Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001

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Purification and characterization of a novel glucansucrase from Leuconostoc lactis EG001
Y M Kim; M J Yeon; Nack-Shick Choi; Young Hyo Chang; Min-Young Jung; Jae Jun SongJoong Su Kim
Bibliographic Citation
Microbiological Research, vol. 165, no. 5, pp. 384-391
Publication Year
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.
GlucansucraseGlycosylationL-ascorbic acidL-ascorbic acid 2-glucoside
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Ochang Branch Institute > Division of National Bio-Infrastructure > Bio-Infrastructure Policy Support Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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