Purification and characterization of an extracellular levansucrase from Zymomonas mobilis ZM1 = Zymomonas mobilis ZM1이 생산하는 균체외 Levansucrase의 정제 및 특성

Cited 0 time in scopus
Metadata Downloads
Title
Purification and characterization of an extracellular levansucrase from Zymomonas mobilis ZM1 = Zymomonas mobilis ZM1이 생산하는 균체외 Levansucrase의 정제 및 특성
Author(s)
Ki Bang Song; Jeong Woo Seo; Hyun Kyu Joo; Sang Ki Rhee
Bibliographic Citation
Korean Journal of (Applied) Microbiology & Biotechnology, vol. 26, no. 4, pp. 309-315
Publication Year
1998
Abstract
An extracellular levansucrase, which catalyzes the the formation of levan from sucrose, from the culture broth of Zymomonas mobilis ZM1 was purified by conventional column purification methods. The final purification yield was 18.3 fold of the crude enzyme from Z. mobilis, with 16.5 % of the enzyme recovered in the preparation step. The molecular weight of the enzyme was estimated to be 91,000 by Superose 12 gel filtration, and 45,000 by SDS- PAGE, indicating that levansucrase is a dimer. The optimum pH for the enzyme activity was around pH 4.0 for sucrose hydrolysis, and was around pH 5.0 for levan formation. The enzyme was inhibited by some metal ions, such as Hg2+ and Cu2+, and 50% of inhibition was observed with 5mM EDTA. The enzyme activity was enhanced by the presence of detergent Triton X-100, but inhibited by SDS completely. The enzyme catalyzes the liberation of reducing sugars, oligosacccharides and the formation of fructose polymer(levan). The enzyme also catalyzes the transfructosylation reaction of fructose moiety from sucrose to various sugar acceptor molecules, including sugar alcohols.
Keyword
Zymomonas mobilislevansucraselevan
ISSN
0257-2389
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.