Immobilization and Properties of β-Galactosidases from Macrophomina phaseoli and Sclerotium tuliparum

概要

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β-Galactosidases from Macrophomina phaseoli and Sclerotium tuliparum were immobilized on porous glass beads. The properties such as optimum temperature, pH-stability and behavior towards various metal ions and reagents except for N-bromosuccinimide of the immobilized enzymes were similar to those of the native enzymes, although Km values of the immobilized enzymes were 2-5 fold higher than those of the native enzymes. The substrate specificities of the immobilized enzymes were similar to those of the native enzymes, but the immobilized enzyme from M. phaseoli showed higher relative activity towards whey, lactose, and skim milk than the native enzyme did. Immobilized enzymes from M. phaseoli and S. tuliparum retained 100% and 78% of the original activities, respectively, after being kept for two months at pH 5.0 and 37℃, whereas the native enzymes from M. phaseoli and S. tuliparum showed 62% and 6% of the original activities, respectively. Both immobilized enzymes could be used repeatedly 10 times without any activity loss. These results suggest that the immobilized enzyme from M. phaseoli is suitable for hydrolytic cleavage of lactose in dairy products.
社団法人日本生物工学会の論文
1977-12-25