Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus
M Rolfsmeier, P Blum - Journal of bacteriology, 1995 - Am Soc Microbiol
M Rolfsmeier, P Blum
Journal of bacteriology, 1995•Am Soc MicrobiolA 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.
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.
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.
American Society for Microbiology以上显示的是最相近的搜索结果。 查看全部搜索结果