J
Jong Suk Lee
Publications - 7
Citations - 181
Jong Suk Lee is an academic researcher. The author has contributed to research in topics: Xylanase & Xylan. The author has an hindex of 6, co-authored 7 publications receiving 157 citations.
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Journal ArticleDOI
Novel GH10 Xylanase, with a Fibronectin Type 3 Domain, from Cellulosimicrobium sp. Strain HY-13, a Bacterium in the Gut of Eisenia fetida
Do Young Kim,Mi Kyung Han,Doo Sang Park,Jong Suk Lee,Hyun Woo Oh,D H Shin,Tae-Sook Jeong,Sung Uk Kim,Kyung Sook Bae,Kwang Hee Son,Ho-Yong Park +10 more
TL;DR: The gene encoding a novel modular xylanase from Cellulosimicrobium sp.
Journal ArticleDOI
Isolation and characterization of a cellulase-free endo-β-1,4-xylanase produced by an invertebrate-symbiotic bacterium, Cellulosimicrobium sp. HY-13
Do Young Kim,Mi Kyoung Han,Jong Suk Lee,Hyun Woo Oh,Doo Sang Park,D H Shin,Kyung Sook Bae,Kwang Hee Son,Ho-Yong Park +8 more
TL;DR: The results of the present study suggest that the relatively highly active XylK lacking exo-xylanolytic activity is a promising candidate for the efficient production of non-digestible xylooligosaccharides that may have beneficial effects to gastrointestinal health via promotion of the growth of probiotics.
Journal ArticleDOI
Genetic and functional characterization of an extracellular modular GH6 endo-β-1,4-glucanase from an earthworm symbiont, Cellulosimicrobium funkei HY-13.
Do Young Kim,Min Ji Lee,Han-Young Cho,Jong Suk Lee,Mi-Hwa Lee,Chung Wook Chung,Dong-Ha Shin,Young Ha Rhee,Kwang-Hee Son,Ho-Yong Park +9 more
TL;DR: The gene (1608-bp) encoding a GH6 endo-β-1,4-glucanase (CelL) from the earthworm-symbiotic bacterium Cellulosimicrobium funkei HY-13 was cloned from its whole genome sequence, expressed recombinantly, and biochemically characterized.
Journal ArticleDOI
Biocatalytic Properties and Substrate-binding Ability of a Modular GH10 β-1,4-Xylanase from an Insect-symbiotic Bacterium, Streptomyces mexicanus HY-14
Do Young Kim,Dong-Ha Shin,Sora Jung,Jong Suk Lee,Han-Young Cho,Kyung Sook Bae,Chang-Keun Sung,Young Ha Rhee,Kwang-Hee Son,Ho-Yong Park +9 more
TL;DR: The results of enzymatic degradation of birchwood xylan and xylooligosaccharides revealed that rXylU preferentially hydrolyzed the substrates to xylobiose as the primary degradation product, indicating that r XylU was a peculiar GH10 β-1,4-xylanase with substrate specificity, which was different from its retaining homologs.
Journal ArticleDOI
Novel alkali-tolerant GH10 endo-β-1,4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis.
Do Young Kim,Dong Ha Shin,Sora Jung,Hyangmi Kim,Jong Suk Lee,Han Young Cho,Kyung Sook Bae,Chang Keun Sung,Young Ha Rhee,Kwang Hee Son,Ho-Yong Park +10 more
TL;DR: The rXylH gene was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis, and was an alkali-tolerant multifunctional enzyme possessing endo-β- 1,4-xylanase activity together with β-1,3/β-4- glucanase activity that exhibited its highest xylanolytic activity at pH 9.0.