Premium
Kinetic Properties of the Rhizopus Glucoamylase and Bacillus α‐Amylase, which are Immobilized on Cellulofine
Author(s) -
Ohnishi Masatake,
Iwata Ken,
Tomita Takayo,
Nishikawa Ukiko,
Hiromi Keitaro
Publication year - 1990
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19900421209
Subject(s) - maltose , amylase , chemistry , starch , degree of polymerization , substrate (aquarium) , amylose , maltotriose , hydrolysis , enzyme , polymerization , pullulan , oligomer , molar mass , polymer chemistry , polymer , chromatography , polysaccharide , organic chemistry , biology , ecology
Glucoamylase from Rhizopus niveus was immobilized on Cellulofine, a kind of cellulose gel, to construct an enzyme‐Cellulofine structure, of which the molar activities k 0 for maltose and for soluble starch were found almost equal to 4 and 1/9 times, respectively, of those found with the intact enzyme. Liquefying Bacillus α‐amylase was fixed to make another enzyme‐Cellulofine structure, of which ratio of the molar activities, k 0 (modified)/k 0 (intact) for an oligomer substrate maltohexaose is much larger than those for high‐polymer substrates, amylose and soluble starch. These findings suggest that the substrate specificity of the amylase‐Cellulofine structure is improved to be useful for the enzyme‐catalyzed hydrolysis of saccharides having small degree of polymerization.