Purification, biochemical characterization, and gene cloning of a new extracellular thermotolerant and glucose tolerant maltooligosaccharide-forming α-amylase from an endophytic ascomycete Fusicoccum sp. BCC4124

• CHAMPREDA Verawat

  Molecular and Enzyme Screening Laboratory, BIOTEC Central Research Unit, National Center for Genetic Engineering and Biotechnology

• KANOKRATANA Pattanop

  Molecular and Enzyme Screening Laboratory, BIOTEC Central Research Unit, National Center for Genetic Engineering and Biotechnology

• SRIPRANG Rutchadaporn

  Molecular and Enzyme Screening Laboratory, BIOTEC Central Research Unit, National Center for Genetic Engineering and Biotechnology

• TANAPONGPIPAT Sutipa

  Molecular and Enzyme Screening Laboratory, BIOTEC Central Research Unit, National Center for Genetic Engineering and Biotechnology

• EURWILAICHITR Lily

  Molecular and Enzyme Screening Laboratory, BIOTEC Central Research Unit, National Center for Genetic Engineering and Biotechnology

書誌事項

タイトル別名

• Purification, Biochemical Characterization, and Gene Cloning of a New Extracellular Thermotolerant and Glucose Tolerant Maltooligosaccharide-Forming .ALPHA.-Amylase from an Endophytic Ascomycete Fusicoccum sp. BCC4124
• Purification biochemical characterization and gene cloning of a new extracellular thermotolerant and glucose tolerant maltooligosaccharide forming a amylase from an endophytic ascomycete Fusicoccum sp BCC4124
• Purification, Biochemical Characterization, and Gene Cloning of a New Extracellular Thermotolerant and Glucose Tolerant Maltooligosaccharide-Forming α-Amylase from an Endophytic Ascomycete<i>Fusicoccum</i>sp. BCC4124

抄録

An endophytic fungus, Fusicoccum sp. BCC4124, showed strong amylolytic activity when cultivated on multi-enzyme induction enriched medium and agro-industry substrates. α-Amylase and α-glucosidase activities were highly induced in the presence of maltose and starch. The purified target α-amylase, Amy-FC1, showed strong hydrolytic activity on soluble starch (kcat/Km=6.47×10³ min⁻¹(ml/mg)) and selective activity on γ- and β-cyclodextrins, but not on α-cyclodextrin. The enzyme worked optimally at 70 °C in a neutral pH range with t_1⁄2 of 240 min in the presence of Ca²⁺ and starch. Maltose, matotriose, and maltotetraose were the major products from starch hydrolysis but prolonged reaction led to the production of glucose, maltose, and maltotriose from starch, cyclodextrins, and maltooligosaccharides (G3–G7). The amylase showed remarkable glucose tolerance up to 1 M, but was more sensitive to inhibition by maltose. The deduced protein primary structure from the putative gene revealed that the enzyme shared moderate homology between α-amylases from Aspergilli and Lipomyces sp. This thermotolerant, glucose tolerant maltooligosaccharide-forming α-amylase is potent for biotechnological application.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 71 (8), 2010-2020, 2007

  公益社団法人 日本農芸化学会

キーワード

• <I>Fusicoccum</I> sp.
• α-amylase
• thermostability
• glucose tolerant
• gene cloning

詳細情報

• CRID: 1390001206479021056
• NII論文ID: 10027517892
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.70198
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 8887800
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8887800
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.70198
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可