Isolation and purification of amyloglucosidase from Halobacterium sodomense
- 1 September 1993
- journal article
- review article
- Published by Wiley in Biomedical Chromatography
- Vol. 7 (5) , 256-261
- https://doi.org/10.1002/bmc.1130070504
Abstract
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.Keywords
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