PURIFICATION AND CHARACTERIZATION OF INVERTASE FROM TORULASPORA-PRETORIENSIS-YK-1

Authors
Citation
Y. Oda et K. Tonomura, PURIFICATION AND CHARACTERIZATION OF INVERTASE FROM TORULASPORA-PRETORIENSIS-YK-1, Bioscience, biotechnology, and biochemistry, 58(6), 1994, pp. 1155-1157
Citations number
5
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
58
Issue
6
Year of publication
1994
Pages
1155 - 1157
Database
ISI
SICI code
0916-8451(1994)58:6<1155:PACOIF>2.0.ZU;2-Y
Abstract
Invertase was purified from Torulaspora pretoriensis YK-1 by acid trea tment and column chromatography on DEAE-Togopearl 650M and phenyl-Toyo pearl 650M to homogeneity. The molecular weight of the purified enzyme was estimated to be 130,000 by SDS-polyacrylamide gel electrophoresis and 530,000 by gel filtration. The enzyme contained 50% molecular wei ght as carbohydrate. Properties of the invertase from T. pretoriensis was similar to external invertase from Saccharomyces cerevisiae.