Alteration of metal ions improves the activity and thermostability of aminoacylase from hyperthermophilic archaeon Pyrococcus horikoshii |
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| Authors: | Motomu Nishioka Koichi Tanimoto Noriko Higashi Harumi Fukada Kazuhiko Ishikawa Masahito Taya |
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| Affiliation: | (1) Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama-cho, Toyonaka Osaka, 560-8531, Japan;(2) Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Osaka, Japan;(3) Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST), Ikeda, Osaka, Japan |
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| Abstract: | Recombinant l-aminoacylase (PhoACY) from a hyperthermophilic archeon, Pyrococcus horikoshii, is a zinc-containing metalloenzyme. When the zinc was substituted by Mn2+ or Ni2+, its specific activity was significantly increased with acetyl-l-methionine as a substrate. The thermostability of PhoACY was improved when it was incubated with 1 mM Zn2+, Mn2+ or Ni2+. The enzyme with external Zn2+ addition had no significant loss of the activity when held at 90°C for up to 12 h and moreover had more than a 10-fold longer half-life even at 100°C, compared to the enzyme without Zn2+ addition. A thermostable structure of the enzyme associated with zinc binding is described based on differential scanning calorimetry. |
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| Keywords: | Aminoacylase Hyperthermophilic archaeon Metal ion effect Thermostability |
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