PURIFICATION AND PROPERTIES OF TREHALOSE-SYNTHESIZING ENZYME FROM PSEUDOMONAS SP. F1

Authors
OHGUCHI M KUBOTA N WADA T YOSHINAGA K URITANI M YAGISAWA M OHISHI K YAMAGISHI M OHTA T ISHIKAWA K
Citation
M. Ohguchi et al., PURIFICATION AND PROPERTIES OF TREHALOSE-SYNTHESIZING ENZYME FROM PSEUDOMONAS SP. F1, Journal of fermentation and bioengineering, 84(4), 1997, pp. 358-360
Citations number
17
Journal title
Journal of fermentation and bioengineering → ACNP
ISSN journal
0922338X
Volume
84
Issue
4
Year of publication
1997
Pages
358 - 360
Database
ISI
SICI code
0922-338X(1997)84:4<358:PAPOTE>2.0.ZU;2-T
Abstract
The trehalose-synthesizing enzyme, which catalyzes the conversion of m altose to trehalose by intramolecular transglucosylation, was purified from a bacterium, Pseudomonas sp. F1. Its molecular mass was estimate d to be 250 kDa by gel filtration and 67 kDa by SDS-polyacrylamide gel electrophoresis, and its pI was 5.8. The native enzyme may consist of 4 subunits. The enzyme was active on maltose and trehalose among sacc harides tested as substrates. The N-terminal amino acid of the enzyme was threonine.