文化大學機構典藏 CCUR:Item 987654321/24303
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    Please use this identifier to cite or link to this item: https://irlib.pccu.edu.tw/handle/987654321/24303


    Title: THE CONSTRUCTION OF BIFUNCTIONAL FUSION XYLANOLYTIC ENZYMES AND THE PREDICTION OF OPTIMUM REACTION CONDITIONS FOR THE ENZYME ACTIVITY
    Authors: Pai, CK (Pai, Cheng-Kang)
    Wang, HT (Wang, Han-Tsung)
    Guo, RT (Guo, Rey-Ting)
    Liu, JR (Liu, Je-Ruei)
    Contributors: Dept Anim Sci
    Keywords: Chimeric enzyme
    Neocallimastix patriciarum
    Xylanase
    Acetylxylan esterase
    Date: 2012
    Issue Date: 2013-02-25 14:23:01 (UTC+8)
    Abstract: Four chimeric xylanolytic enzymes were formed by fusion of a thermally stable xylanase XynCDBFV either to the N-terminus or C-terminus of a thermally stable acetylxylan esterase AxeS20E, with or without a Gly-rich flexible linker (S2). The three-dimensional (3D) structures of the chimeric enzymes were predicted using the I-TASSER server, and the results indicated that the structures of Axe-S2-Xyn and Xyn-S2-Axe were more similar to the native structures than were those of Axe-Xyn and Xyn-Axe. Axe-S2-Xyn and Xyn-S2-Axe were expressed in Escherichia coli and purified by means of affinity chromatography. Response surface modeling (RSM), combined with central composite design (CCD) and regression analysis, was then employed to optimize the xylanase activities of the chimeric enzymes. Under the optimal conditions, Xyn-S2Axe had greater hydrolytic activities on natural xylans and rice straw than did the parental enzymes. These results suggested that the chimeric enzyme Xyn-S2-Axe could be effective at hydrolyzing xylan in biomass and that it has potential to be used in a range of biotechnological applications.
    Relation: BIORESOURCES 卷: 7 期: 4 頁數: 5647-5665
    Appears in Collections:[Department of Animal Science] journal articles

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