Purification and Characterization of α-D-Mannosidase from the Seeds of Kaya, Torreya nucifera

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概要

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• Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of 〜3.6 x 10^5 daltons. This enzyme had an optimum pH at 4.5, and was stable at pH between 5.5 and 6.5. This enzyme appeared to be a metal enzyme containing Zn^<2+>. The enzyme hydrolyzed p-nitrophenyl-α-D-mannoside, methyl-α-D-mannoside, α-1→3-man-nobiose, and α-1→6-mannobiose, with K_m of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, fespectively. The hydrolysis of various α-linked mannobioses indicated that the enzyme hydrolyzes the α-mannobioses in the order of α-(1→2)> -(1→6)> -(1→3).

• 社団法人日本農芸化学会の論文
• 1996-04-23

著者

• 湯浅 勲

  鳥取大学 法医

• Yuasa I

  Tottori Univ. Yonago Jpn

• Yuasa Isao

  Faculty Of Human Life Science Osaka City University

• Ohtani Kimiko

  Faculty of Human Life Science, Osaka City University

• Misaki Akira

  Faculty of Human Life Science, Osaka City University

• 湯浅 勲

  Department Of Legal Medicine Tottori University School Of Medicine

• Misaki A

  Osaka City Univ. Osaka Jpn

• Ohtani Kimiko

  Faculty Of Human Life Science Osaka City University

• Nakatani Masato

  Faculty Of Human Life Science Osaka City University

• SHIROO Tomomi

  Faculty of Human Life Science, Osaka City University

• HUCHIGAMI Kyoko

  Faculty of Human Life Science, Osaka City University

• Shiroo Tomomi

  Faculty Of Human Life Science Osaka City University

• Huchigami Kyoko

  Faculty Of Human Life Science Osaka City University

• Misaki Akira

  Faculty Of Human Life Science Osaka City University

• OHTANI Kimiko

  Faculty of Home Science, Mukogawa Woman's University:(Present office)Faculty of Science of Living, Osaka City University

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