Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001.

Abstract

A gene encoding glucansucrase was identified in Leuconostoc lactis EG001 isolated from lactic acid bacteria (LAB) in Kimchi, a traditional Korean fermented food. The L. lactis EG001 glucansucrase gene consists of 4503 bp open reading frame (ORF) and encodes an enzyme of 1500 amino acids with an apparent molecular mass of 165 kDa. The deduced amino-acid sequence showed the highest amino-acid sequence identity (75%) to that of dextransucrase of L. mesenteroides. The gene was cloned and over-expressed in Escherichia coli strain. The recombinant enzyme was purified via Ni-NTA affinity chromatography and its enzymatic properties were characterized. The enzyme exhibited optimum activity at 30 degrees C and pH 5.0. In addition, the enzyme was able to catalyze the glycosylation of l-ascorbic acid to l-ascorbic acid 2-glucoside. The glycosylated product via EG001 glucansucrase has the potential as an antioxidant in industrial applications.

• Authors: Yong-Mo Kim, Min Ji Yeon, Nack-Shick Choi, Young-Hyo Chang, Min Young Jung, Jae Jun Song, Joong Su Kim
• Journal: Microbiological research (Microbiol Res) Vol. 165 Issue 5 Pg. 384-91 (Jul 20 2010) ISSN: 1618-0623 [Electronic] Germany
• PMID: 19853426 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright 2009 Elsevier GmbH. All rights reserved.

Chemical References

• Glycosyltransferases
• alternansucrase

Topics

• Amino Acid Sequence
• Base Sequence
• Glycosyltransferases (genetics, isolation & purification, metabolism)
• Leuconostoc (classification, enzymology, genetics)
• Molecular Sequence Data
• Phylogeny