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J. Bacteriol., Jan 1995, 482-485, Vol 177, No. 2
Copyright © 1995, American Society for Microbiology

Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus

M Rolfsmeier and P Blum
School of Biological Sciences, University of Nebraska, Lincoln 68588- 0188.

A soluble maltase (alpha-glucosidase) with an apparent subunit mass of 80 kDa was purified to homogeneity from Sulfolobus solfataricus. The enzyme liberates glucose from maltose and malto-oligomers. Maximal activity was observed at 105 degrees C, with half-lives of 11 h (85 degrees C), 3.0 h (95 degrees C), and 2.75 h (100 degrees C). The enzyme was generally resistant to proteolysis and denaturants including aliphatic alcohols. n-Propanol treatment at 85 degrees C increased both Km and Vmax for maltose hydrolysis.


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