Cloning and characterization of a novel lipase from Stenotrophomonas maltophilia GS11: The first member of a new bacterial lipase family XVI

J Biotechnol. 2016 Jun 20:228:30-36. doi: 10.1016/j.jbiotec.2016.04.034. Epub 2016 Apr 23.

Abstract

Bacterial lipases are an important group of enzymes that offer enormous potential in organic synthesis, and there is considerable interest in identifying and developing novel bacterial lipases. In previous studies, strains of the genus Stenotrophomonas were proved to be potential source of lipases, but there is little genetic information describing lipase from the genus Stenotrophomonas. We have cloned and characterized a novel lipase (LipSM54), the first lipase described from the genus Stenotrophomonas. Enzymatic study showed that LipSM54 was a cold-active, solvent-tolerant and alkaline lipase. Using bioinformatics tools, LipSM54 was found to be related only to several putative lipases from different bacterial origins, none of which could be assigned to any previously described bacterial lipase family. LipSM54 and these related putative lipases share four conserved motifs around the catalytic residues. These motifs clearly distinguish them from the known bacterial lipase families. Consequently, LipSM54 is the first characterized member of the novel bacterial lipase family.

Keywords: Bacterial lipase family; Cold-active; Lipase; Organic solvent-tolerant; Stenotrophomonas maltophilia.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Lipase / chemistry*
  • Lipase / genetics
  • Lipase / metabolism
  • Models, Molecular
  • Phylogeny
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Stenotrophomonas maltophilia / enzymology*
  • Stenotrophomonas maltophilia / genetics
  • Substrate Specificity
  • Temperature

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Lipase