Purification and characterization of α-D-mannosidase from the seeds of Kaya, Torreya nucifera

Article abstract of DOI:10.1271/bbb.60.687

Alpha-D-mannosidase was purified from the extract of seeds of Kaya, Torreya nucifera. The purified enzyme had a molecular mass of ～ 3.6 × 10⁵ 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-mannobiose, and α-1-→6-mannobiose, with K_m of 0.785 mM, 0.236 M, 2.505 mM, and 0.268 mM, respectively. 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).

Full text of DOI:10.1271/bbb.60.687

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Purification and Characterization of α-D-Mannosidase
from the Seeds of Kaya, Torreya nucifera
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Tomomi Shiroo , Kimiko Ohtani , Kyoko Huchigami , Masato Nakatani , Isao Yuasa &
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Akira Misaki
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Faculty of Human Life Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku,
Osaka 558, Japan
Published online: 12 Jun 2014.
To cite this article: Tomomi Shiroo, Kimiko Ohtani, Kyoko Huchigami, Masato Nakatani, Isao Yuasa & Akira Misaki
(1996) Purification and Characterization of α-D-Mannosidase from the Seeds of Kaya, Torreya nucifera, Bioscience,
Biotechnology, and Biochemistry, 60:4, 687-688, DOI: 10.1271/bbb.60.687
To link to this article: http://dx.doi.org/10.1271/bbb.60.687
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