Oil pollution remains a persistent global environmental challenge due to the recalcitrance and toxicity of lipid-rich contaminants in terrestrial and aquatic ecosystems. Bacterial lipases (EC 3.1.1.3) play a pivotal role in the initial stages of bioremediation by catalysing the hydrolysis of complex lipids into more bioavailable intermediates, thereby facilitating downstream microbial degradation and mineralisation. This review critically examines the mechanistic basis of lipase-mediated hydrocarbon degradation, with emphasis on enzyme structure–function relationships, catalytic pathways, and regulation under environmentally relevant conditions. In addition to conventional applications in soil and wastewater bioremediation, emerging strategies involving immobilised enzymes, microbial consortia, and waste-derived substrates are evaluated for their effectiveness and scalability. Attention is given to advances in molecular and omics approaches, including metagenomics, transcriptomics, and proteomics, which have expanded the discovery of novel lipases but remain limited in their ability to predict in situ functionality. The review highlights the growing role of protein engineering and artificial intelligence in tailoring lipase properties; however, it also critically assesses current limitations, including insufficient experimental validation and challenges in translating computational predictions to complex environmental systems. Furthermore, integrating multi-omics data into quantitative and predictive frameworks is identified as a key future direction for improving bioremediation efficiency. Despite significant progress, major gaps persist in linking enzyme activity to real-world degradation performance and in developing standardized, scalable approaches. This review therefore provides a comprehensive and critical synthesis of current knowledge while identifying strategic research priorities required to advance bacterial lipases as robust tools for sustainable bioremediation of lipid-based pollutants.
A. Baruwa, Nyashadzashe P. Masvingwe, G. Kana et al.· Applied Sciences· 0 citations
Lipases are important enzymes in the esterase family that hydrolyze ester bonds in triglycerides, producing simpler molecules. This property makes them valuable in biotechnology and environmental cleanup. In this study, lipase-producing bacteria were isolated and characterized from petroleum-contaminated soil to establish a cost-effective platform for enzyme production and bioremediation. Among the recovered isolates, Serratia liquefaciens AB1 exhibited the highest lipolytic activity and was therefore selected for further investigation. The influence of various inducer oils and agro-industrial residues on enzyme production was systematically assessed. In addition, fermentation parameters were optimized through the evaluation of different carbon and nitrogen sources to enhance lipase yield. Waste frying oil was identified as the most effective inducer, while glucose and yeast extract supported optimal enzyme production. The enzyme lipase AB1 was fully purified using CM-Sephadex C-50 chromatography, Sephadex G-100 and further characterized by SDS-PAGE, kinetic studies, and stability assays. Purification of the enzyme resulted in a specific activity of 610.92 U/mg, corresponding to a 9.42-fold increase in purity with an overall recovery of 76%. The enzyme exhibited an apparent molecular mass of approximately 64 kDa. It demonstrated optimal catalytic activity at 60 °C and pH 8 and retained substantial stability at this temperature for up to 120 min. Kinetic analysis revealed a low Km value of 30 µM, indicating strong substrate affinity, along with a Vmax of 23.89 U/mL, reflecting a high catalytic efficiency under the tested conditions. Enzyme activity was enhanced by Ca2+, Na+, and Ba2+, but inhibited by Mn2+ and Hg2+. These findings demonstrate the favorable biochemical properties of the purified lipase and provide a basis for future investigations into its potential application as a biocatalyst for bioremediation.
A. Baruwa, K. Permaul· Applied microbiology· 0 citations
