Isolation and purification of amyloglucosidase from Halobacterium sodomense.
Amyloglucosidase from Halobacterium sodomense was purified by a combination of hydrophobic interaction chromatography and immobilized metal ion affinity chromatography at analytical and preparative scale with 75% recovery. The enzyme was found to be a dimer of two different subunits with molecular weights of 72,000 and 82,000 D, respectively, combining in a 175,000 D native protein. The specific activity, KM, and amino acid composition of the enzyme was determined.
Chaga
G
G
Biochemical Separation Centre, Uppsala University, Sweden.
Porath
J
J
Illéni
T
T
D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification* / Q000378:metabolism; D006217:Halobacterium / Q000201:enzymology*; D008670:Metals; D008970:Molecular Weight
D008670:Metals; D005087:Glucan 1,4-alpha-Glucosidase