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Invertase covalently coupled to porous glass: Preparation and characterization
Author(s) -
Mason R. D.,
Weetall H. H.
Publication year - 1972
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260140409
Subject(s) - invertase , porous glass , covalent bond , immobilized enzyme , enzyme , chemistry , chromatography , porosity , enzyme assay , hydrolysis , biochemistry , organic chemistry
The enzyme invertase has been covalently coupled to porous glass particles. The product is extremely stable over a long period of time. Kinetic values for the immobilized enzyme are similar to the native enzyme. Excellent enzymatic activity for the immobilized enzyme was exhibited over a broad pH range. The immobilized enzyme when continuously operated for one month was found to have an operational half‐life of over 40 days.