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Purification and Characterization of Extracellular Isoamylase from Flavobacterium sp
Author(s) -
Sato Hélia Harumi,
Park Yong K.
Publication year - 1980
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.19800320410
Subject(s) - isoamylase , amylopectin , maltose , maltotriose , chemistry , chromatography , glycogen debranching enzyme , amylose , pullulan , biochemistry , hydrolysis , dextrin , sephadex , polyacrylamide gel electrophoresis , starch , polysaccharide , glycogen , enzyme , amylase , glycogen phosphorylase
An extracellular isoamylase from Flavobacterium sp. , was purified by fractionation with ammonium sulfate, DEAE‐cellulose, DEAE‐Sephadex A‐50, and CM‐cellulose column chromatography. Single band of the debranching activity of the purified enzyme was detected by polyacrylamide gel electrophoresis. The enzyme efficiently hydrolyzed α‐1,6‐glucosidic linkage of glycogen and amylopectin and formed amylose chains, but did not hydrolyze pullulan. The enzyme released maltotriose from ß‐limit dextrin of waxy maize amylopectin and glycogen, but no detectable maltose and glucose. Action of the isoamylase is similar to other microbial isoamylases but its physical properties are different.