Purification and Characterization of L-Aminoacylase from Alcaligenes denitrificans DA181

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概要

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• The L-aminoacylase produced intracellularly by Alcaligenes denitrificans DA181 was purified to homogeneity. This enzyme had an apparent molecular weight of 80,000, and was composed of two subunits of identical molecular weight. Its isoelectric point was pH 5.1. The optimal reaction temperature and pH were 65℃ and 8.0, respectively. This enzyme showed specificity toward N-acetyl-derivative of hydrophobic L-amino acids with N-acetyl-L-valine as the favored substrate, followed by N-acetyl-L-alanine.

• 社団法人日本農芸化学会の論文
• 1994-01-23

著者

• Tsai Y‐c

  National Yang‐ming Univ. Taipei Twn

• Li Hung

  Institute Of Biochemistry National Yang-ming Medical College

• Yang Yunn-Bor

  Institute of Biochemistry, National Yang-Ming Medical College

• Hu Hsiang-Ling

  Institute of Biochemistry, National Yang-Ming Medical College

• Chang Ming-Chung

  Department of Biochemistry, Medical College, National Cheng-Kung University

• Tsai Ying-Chieh

  Institute of Biochemistry, National Yang-Ming Medical College

• Yang Yunn-bor

  Institute Of Biochemistry National Yang-ming Medical College

• Tsai Ying-chieh

  Institute Of Biochemistry National Yang-ming Medical College

• Hu Hsiang-ling

  Institute Of Biochemistry National Yang-ming Medical College

• Chang Ming-chung

  Department Of Biochemistry Medical College National Cheng-kung University

関連論文

• Purification and Characterization of L-Aminoacylase from Alcaligenes denitrificans DA181
• Characterization of D-Aminoacylase from Alcaligenes denitrificans DA181
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