Purificatioin, Crystallization, and Characterization of the Extracellular Invertase from Zymomonas mobilis

概要

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Zymomonas mobilis IFO 13756 (ATCC 29191) produces three kinds of sucrose-hydrolyzing eynzymes, E1,E2,and E3. Extracellular enzymes E2 and E3 bound to the cell surface were released from cells by suspension in 20 mM potassium phosphate buffer (pH 7.0) and incubation at 30℃ for 10 min with gentle shaking. After centrifugation of the cell suspension, E3 was isolated from the supernatant as crystals in a 52-fold purification. The enzyme consisted of a monomer subunit having a molecular mass of 58 kDa and its isoelectric point was pH 3.2. The N-terminal amino acid sequence was MFNFNASRWTRAQAMKVNKFDL. The enzyme catalyzed the hydrolysis of sucrose, and was identified as an invertase that had a substrate specificity for sucrose. The optimum pH and temperature were pH 5.5 and 50℃, respectively. Thiol reagents inhibited the enzyme activity markedly.
社団法人日本生物工学会の論文
1995-04-25