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Preparation and properties of an immobilized Barley β-amylase

✍ Scribed by Per Vretblad; Rolf Axen

Publisher
John Wiley and Sons
Year
1973
Tongue
English
Weight
529 KB
Volume
15
Category
Article
ISSN
0006-3592

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✦ Synopsis

Abstract

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.

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