Abstract
Even though lipase genes from a variety of microorganism have been cloned and over-expressed, the prospective lipase resources for commercial production and industry application are still limited. In the present study, a lipase from Burkholderia cepacia Lu10-1 is heterologously over-expressed in Escherichia coli strain BL21(DE3) and purified to homogeneity. The molecular weight of the recombinant lipase from B. cepacia Lu10-1 (abbreviated as lipase Lu10-1) is estimated to be about 33 kDa by SDS-PAGE. The lipase Lu10-1 has a priority for the long- chain length substrates. The optimal temperature of lipase Lu10-1 is 60°C and it preserves high thermostability with residual activities of over 80% after 100 h at 60°C or over 60% after 30 h at 70°C. The optimal pH of lipase Lu10-1 is 9.0 and it has broad pH adaptability over a range of 5.0-10.0 retaining 80% activity between pH 6.0 and 9.0 after incubation at 37°C for 24 h. Moreover, the enzymatic activity of lipase Lu10-1 is not obviously affected by several metal ions and it exhibites solid tolerance and stability towards various surfactants and organic solvents. The present study provides the basis for the potential applications of lipase Lu10-1 in related industries.
Highlights
Lipase, or triacylglycerol acylhydrolase (EC 3.1.1.3) can hydrolyze glycerol at the oil-water interface and ester bonds of triglycerides, and catalyze transesterification and ester synthesis
Nucleotide sequence analysis indicated that this lipase gene length was 960 bp for encoding a mature protein consisting of 320 amino acids
Multiple sequence alignment showed that lipase Lu10-1 shared 99.8% homology of nucleotide sequence and 100% homology of amino acid sequence with that of Burkholderia sp
Summary
Triacylglycerol acylhydrolase (EC 3.1.1.3) can hydrolyze glycerol at the oil-water interface and ester bonds of triglycerides, and catalyze transesterification and ester synthesis. It has been reported that the lipase from Burkholderia (previously Pseudomonas) cepacia possesses attractive particular interest due to its high thermostability and strong tolerance to organic solvents (Jia et al, 2010; Mello Bueno et al, 2015; Sasso et al, 2016), different kinds of Burkholderia lipase genes have been cloned and over-expressed in heterogonous or homologous hosts (Jia et al, 2010; Shu et al, 2016; Wang et al, 2009; Xie et al, 2016; Yang et al, 2007). The high yield of the active forms in heterogonous host such as Escherichia coli has not yet been achieved. The main reason is that most of lipase proteins exist in the cell periplasmic space in the form of inactive inclusion bodies and the refolding procedure is request to obtain the active proteins, which limits the lipase for large-scale industrial application
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