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Title 

Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001

Authors 

Y M KimM J YeonNack-Shick ChoiYoung Hyo ChangMin-Young JungJae Jun SongJoong Su Kim

Publisher 

Elsevier

Issue Date 

2010

Citation 

Microbiological Research, vol. 165, no. 5, pp. 384-391

Keywords 

GlucansucraseGlycosylationL-ascorbic acidL-ascorbic acid 2-glucoside

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°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.

ISSN 

0944-5013

Link 

http://dx.doi.org/10.1016/j.micres.2009.08.005

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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