Immobilization-Stabilization of Kerase, a Serine Protease from Streptomyces fradiae, by Covalent Attachment to Porous Glass

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Kerase, a serine protease from Streptomyces fradiae, was immobilized on porous glass by covalent attachment of the enzyme through its amino groups. Chemical modification studies have shown that the amino groups can be used to establish covalent attachment of this protease to porous glass, modification of four lysine residues (44.4% of the accessible amino groups) resulting in a 6.5% loss of enzymatic activity. After immobilization, the optimal reaction pH range changed from 7.5-8.5 to 9-10, the protease being stable over a broad pH range of 6-12, while the soluble protease was irreversibly denatured in the alkaline pH range (pH > 8). Moreover, the optimal reaction temperature was changed from 55 to 65℃, showing higher thermal stability. Kerase immobilized onto porous glass was stable for at least 28 days when working in a repeated-batch process of three cycles per day, with an activity loss of 22.1±3.1%.
社団法人日本農芸化学会の論文
1995-05-23