Abstract
A total of 118 halophilic archaeal collection of strains were screened for lipolytic activity and 18 of them were found positive on Rhodamine agar plates. The selected five isolates were further characterized to determine their optimum esterase and lipase activities at various ranges of salt, temperature and pH. The esterase and lipase activities were determined by the hydrolysis of pNPB and pNPP, respectively. The maximum hydrolytic activities were found in the supernatants of the isolates grown at complex medium with 25% NaCl and 1% gum Arabic. The highest esterase activity was obtained at pH 8–8.5, temperature 60–65°C and NaCl 3–4.5 M. The same parameters for the highest lipase activities were found to be pH 8, temperature 45–65°C and NaCl 3.5–4 M. These results indicate the presence of salt-dependent and temperature-tolerant lipolytic enzymes from halophilic archaeal strains. Kinetic parameters were determined according to Lineweaver–Burk plot. The KM and V max values were lower for pNPP hydrolysis than those for pNPB hydrolysis. The results point that the isolates have higher esterase activity comparing to lipase activity.
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This study was supported by the Research Project Units of Mustafa Kemal University (project number 06 F 302) and in part by the Scientific and Technical Research Council of Turkey (TUBITAK) (project numbers 105T041 and 107T919).
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Ozcan, B., Ozyilmaz, G., Cokmus, C. et al. Characterization of extracellular esterase and lipase activities from five halophilic archaeal strains. J Ind Microbiol Biotechnol 36, 105–110 (2009). https://doi.org/10.1007/s10295-008-0477-8
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DOI: https://doi.org/10.1007/s10295-008-0477-8