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

• 資料種別: 記事
• タイトル: α-amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong) : nucleotide sequence analysis, cloning and expression
• 著者・編者: Saijai Posoongnoen; Raksmont Ubonbal; Sompong Thammasirirak
• 出版事項: 日本 : 日本植物細胞分子生物学会
• 出版年月日等: 2015
• 出版年（W3CDTF）: 2015
• タイトル（掲載誌）: Plant biotechnology
• 巻号年月日等（掲載誌）: 32(1)
• 掲載巻: 32(1)
• ISSN（掲載誌）: 1347-6114
• ISSN-L（掲載誌）: 1342-4580
• 本文の言語コード: eng
• DOI: 10.5511/plantbiotechnology.14.1122a; https://doi.org/10.5511/plantbiotechnology.14.1122a
• 国立国会図書館永続的識別子: info:ndljp/pid/11000412; https://dl.ndl.go.jp/pid/11000412
• コレクション（共通）: 障害者向け資料
• コレクション（障害者向け資料：レベル1）: テキストデータ
• コレクション（個別）: 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > 学術機関 > 学協会; https://dl.ndl.go.jp/collections/B00043
• 収集根拠: インターネット資料収集保存事業（WARP）
• 受理日（W3CDTF）: 2017-12-08T10:56:38+09:00
• 保存日（W3CDTF）: 2015-08-15
• 記録形式（IMT）: application/pdf
• オンライン閲覧公開範囲: インターネット公開
• 遠隔複写可否（NDL）: 不可
• 掲載誌（URI）: https://warp.da.ndl.go.jp/info:ndljp/pid/9483390/www.jspcmb.jp/journal/pb32_1.html
• 掲載誌（国立国会図書館永続的識別子）: info:ndljp/pid/11000411; https://dl.ndl.go.jp/pid/11000411
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館デジタルコレクション; https://dl.ndl.go.jp

• コレクション（個別）: 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > 学術機関 > 学協会; https://dl.ndl.go.jp/collections/B00043
• オンライン閲覧公開範囲: インターネット公開
• 遠隔複写可否（NDL）: 不可
• 所蔵機関: 国立国会図書館
• 請求記号: Z54-J126
• 関連情報（URI）: http://dl.ndl.go.jp/info:ndljp/pid/11000412
• 関連情報（国立国会図書館永続的識別子）: info:ndljp/pid/11000412; http://dl.ndl.go.jp/info:ndljp/pid/11000412
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館雑誌記事索引; https://ndlsearch.ndl.go.jp
• 書誌ID（NDLBibID）: 026292476; http://id.ndl.go.jp/bib/026292476
• 整理区分コード: 632

• 要約等: 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 (<i>Durio zibethinus</i> 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 <i>Escherichia coli</i>. 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.
• DOI: 10.5511/plantbiotechnology.14.1122a
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: 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 (<i>Durio zibethinus</i> 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 <i>Escherichia coli</i>. 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.
• DOI: 10.5511/plantbiotechnology.14.1122a; https://doi.org/10.5511/plantbiotechnology.14.1122a
• オンライン閲覧公開範囲: インターネット公開
• 関連情報（URI）: http://id.ndl.go.jp/bib/026292476; https://ndlsearch.ndl.go.jp/books/R000000004-I026292476; https://dl.ndl.go.jp/pid/11000412; http://id.ndl.go.jp/digimeta/11000412
• 参照: Purification and characterization of thermostable α-amylase from germinating Sword bean (Canavalia gladiata (Jacq.) DC.) seeds; https://cir.nii.ac.jp/crid/1390565134843562752
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• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; Crossref; https://www.crossref.org; CiNii Articles
• 書誌ID（NDLBibID）: 026292476; http://id.ndl.go.jp/bib/026292476; 11000412; http://id.ndl.go.jp/bib/11000412
• NII論文ID: 130005061607