Purification and Characterization of Endo-Pectate Lyase from Bacillus macerans(Biological Chemistry)

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概要

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• Bacillus macerans produced an extracellular ewrfo-pectate lyase when cultivated with grated potato tuber. The enzyme activity was markedly activated by 1m_M calcium or manganese ion, but completely inactivated by ethylenediaminetetraacetate (EDTA). The activity was maximum at pH 9.0 and 60℃. The enzyme activity was stable up to 50℃ and 55℃ for 10 min at pH 9.0 in the absence and presence of calcium ion, respectively, and between pH 6.5 and 9.5 for 2 hr at 37℃. The enzyme had a molecular weight of 35,000 and a pI of 10.3. The Michaelis constant and maximum reaction velocity of the enzyme for polypectate were 0.11% and 74μmol of unsaturated galacturonate formed per min per mg protein, respectively. The enzyme also attacked pectin that contained 4.3% methoxyl groups. The enzyme was stable in 100 m_M ammonium chloride buffer (pH 9.0) for a month at 10℃, but 70% of its activity was lost in 20 m_M ammonium chloride buffer (pH 9.0) after 24 hr at 10℃.

• 社団法人日本農芸化学会の論文
• 1991-01-23

著者

• Miyazaki Yoshimitsu

  Department Of Applied Biological Sciences Faculty Of Agriculture Saga University

• MIYAZAKI Yoshimitsu

  Department of Agricultural Chemistry, Faculty of Agriculture, Saga University

関連論文

• Purification, Crystallization, and Properties of β-Galactosidase from Bacillus macerans(Biological Chemistry)
• Purification and Characterization of Endo-Pectate Lyase from Bacillus macerans(Biological Chemistry)

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