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• W2018092800 abstract "The zymogen alpha-chymotrypsinogen A is bound to mesoporous silica MCM-41 with a protein loading of 170 mg/g solid (MCM-Z) by a simple stirring in aqueous tris-HCl buffer (pH 7.2). The bound zymogen is then activated with trypsin to obtain alpha-chymotrypsin immobilized on MCM-41 (MCM-E.I) that displays an effective enzyme activity corresponding to 65 mg protein/g of solid support (3250 BTEE units/g). A direct immobilization of commercially available alpha-chymotrypsin (MCM-E.II) gives lower loading (1250 BTEE units/g). Protein content of the solid support after immobilization is confirmed by thermogravimetric analysis (TGA). The enzyme is tightly bound to the support and can be used over 100 recycles over 1 week in aqueous as well as reverse micellar media. The immobilized enzyme (MCM-E.I) has been used for resolution of N-acetyl-dl-amino acid esters and racemic trans-4-methoxy-3-phenylglycidic acid (PGA) methyl ester." @default.
• W2018092800 created "2016-06-24" @default.
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• W2018092800 date "2003-01-01" @default.
• W2018092800 modified "2023-10-15" @default.
• W2018092800 title "Highly Efficient Tight Fit Immobilization of α-Chymotrypsin in Mesoporous MCM-41: A Novel Approach Using Precursor Immobilization and Activation" @default.
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• W2018092800 doi "https://doi.org/10.1021/bp025678s" @default.
• W2018092800 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12675570" @default.
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