Characterization of Catalase from Psychrotolerant Psychrobacter piscatorii T-3 Exhibiting High Catalase Activity

International Journal of Molecular Sciences

Hideyuki Kimoto²  Kazuaki Yoshimune¹  Hidetoshi Matsuyma² 

[1] Department of Applied Molecular Chemistry, College of Industrial Technology, Nihon University, 1-2-1, Izumichou, Narashino, Chiba 275-8575 Japan; E-Mail:;Department of Bioscience and Technology, School of Engineering, Tokai University, Minamisawa, Minami-ku, Sapporo 005-8601 Japan; E-Mails:

关键词: catalase;    Psycrobacter piscatorii;    PktA;    hydrogen peroxide;   

DOI  :  10.3390/ijms13021733

来源: mdpi

【 摘 要 】

A psychrotolerant bacterium, strain T-3 (identified as Psychrobacter piscatorii), that exhibited an extraordinarily high catalase activity was isolated from the drain pool of a plant that uses H₂O₂ as a bleaching agent. Its cell extract exhibited a catalase activity (19,700 U·mg protein⁻¹) that was higher than that of Micrococcus luteus used for industrial catalase production. Catalase was approximately 10% of the total proteins in the cell extract of the strain. The catalase (PktA) was purified homogeneously by only two purification steps, anion exchange and hydrophobic chromatographies. The purified catalase exhibited higher catalytic efficiency and higher sensitivity of activity at high temperatures than M. luteus catalase. The deduced amino acid sequence showed the highest homology with catalase of Psycrobacter cryohalolentis, a psychrotolelant bacterium obtained from Siberian permafrost. These findings suggest that the characteristics of the PktA molecule reflected the taxonomic relationship of the isolate as well as the environmental conditions (low temperatures and high concentrations of H₂O₂) under which the bacterium survives. Strain T-3 efficiently produces a catalase (PktA) at a higher rate than Exiguobacterium oxidotolerans, which produces a very strong activity of catalase (EktA) at a moderate rate, in order to adapt to high concentration of H₂O₂.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.