Preparation of an immobilized two-enzyme system, β-amylase-pullulanase, to an acrylic copolymer for the conversion of starch to maltose. I. Preparation and stability of immobilized β-amylase

✍ Scribed by Kaj Mårtensson

• Publisher: John Wiley and Sons
• Year: 1974
• Tongue: English
• Weight: 520 KB
• Volume: 16
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260160502

✦ Synopsis

Abstract

β‐Amylase (EC 3.2.1.2), obtained from barley, was chemically attached to a crosslinked copolymer of acrylamide‐acrylic acid using a water‐soluble carbodiimide. The derivative showed 23% β‐amylase activity in relation to that of free enzyme with a coupling yield of 40% based on the amount of added β‐amylase. In order to find optimal coupling conditions, the effect of pH and different carbodiimide concentrations was investigated. The enzymic activity associated with different β‐amylase concentrations was further outlined. A slightly increased operational stability for the enzyme upon immobilization was observed. Markedly improved operational stability has been obtained by coupling in the presence of reduced glutathione of bovine serum albumin.