Journal of Microbiology

Research Support, Non-U.S. Gov'ts

Physiological and Metabolic Responses for Hexadecane Degradation in Acinetobacter oleivorans DR1: Jaejoon Jung , Jaemin Noh , Woojun Park; J. Microbiol. 2011;49(2):208-215. Published online May 3, 2011; DOI: https://doi.org/10.1007/s12275-011-0395-8

Abstract: The hexadecane degradation of Acinetobacter oleivorans DR1 was evaluated with changes in temperature and ionic salt contents. Hexadecane degradation of strain DR1 was reduced markedly by the presence of sodium chloride (but not potassium chloride). High temperature (37°C) was also shown to inhibit the motility, biofilm formation, and hexadecane biodegradation. The biofilm formation of strain DR1 on the oil-water interface might prove to be a critical physiological feature for the degradation of hexadecane. The positive relationship between biofilm formation and hexadecane degradation could be observed at 30°C, but not at low temperatures (25°C). Alterations in cell hydrophobicity and EPS production by temperature and salts were not correlated with biofilm formation and hexadecane degradation. Our proteomic analyses have demonstrated that metabolic changes through the glyoxylate pathway are important for efficient degradation of hexadecane. Proteins involved in fatty acid metabolism, gluconeogenesis, and oxidative stress defense proteins appear to be highly expressed during biodegradation of hexadecane. These results suggested that biofilm formation and oxidative stress defense are important physiological responses for hexadecane degradation along with metabolic switch to glyoxylate pathway in strain DR1.

Comparative Proteomic Analysis of Virulent Korean Mycobacterium tuberculosis K-strain with Other Mycobacteria Strain Following Infection of U-937 Macrophage: Sung Weon Ryoo , Young Kil Park , Sue-Nie Park , Young Soo Shim , Hyunjeong Liew , Seongman Kang , Gill-Han Bai; J. Microbiol. 2007;45(3):268-271.; DOI: https://doi.org/2532 [pii]

Abstract: In Korea, the Mycobacterium tuberculosis K-strain is the most prevalent clinical isolates and belongs to the Beijing family. In this study, we conducted comparative porteomics of expressed proteins of clinical isolates of the K-strain with H37Rv, H37Ra as well as the vaccine strain of Mycobacterium bovis BCG following phagocytosis by the human monocytic cell line U-937. Proteins were analyzed by 2-D PAGE and MALDITOF-MS. Two proteins, Mb1363 (probable glycogen phosphorylase GlgP) and MT2656 (Haloalkane dehalogenase LinB) were most abundant after phagocytosis of M. tuberculosis K-strain. This approach provides a method to determine specific proteins that may have critical roles in tuberculosis pathogenesis.

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