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Preparation and properties of an immobilized Barley β‐amylase
Author(s) -
Vretblad Per,
Axen Rolf
Publication year - 1973
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.260150410
Subject(s) - chemistry , epichlorohydrin , amylase , immobilized enzyme , covalent bond , starch , chromatography , enzyme , biochemistry , organic chemistry
Barely β‐amylase (α‐1,4‐glucan maltohydrolase, EC 3.2.1.2) has been immobilized by covalent fixation to amino derivatives of epichlorohydrin crosslinked Sepharose mediated by cyclohexyl isocyanide and acetaldehyde. The enzyme conjugates contain up to 35% of the total activity of the β‐amylase added to the coupling mixture. The profiles of activity versus pH and ionic strength are essentially the same for free and immobilized β‐amylase, whereas the resistance to inactivation during storage and use is considerably enhanced by immobilization. Columns with immobilized β‐amylase have been used for continuous degradation of starch. At 45°C, half of the initial activity remains after seven weeks, and the corresponding figure at 23°C is 85 percent.