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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:
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
Descripción
Sumario: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.