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Purification and biochemical characterization of an organic solvent‐tolerant and detergent‐stable lipase from Staphylococcus capitis
Author(s) -
Rmili Fatma,
Achouri Neila,
Smichi Nabil,
Krayem Najeh,
Bayoudh Ahmed,
Gargouri Youssef,
Chamkha Mohamed,
Fendri Ahmed
Publication year - 2019
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.2833
Subject(s) - lipase , tributyrin , chemistry , chromatography , mesophile , triacylglycerol lipase , enzyme , emulsion , food science , solvent , biochemistry , bacteria , biology , genetics
Abstract A mesophilic bacterial culture, producing an extracellular alkaline lipase, was isolated from the gas‐washing wastewaters generated from the Sfax phosphate plant of the Tunisian Chemical Group and identified as Staphylococcus capitis strain. The lipase, named S. capitis lipase (SCL), has been purified to homogeneity from the culture medium. The purified enzyme molecular weight was around 45 kDa. Specific activities about 3,900 and 500 U/mg were measured using tributyrin and olive oil emulsion as substrates, respectively at 37°C and pH 8.5. Interestingly, the SCL maintained more than 60% of its initial activity over a wide pH values ranging from 5 to 11 with a high stability between pH 9 and 11 after 1 hr of incubation at room temperature. The lipase activity was enhanced in the presence of 2 mM of Mg 2+ , Ca 2+ , and K + . SCL showed significant stability in the presence of detergents and organic solvents. Altogether, these features make the SCL useful for industrial applications. Besides, SCL was compatible with commercially available detergents, and its incorporation increases lipid degradation performances making it a potential candidate in detergent formulation.