NOTES Characterization of a Neocallimastix patriciarum xylanase gene and its product1
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چکیده
A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for
منابع مشابه
Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses
BACKGROUND Neocallimastix patriciarum is one of the common anaerobic fungi in the digestive tracts of ruminants that can actively digest cellulosic materials, and its cellulases have great potential for hydrolyzing cellulosic feedstocks. Due to the difficulty in culture and lack of a genome database, it is not easy to gain a global understanding of the glycosyl hydrolases (GHs) produced by this...
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A thermally stable and alkalophilic xylanase, XynCDBFV, from Neocallimastix patriciarum was overexpressed in Escherichia coli as a recombinant protein fused to the N-terminus of oleosin, a unique structural protein of seed oil bodies. As a result of the reconstitution of the artificial oil bodies (AOBs), the immobilization of active xylanase was accomplished. Response surface methodology (RSM) ...
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1 Commonwealth Scientific and Industrial Research Organisation, Division of Tropical Animal Production, Private Bag No. 3, PO Indooroopilly, QLD 4068, Australia * Commonwealth Scientific and Industrial Research Organisation, Division of Tropical Crops and Pastures, 306 Ca rmody Road, S t Lucia, QLD 4067, Australia Acetylesterase and cinnamoyl ester hydrolase activities were demonstrated in cult...
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