U
Uyangaa Temuujin
Researcher at Myongji University
Publications - 7
Citations - 195
Uyangaa Temuujin is an academic researcher from Myongji University. The author has contributed to research in topics: Streptomyces coelicolor & Agarase. The author has an hindex of 4, co-authored 7 publications receiving 180 citations.
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Journal ArticleDOI
Overexpression and biochemical characterization of DagA from Streptomyces coelicolor A3(2): an endo-type β-agarase producing neoagarotetraose and neoagarohexaose
TL;DR: Thin layer chromatography analysis, matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry, and Fourier transform nuclear magnetic resonance (FT-NMR) spectrometer of the hydrolyzed products of agarose by DagA revealed that DagA is an endo-type β-agarase that degrades agarOSE into neoagarotetraose and neoagarohexaose.
Journal ArticleDOI
Identification and Biochemical Characterization of Sco3487 from Streptomyces coelicolor A3(2), an Exo- and Endo-Type β-Agarase-Producing Neoagarobiose
TL;DR: Thin-layer chromatography analysis, matrix-assisted laser desorption ionization-time of flight mass spectrometry, and Fourier transform-nuclear magnetic resonance spectrometer of the Sco3487 hydrolysis products revealed that Sco34 87 is both an exo- and endo-type β-agarase that degrades agarose, neoagarotetraose, and neoagarohexaose into neoagarobiose.
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Identification and Characterization of a Xyloglucan-Specific Family 74 Glycosyl Hydrolase from Streptomyces coelicolor A3(2)
Bolormaa Enkhbaatar,Uyangaa Temuujin,Ju-Hyeon Lim,Won-Jae Chi,Yong Keun Chang,Soon-Kwang Hong +5 more
TL;DR: It is demonstrated that the sco6545 gene of Streptomyces coelicolor A3(2) is not a cellulase but a xyloglucan-specific glycosyl hydrolase which cleaves xylglucan at unbranched glucose residues.
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Identification and characterization of a novel β-galactosidase from Victivallis vadensis ATCC BAA-548, an anaerobic fecal bacterium.
TL;DR: It is clearly demonstrated that VadG925 is a novel β-galactosidase that can hydrolyze lactose, which is unusual because of its low homology to validated β- Galactopyranoside.
Journal ArticleDOI
Molecular Characterization of the α-Galactosidase SCO0284 from Streptomyces coelicolor A3(2), a Family 27 Glycosyl Hydrolase.
TL;DR: The SCO0284 gene of Streptomyces coelicolor A3(2) is predicted to encode an α-galactosidase (680 amino acids) belonging to glycoside hydrolase family 27, indicating that it specifically cleaves the α-1,6-glycosidic bond of the substrate, releasing the terminal D- Galactose.