Purification and Properties of D-Aminoacylase from Alcaligenes denitrificans subsp. xylosoxydans MI-4

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概要

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• D-Aminoacylase has been purifies 144-fold to electrophoretic homogeneity by ammonium sulfate fractionation, DEAE-Toyopearl and affinity column choromatographies, and Sephadex G-100 gel filtration from the crude extracts of Alcaligenes dentirificans subsp. xylosoxydans MI-4. The enzyme was composed of a single polypeptide of about 51,000. The enzyme catalyzed hydrolysis of N-acyl-derivatives of neutral D-amino acids. Optimal pH and temperature were 7.8 and 50℃. The apparent K_m and the V_<max> for N-acetyl-D-henylalanine were 14.1mM and 1331 units/mg protein, respectively. The activity of the enzyme was inhibited by N-accetyl-D-valine(K_i=2.15mM)and N-acetyl-D-alloisoleucine(K_i=1.47mM), but not by its products(i. e., amino acids and acetate). The enzyme also had dipeptidase activity. Activation by metal ions was not observed.

• 社団法人日本生物工学会の論文
• 1991-02-25

著者

• MORIGUCHI Mitsuaki

  Department of Applied Chemistry, Faculty of Engineering, Oita University

• Moriguchi Mitsuaki

  Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University

• Moriguchi Mitsuaki

  Department Of Applied Chemistry Faculty Of Engineering Oita University

• SAKAI KENNJI

  Department of Environmental Chemistry and Engineering, Faculty of Engineering, Oita University

• OBATA TAKETERU

  Department of Environmental Chemistry and Engineering, Faculty of Engineering, Oita University

• IDETA KOHTARO

  Department of Environmental Chemistry and Engineering, Faculty of Engineering, Oita University

• Sakai Kennji

  Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University

• Obata Taketeru

  Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University

• Ideta Kohtaro

  Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University

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