Burkholderia cepacia lipase is a promising biocatalyst for biofuel production. Issue 7 (29th April 2016)

• Record Type: Journal Article
• Authors: Sasso, Francesco; Natalello, Antonino; Castoldi, Simone; Lotti, Marina; Santambrogio, Carlo; Grandori, Rita
• Is Part Of: Biotechnology journal. Volume 11:Issue 7(2016)
• Page Start: 954
• Page End: 960
• Publication Date: 2016-04-29
• Subjects: Biofuel -- Circular dichroism -- Conformational stability -- Intrinsic fluorescence -- Transesterification; Biotechnology -- Periodicals; 660.605
• DOI: 10.1002/biot.201500305
• Languages: English
• ISSNs: 1860-6768

Abstract

Abstract: Lipases resistant to inhibition and denaturation by methanol are valuable tools for biotechnological applications, in particular for biofuel production. Microbial lipases have attracted a great deal of interest because of their stability at high concentrations of organic solvents. Burkholderia cepacia lipase (BCL) is tested here for robustness towards methanol in terms of conformational stability and catalytic activity in transesterification assays. This lipase turns out to be even more tolerant than the homologous and better characterized enzyme from Burkholderia glumae . BCL unfolding transition, as monitored by far‐UV circular dichroism (CD) and intrinsic fluorescence, displays a T m above 60°C in the presence of 50% methanol. The protein unfolds at low pH, and the organic solvent affects the nature of the denatured state under acidic conditions. The protein performs well in transesterification assays upon prolonged incubations at high methanol concentrations. BCL is highly tolerant to methanol and displays particularly high conformational stability under conditions employed for transesterification reactions. These features depict BCL as a promising enzyme for biofuel industry. Abstract : Lipases resistant to methanol are useful catalysts for biofuel production. In this work, the conformational stability of Burkholderia cepacia lipase and its enzymatic activity in transesterification assays is studied. The protein has been shown to present a high robustness towards methanol and good performances in transesterification reactions. These features depict this lipase as a promising enzyme for biofuel industry.