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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/32785

Title: Biochemical Characterization of Two Truncated Forms of Amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to Identify Its Enzymatically Active Region
Authors: Fu-Pang Lin;Hsiu-Yen Ma;Hui-Ju Lin;Shiu-Mei Liu;Wen-Shyong Tzou
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Thermoanaerobacterium saccharolyticum NTOU1;Amylopullulanase;Truncation mutagenesis;Circular dichroism
Date: 2011-10
Issue Date: 2012-06-18T06:41:33Z
Publisher: Applied Biochemistry and Biotechnology
Abstract: Abstract:The enzymatically active region of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 (TsaNTOU1Apu) was identified by truncation mutagenesis. Two truncated TsaNTOU1Apu enzymes, TsaNTOU1ApuM957 and TsaNTOU1ApuK885, were selected and characterized. Both TsaNTOU1ApuM957 and TsaNTOU1ApuK885 showed similar specific activities toward various substrates. The overall catalytic efficiency (k cat/apparent K m) for the soluble starch or pullulan substrate, however, was 20–25% lower in TsaNTOU1ApuK885 than in TsaNTOU1ApuM957. Both truncated enzymes exhibited similar thermostability and substrate-binding ability against the raw starch. The fluorescence and circular dichroism spectrometry studies indicated that TsaNTOU1ApuK885 retained an active folding conformation similar to that of TsaNTOU1ApuM957. These results indicate that a large part of the TsaNTOU1Apu, such as the C-terminal carbohydrate-binding module family 20, the second fibronectin type III, and a portion of the first FnIII motifs, could be removed without causing a serious aberrant structural change or a dramatic decrease in hydrolysis of soluble starch and pullulan.
Relation: 165(3-4), pp.1047-1056
URI: http://ntour.ntou.edu.tw/handle/987654321/32785
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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