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 Tm 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.

Sasso, F., Natalello, A., Castoldi, S., Lotti, M., Santambrogio, C., Grandori, R. (2016). Burkholderia cepacia lipase is a promising biocatalyst for biofuel production. BIOTECHNOLOGY JOURNAL, 11(7), 954-960 [10.1002/biot.201500305].

Burkholderia cepacia lipase is a promising biocatalyst for biofuel production

SASSO, FRANCESCO
Primo
;
NATALELLO, ANTONINO
Secondo
;
LOTTI, MARINA;SANTAMBROGIO, CARLO
;
GRANDORI, RITA
Ultimo
2016

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 Tm 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.
Articolo in rivista - Articolo scientifico
Biofuel; Circular dichroism; Conformational stability; Intrinsic fluorescence; Transesterification;
Biofuel; Circular dichroism; Conformational stability; Intrinsic fluorescence; Transesterification; Applied Microbiology and Biotechnology; Molecular Medicine
English
2016
11
7
954
960
partially_open
Sasso, F., Natalello, A., Castoldi, S., Lotti, M., Santambrogio, C., Grandori, R. (2016). Burkholderia cepacia lipase is a promising biocatalyst for biofuel production. BIOTECHNOLOGY JOURNAL, 11(7), 954-960 [10.1002/biot.201500305].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/127833
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