Title: Properties of native and immobilised preparations of β-D-glucosidase from Aspergillus niger
Abstract: Abstract The enzyme β‐D‐glucosidase from Aspergillus niger has been immobilised through its carbohydrate moiety on concanavalin A‐Sepharose and on cyanogen bromide‐activated Sepharose after aminoalkylation of the carbohydrate side chains of the enzyme. For comparison, the enzyme was also immobilised on microcrystalline cellulose through its protein moiety. High retention of activity and a decrease in K m and V max. were observed when β‐D‐glucosidase was immobilised by these methods. An increase in the thermal stability of the immobilised β‐D‐glucosidase preparations over the soluble enzyme was achieved if it was treated with glutaraldehyde before its adsorption on concanavalin A‐Sepharose or if the enzyme immobilised on cyanogen bromide‐activated Sepharose was subsequently treated with glutaraldehyde. Treatment of β‐D‐glucosidase immobilised on microcrystalline cellulose with glutaraldehyde hardly increased its thermal stability over the soluble enzyme.
Publication Year: 1982
Publication Date: 1982-01-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 18
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