α-Amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

• Posoongnoen Saijai

  Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University

• Ubonbal Raksmont

  Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University

• Thammasirirak Sompong

  Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University

• Daduang Jureerut

  Department of Clinical Chemistry, Faculty of Associated Medical Sciences, Khon Kaen University

• Minami Hiromichi

  Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University

• Yamamoto Kenji

  Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University

• Daduang Sakda

  Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Department of Biochemistry, Faculty of Science, Khon Kaen University

書誌事項

タイトル別名

• α-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression
• &#x3b1;-Amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong)-nucleotide sequence analysis, cloning and expression

抄録

Amylase is hypothesized to involve in the initiation of intracellular starch granule digestion in the plastids of ripening durians. A putative α-amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong; DzAmy3) was successfully isolated and its gene contain a 2,679 base pair open reading frame, which encodes 892 amino acids with a calculated molecular mass of 93.7 kDa and an isoelectric point of 5.77. The DzAmy3 contains starch binding domain with a putative plastid transit peptide and α-amylase like domain. Phylogenetic tree analysis proved it into the family three of plant α-amylases. The predicted structural model proposed a catalytic triad (Asp611, Glu636 and Asp719) for general acid/base hydrolysis. Recombinant DzAmy3 (rDzAmy3) was successfully expressed in Escherichia coli. rDzAmy3 hydrolyzed starch and ethylidene-pNP-G7 which confirms the authenticity of DzAmy3 gene and functional α-amylase. The rDzAmy3 had an optimum activity at pH 8.0 and 30°C. It was stable in the pH range of 7–8 at 37°C, temperature range of 5–20°C and in the presence of 1% (v/v) Tween 20 and Triton X-100. Substrate specificity analysis revealed that rDzAmy3 was active toward β-limit dextrin, starch, amylopectin, amylose and glycogen.

収録刊行物

• Ｐｌａｎｔ　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ

  Ｐｌａｎｔ　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ 32 (1), 1-10, 2015

  日本植物バイオテクノロジー学会

キーワード

• α-Amylase
• Mon Thong durian
• structural characterization
• expression
• amylase activity

詳細情報

• CRID: 1390001204326868480
• NII論文ID: 130005061607
• NII書誌ID: AA11250821
• DOI: 10.5511/plantbiotechnology.14.1122a
• ISSN: 13476114
• ISSN: 13424580
• NDL書誌ID: 026292476
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I026292476
• 本文言語コード: en
• データソース種別:
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  • CiNii Articles
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