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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: 國立臺灣海洋大學:海洋生物研究所
Keywords: Truncation mutagenesis
Circular dichroism
Thermoanaerobacterium saccharolyticum NTOU1
Date: 2011
Issue Date: 2018-05-02T02:56:51Z
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
Appears in Collections:[Institute of Marine Biology] Periodical Articles

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