NDLI: Characterization of extracellular esterase and lipase activities from five halophilic archaeal strains

Content Provider	Springer Nature Link
Author	Ozcan, Birgul Ozyilmaz, Gul Cokmus, Cumhur Caliskan, Mahmut
Copyright Year	2008
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.
Starting Page	105
Ending Page	110
Page Count	6
File Format	PDF
ISSN	13675435
Journal	Journal of Industrial Microbiology and Biotechnology
Volume Number	36
Issue Number	1
e-ISSN	14765535
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-10-02
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Halophilic archaea Esterase Lipase Characterization Microbiology Bioinformatics Biotechnology Genetic Engineering Inorganic Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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