PMID: 8145Sep 14, 1976

Purification and properties of extracellular alpha-glucosidase of a thermophile, Bacillus thermoglucosidus KP 1006

Biochimica Et Biophysica Acta
Y SuzukiS Abe


An extracecular alpha-glucosidase (alpha-D-glucoside glycohydrolase, EC of a thermophile, Bacillus thermoglucosidius KP 1006, was purified about 350-fold. The purified enzyme had a specific activity of 164 mumol of p-nitrophenyl-alpha-D-glucopyranoside hydrolyzed per min at 60 degrees C and pH 6.8 per mg of protein. The molecular weight was estimated at 55 000. The pH and temperature optima for activity were 5.0--6.0 and 75 degrees C, respectively. Below 40 degrees C, the activity was less than 4.5% of the optimym. The enzyme showed a high specificity for alpha-D-glucopyranoside. The maximal hydrolyzing velocity per substrate diminished in the order: phenyl-alpha-D-glucopyranoside, p-nitrophenyl-alpha-D-glucopyranoside, isomaltose, methyl-alpha-glycopyranoside. The respective Km values were 3.0, 0.23, 3.2 and 27 mM. The activity was trace for turanose, and not detectable for sucrose, trehalose, raffinose, melezitose, maltose, maltotriose, phenyl-alpha-D-maltoside, dextran, dextrin and starch. Tris, p-nitrophenyl-alpha-D-xylopyranoside, glucose and glucono-delta-lactone blocked competitively the enzyme with respect to p-nitrophenyl-alpha-D-glucopyranoside. The Ki values were 0.12, 0.14, 2.2 and 2.4 mM, respectively. Th...Continue Reading


Jul 1, 1986·European Journal of Biochemistry·Y Suzuki, Y Tomura
Jul 15, 1989·European Journal of Biochemistry·A GuagliardiS Bartolucci
Oct 26, 2001·Bioscience, Biotechnology, and Biochemistry·K WatanabeY Suzuki
May 4, 2016·Cellular and Molecular Life Sciences : CMLS·Masayuki OkuyamaAtsuo Kimura
Jan 17, 1997·The Journal of Biological Chemistry·M Inohara-OchiaiY Shibano
Jan 1, 1989·Critical Reviews in Biochemistry and Molecular Biology·M Vihinen, P Mäntsälä

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