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Preparation and properties of immobilized amyloglucosidase
Author(s) -
Nithianandam V. S.,
Srinivasan K. S. V.,
Joseph K. Thomas,
Santappa M.
Publication year - 1981
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.260231010
Subject(s) - amylase , immobilized enzyme , chemistry , thermal stability , copolymer , chromatography , enzyme , organic chemistry , polymer
Amyloglucosidase was immobilized on a copolymer of methyl methacrylate and 2‐dimethylaminoethyl methacrylate. The resulting immobilized amyloglucosidase has 19% of the soluble enzyme specific activity. The pH optimum of immobilized amyloglucosidase is shifted towards acidity by 1.9 units. The temperature optimum of immobilized enzyme is shifted upward by 5°C. The immobilized amyloglucosidase has the maximum stability at pH 4.6, whereas the soluble enzyme has maximum stability at pH 5.5. While soluble amyloglucosidase has a maximum thermal stability at 50°C, the stability of the immobilized amyloglucosidase steadily decreases with the increase in temperature.

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