PURIFICATION, CRYSTALLIZATION, AND CHARACTERIZATION OF THE EXTRACELLULAR INVERTASE FROM ZYMOMONAS-MOBILIS

Citation
H. Yanase et al., PURIFICATION, CRYSTALLIZATION, AND CHARACTERIZATION OF THE EXTRACELLULAR INVERTASE FROM ZYMOMONAS-MOBILIS, Journal of fermentation and bioengineering, 79(4), 1995, pp. 367-369
Citations number
17
Categorie Soggetti
Food Science & Tenology","Biothechnology & Applied Migrobiology
ISSN journal
0922338X
Volume
79
Issue
4
Year of publication
1995
Pages
367 - 369
Database
ISI
SICI code
0922-338X(1995)79:4<367:PCACOT>2.0.ZU;2-#
Abstract
Zymomonas mobilis IFO 13756 (ATCC 29191) produces three kinds of sucro se-hydrolyzing enzymes, E1, E2, and E3. Extracellular enzymes E2 and E 3 bound to the cell surface were released from cells by suspension in 20 mM potassium phosphate buffer (pH 7.0) and incubation at 30 degrees C for 10 min with gentle shaking. After centrifugation of the cell su spension, E3 was isolated from the supernatant as crystals in a 52-fol d purification. The enzyme consisted of a monomer subunit having a mol ecular mass of 58 kDa and its isoelectric point was pH 3.2. The N-term inal amino acid sequence was MFNFNASRWTRAQAMKVNKFDL. The enzyme cataly zed the hydrolysis of sucrose, and was identified as an invertase that had a strict substrate specificity for sucrose. The optimum pH and te mperature were pH 5.5 and 50 degrees C, respectively. Thiol reagents i nhibited the enzyme activity markedly.