Properties of β-Glucosidase Immobilized in Serichin Membrane

概要

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A sericin membrane was used to support immobilized β-glucosidase. The immobilized enzyme was prepared by drying sericin-enzyme solution on a plate, followed by treatment with glutaraldehyde. The properties of the immobilized β-glucosidase were compared with those of the native enzyme. The activity yield of the immobilized enzyme was 46% of that of the native enzyme, and the activity was considerably stable on re-use and storage and retained over 86% after 30 days. Many differences were not found in pH and temperature dependencies between the two enzymes. Stabilities against heating and electrodialysis were fairly enhanced by the immobilization. The immobilized enzyme activity was little affected by treatment with trypsin, a-chymotrypsin or papain, but was reduced to 68% with pronase E. The apparent Michaelis constant of the immobilized enzyme was 3.5 mM (thickness : 85μm, enzyme conten : 5.4%) and the Michaelis constant of the native enzyme was 2.3 mM, at pH 5.7.
公益社団法人日本生物工学会の論文
1978-08-25