scispace - formally typeset
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.

Papers
More filters
Journal ArticleDOI

Isolation and characterization of a cellulase-free endo-β-1,4-xylanase produced by an invertebrate-symbiotic bacterium, Cellulosimicrobium sp. HY-13

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.

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

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.

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.