Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA

Biochimie
C BofillPilar Diaz

Abstract

Growth of Pseudomonas sp. 42A2 on oleic acid releases polymerized hydroxy-fatty acids as a result of several enzymatic conversions that could involve one or more lipases. To test this hypothesis, the lipolytic system of strain Pseudomonas sp. 42A2 was analyzed, revealing the presence of at least an intracellular carboxylesterase and a secreted lipase. Consensus primers derived from a conserved region of bacterial lipase subfamilies I.1 and I.2 allowed isolation of two secreted lipase genes, lipA and lipC, highly homologous to those of Pseudomonas aeruginosa PAO1. Homologous cloning of the isolated lipA and lipC genes was performed in Pseudomonas sp. 42A2 for LipA and LipC over-expression. The overproduced lipases were further purified and characterized, both showing preference for medium fatty acid chain-length substrates. However, significant differences could be detected between LipA and LipC in terms of enzyme kinetics and behaviour pattern. Accordingly, LipA showed maximum activity at moderate temperatures, and displayed a typical Michaelis-Menten kinetics. On the contrary, LipC was more active at low temperatures and displayed partial interfacial activation, showing a shift in substrate specificity when assayed at differen...Continue Reading

Citations

Nov 16, 2011·Applied Microbiology and Biotechnology·Noelia Torrego-SolanaAngeles Manresa
May 31, 2011·Biochimica Et Biophysica Acta·Jean Borges BertoldoHernán Terenzi
Apr 6, 2019·Acta Crystallographica. Section F, Structural Biology Communications·Florian BleffertFilip Kovacic
Apr 4, 2021·International Journal of Molecular Sciences·Irene Jurado-MartínSiobhán McClean
Jul 20, 2021·Current Microbiology·Zhenghong Zhang, Xuehong Zhang

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