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BioMed Research International
Volume 2014, Article ID 409626, 7 pages
http://dx.doi.org/10.1155/2014/409626
Research Article

Purification and Characterization of Catalase from Marine Bacterium Acinetobacter sp. YS0810

1Key Laboratory of Sustainable Development of Marine Fisheries, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China
2Shanghai Ocean University, Shanghai 201306, China
3Weifang Medical University, Weifang 261053, China
4School of Electrical and Information Engineering, Jiangsu University, Zhenjiang 212013, China
5Marine Products Resource and Enzyme Engineering Laboratory, Yellow Sea Fisheries Research Institute, 106 Nanjing Road, Qingdao, Shandong 266071, China

Received 29 March 2014; Accepted 27 May 2014; Published 18 June 2014

Academic Editor: Pier A. Borea

Copyright © 2014 Xinhua Fu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The catalase from marine bacterium Acinetobacter sp. YS0810 (YS0810CAT) was purified and characterized. Consecutive steps were used to achieve the purified enzyme as follows: ethanol precipitation, DEAE Sepharose ion exchange, Superdex 200 gel filtration, and Resource Q ion exchange. The active enzyme consisted of four identical subunits of 57.256 kDa. It showed a Soret peak at 405 nm, indicating the presence of iron protoporphyrin IX. The catalase was not apparently reduced by sodium dithionite but was inhibited by 3-amino-1,2,4-triazole, hydroxylamine hydrochloride, and sodium azide. Peroxidase-like activity was not found with the substrate o-phenylenediamine. So the catalase was determined to be a monofunctional catalase. N-terminal amino acid of the catalase analysis gave the sequence SQDPKKCPVTHLTTE, which showed high degree of homology with those of known catalases from bacteria. The analysis of amino acid sequence of the purified catalase by matrix-assisted laser desorption ionization time-of-flight mass spectrometry showed that it was a new catalase, in spite of its high homology with those of known catalases from other bacteria. The catalase showed high alkali stability and thermostability.