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Title 

Biocatalytic properties and substrate-binding ability of a modular GH10 beta-1,4-xylanase from an insect-symbiotic bacterium, Streptomyces mexicanus HY-14

 

곤충 공생세균 Streptomyces mexicanus HY-14가 생산하는 GH10 Xylanase의 생촉매적 특성과 기질 결합능

Authors 

Do Young KimD H ShinS JungJ S LeeHan-Young ChoKyung Sook BaeC K SungY H RheeKwang- Hee SonHo Yong Park

Publisher 

Microbiological Society of Korea

Issue Date 

2014

Citation 

Journal of Microbiology, vol. 52, no. 10, pp. 863-870

Keywords 

Binding abilityGH family 10Modular enzymeStreptomyces mexicanus HY-14β-1,4-xylanase

Abstract 

The gene (1350-bp) encoding a modular β-1,4-xylanase (XylU), which consists of an N-terminal catalytic GH10 domain and a C-terminal carbohydrate-binding module 2 (CBM 2), from Streptomyces mexicanus HY-14 was cloned and functionally characterized. The purified His-tagged recombinant enzyme (rXylU, 44.0 kDa) was capable of efficiently hydrolyze diverse xylosidic compounds, p-nitrophenyl-cellobioside, and p-nitrophenyl-xylopyranoside when incubated at pH 5.5 and 65°C. Especially, the specific activities (649.8 U/mg and 587.0 U/mg, respectively) of rXylU toward oat spelts xylan and beechwood xylan were relatively higher than those (<500.0 U/mg) of many other GH10 homologs toward the same substrates. The results of enzymatic degradation of birchwood xylan and xylooligosaccharides (xylotriose to xylohexaose) revealed that rXylU preferentially hydrolyzed the substrates to xylobiose (>75%) as the primary degradation product. Moreover, a small amount (4%<) of xylose was detected as the degradation product of the evaluated xylosidic substrates, indicating that rXylU was a peculiar GH10 β-1,4-xylanase with substrate specificity, which was different from its retaining homologs. A significant reduction of the binding ability of rXylU caused by deletion of the C-terminal CBM 2 to various insoluble substrates strongly suggested that the additional domain might considerably contribute to the enzyme-substrate interaction.

ISSN 

1225-8873

Link 

http://dx.doi.org/10.1007/s12275-014-4390-8

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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