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- 저자 : Nashiru, (검색결과 2 건)
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Novel $\alpha$-Glucosidase from Extreme Thermophile Thermus caldophilus GK24
Nashiru, Oyekanmi,Koh, Suk-Hoon,Lee, Se-Yong,Lee, Dae-Sil Korean Society for Biochemistry and Molecular Biol 2001 Journal of biochemistry and molecular biology Vol.34 No.4
$\alpha$-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 $90^{\circ}C$, and was stable from pH 6.0 to 85 and up to $90^{\circ}C$. The enzyme had a half-life of 85 minutes at $90^{\circ}C$. An analysis of the substrate specificity showed that the enzyme hydrolyzed the non-reducing terminal unit of $\alpha$-1,6-glucosidic linkages of isomaltosaccharides and panose, $\alpha$-1,3-glycosidic bond of nigerose and turanose, and $\alpha$-1,2-glycosidic bond of sucrose. The gene encoding the TcaAG was cloned, sequenced, and sequenced 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 $\alpha$-amylase family. We suggest that this monomeric, thermostable, and broad-acting $\alpha$-glucosidase is a departure from previously exhibited specificities. It is, therefore, a novel $\alpha$-glucosidase.
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Novel α - Glucosidase from Extreme Thermophile Thermus caldophilus GK24
Lee, Se Yong,Lee, Dae Sil,Koh, Suk Hoon,Nashiru, Oyekanmi 생화학분자생물학회 1976 BMB Reports Vol.34 No.4
α-Glucosidase of an extreme thermophile, Thernius 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℃, and was stable from pH 6.0 to 85 and up to 90℃. The enzyme had a half-life of 85 minutes at 90℃. 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 enpressed 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 aamylase family. We suggest that this monomeric, thermostable, and broad-acting α-glucosidase is a departure from previously exhibited specificities. It is, therefore, a novelα-glucosidase.
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