Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus.
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.
Rolfsmeier
M
M
School of Biological Sciences, University of Nebraska, Lincoln 68588-0188.
Blum
P
P
D000438:Alcohols; D010450:Endopeptidases; D004795:Enzyme Stability; D006358:Hot Temperature; D013379:Substrate Specificity; D016944:Sulfolobus / Q000201:enzymology*; D000520:alpha-Glucosidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D000438:Alcohols; D000520:alpha-Glucosidases; D010450:Endopeptidases