Novel glycoside hydrolases identified by screening a Chinese Holstein dairy cow rumen-derived metagenome library.
One clone encoding glycoside hydrolases was identified through functional screening of a rumen bacterial artificial chromosome (BAC) library. Of the 68 open reading frames (ORFs) predicted, one ORF encodes a novel endo-β-1,4-xylanase with two catalytic domains of family GH43 and two cellulose-binding modules (CBMs) of family IV. Partial characterization showed that this endo-xylanase has a greater specific activity than a number of other xylanases over a wide temperature range at neutral pH and could be useful in some industrial applications.
Zhao
Shengguo
S
State Key Laboratory of Animal Nutrition, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China.
Wang
Jiaqi
J
Bu
Dengpan
D
Liu
Kailang
K
Zhu
Yaxin
Y
Dong
Zhiyang
Z
Yu
Zhongtang
Z
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle / Q000382:microbiology*; D002681:China; D022202:Chromosomes, Artificial, Bacterial; D003001:Cloning, Molecular / Q000379:methods; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D054892:Metagenome; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D017434:Protein Structure, Tertiary; D012417:Rumen / Q000382:microbiology*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity; D013696:Temperature
D043364:Endo-1,4-beta Xylanases