Preparation and Properties of Naringinase Immobilized by Ionic Binding to DEAE-Sephadex

概要

論文の詳細を見る
Naringinase from Aspergillus niger was immobilized with a 50-80% yield by ionic binding of the enzyme to DEAE-Sephadex A-25. Some enzymatic properties of the immobilized naringinase were investigated and compared with those of the native enzyme. The optimal pH of the immobilized enzyme was 0.5 pH units to the acid side of that of the native enzyme. The optimal temperature had moved from 50℃ to 60℃. The heat stability of the immobilized enzyme was better than that of the native naringinase. No significant difference in the Michaelis constant was detected.When the substrate solution of 0.05% naringin was passed through the immobilized column packed with a mixture of 1 part of immobilized naringinase and 49 parts of Sephadex G-25 below a space velocity of 4.6 hr^<-1> at 37℃, complete hydrolysis of naringin was observed. The enzyme activity of the immobilized enzyme column was stable, and its half-life was 60.0 days at 25℃ and 43.8 days at 37℃. However, when Natsudaidai juice was passed through the immobilized naringinase column, the activity of the column rapidly decreased.
社団法人日本生物工学会の論文
1977-10-25