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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/32786

Title: Effect of C-terminal truncation on enzyme properties of recombinant amylopullulanase from Thermoanaerobacter pseudoethanolicus
Authors: Fu-Pang Lin;Yi-Hsuan Ho;Hsu-Yang Lin;Hui-Ju Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Thermoanaerobacter pseudoethanolicus;Amylopullulanase;C-terminal truncation mutagenesis;Circular dichroism
Date: 2012-05-01
Issue Date: 2012-06-18T06:41:35Z
Publisher: Extremophiles
Abstract: Abstract:The smallest and enzymatically active molecule, TetApuQ818, was localized within the C-terminal Q818 amino acid residue after serial C-terminal truncation analysis of the recombinant amylopullulanase molecule (TetApuM955) from Thermoanaerobacter pseudoethanolicus. Kinetic analyses indicated that the overall catalytic efficiency, k cat/K m, of TetApuQ818 was 8–32% decreased for the pullulan and the soluble starch substrate, respectively. Changes to the substrate affinity, K m, and the turnover rate, k cat, were decreased significantly in both enzymatic activities of TetApuQ818. TetApuQ818 exhibited less thermostability than TetApuM955 when the temperature was raised above 85°C, but it had similar substrate-binding ability and hydrolysis products toward various substrates as TetApuM955 did. Both enzymes showed similar spectroscopies of fluorescence and circular dichroism, suggesting the active folding conformation was maintained after this C-terminal Q818 deletion. This study suggested that the binding ability of insoluble starch by TetApuM955 did not rely on the putative C-terminal carbohydrate binding module family 20 (CBM20) and two FnIII regions of TetApu, though the integrity of the AamyC module of TetApuQ818 was required for the enzyme activity.
Relation: 16(3), pp.395-403
URI: http://ntour.ntou.edu.tw/handle/987654321/32786
Appears in Collections:[Department of Bioscience and Biotechnology ] Periodical Articles

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