Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 42, Issue 4, Pages 346-352Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2007.10.015
Keywords
lipase; Streptomyces fradiae; proteolytic resistance; characterization
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A novel lipase gene, lipS221, was cloned from Streptomyces fradiae var. k11, which secretes multiple proteases. The 930-bp nucleotide sequence encodes 309 amino acid residues with a calculated molecular weight of 28.5 kDa. The protein sequence shows highest identity (82%) with a putative lipase of Streptomyces coelicolor A3(2). LipS221 was functionally expressed in Pichia pastoris and purified to homogeneity with a final specific activity of 569 U mg(-1). The purified enzyme showed the maximum activity at 55 degrees C and pH 9.8 for hydrolysis of p-nitrophenyl palmitate. Importantly, lipS221 was stable towards degradation by alkaline and neutral proteases, but activity decreased when hydrolyzed by savinase or proteinase K together with surfactant (SDS or CTAB). These results indicate that the proteolytic resistance of lipS221 may be related to its surface charge distribution. (c) 2007 Elsevier Inc. All rights reserved.
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