Lu, M.; Wang, Z.; Li, Z. Improvement of the Enzyme Performance of Trypsin via Adsorption in Mesoporous Silica SBA-15: Hydrolysis of BAPNA. Molecules 2013, 18, 1138-1149.

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