Isolation and purification of amyloglucosidase from Halobacterium sodomense

✍ Scribed by Grigoriy Chaga; Jerker Porath; Tibor Illéni

• Publisher: John Wiley and Sons
• Year: 1993
• Tongue: English
• Weight: 468 KB
• Volume: 7
• Category: Article
• ISSN: 0269-3879
• DOI: 10.1002/bmc.1130070504

✦ Synopsis

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, K,, and amino acid composition of the enzyme was determined.