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Title 

Novel α-glucosidase from extreme thermophile Thermus caldophilus GK24

Authors 

Oyekanmi NashiruSuk Hoon KohSe Yong LeeDae Sil Lee

Publisher 

Springer Verlag (Germany)

Issue Date 

2001

Citation 

Journal of Biochemistry and Molecular Biology, vol. 34, no. 4, pp. 347-354

Keywords 

α-GlucosidaseGene cloningThermostable enzymeThermus spTransglucosylation

Abstract 

α-Glucosidase of an extreme thermophile, Thermus caldophilus GK24 (TcaAG), was purified 80-fold from cells to a homogeneous state and characterized. The enzyme exhibited optimum activity at pH 6.5 and 90°C, and was stable from pH 6.0 to 8.5 and up to 90°C. The enzyme had a half-life of 85 minutes at 90°C. An analysis of the substrate specificity showed that the enzyme hydrolyzed the non-reducing terminal unit of α-1,6-glucosidic linkages of isomaltosaccharides and panose, α-1,3-glycosidic bond of nigerose and turanose, and α-1,2-glycosidic bond of sucrose. The gene encoding the TcaAG was cloned, sequenced, and expressed in E. coli. The nucleotide sequence of the gene encoded a 530 amino acid polypeptide and had a G+C content of 68.4% with a strong bias for G or C in the third position of the codons (93.6%). A sequence analysis revealed that TcaAG belonged to the α-amylase family. We suggest that this monomeric, thermostable, and broad-acting α-glucosidase is a departure from previously exhibited specificities. It is, therefore, a novel α-glucosidase.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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