Protein Engineering of Penicillinase as Affinity Ligands for Bioprocessing

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概要

• 論文の詳細を見る

• The activie site and the substrate binding site of penicillinase (β-lactamase) from bacillus licheniformis were altered in this study so that the enzyme retains the specific binding capability to the β-lactam antibiotics, but fails to hydrolye them When Lys47 in the enzyme molecule was replaced by Ala47,the mutant protein PenP(KA) lost not only its catalytic activity but also the substrate binding ability. In contrast, when Ser44 was replaced by Ala, the mutant protein PenP(SA) lost its catalytic activity but still kept the substrate binding ability. It was found that PenP(SA) exhibited the characteristic association and dissociation with penicillin G, but the dissociation constant was much larger then expected. Possible use of this mutant protein as an affinity ligand is also discussed.

• 公益社団法人日本生物工学会の論文
• 1989-05-25

著者

• Imanaka Tadayuki

  Department Of Applied Biotechnology Faculty Of Engineering Osaka University

• Imanaka Tadayuki

  Department Of Fermentation Technology Faculty Of Engineering Osaka University

• Wang H

  Michigan Biotechnology Inst. Michigan Usa

• Kuroda Akio

  Department Of Molecular Biotechnology Hiroshima University

• Wang Henry

  Department Of Chemical Engineering The University Of Michigan

• Kuroda Akio

  Department Of Fermentation Technology Faculty Of Engineering Osaka University

• Kuroda Akio

  Department Of Chemistry Faculty Of Science Nagoya University

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