Lubricants based on fatty acid ester (FAE) mixtures are widely used in the textile industry, e.g., in spin finishes applied during the production of synthetic fibres, or in sizes added to fibres before weaving. FAE lubricants can significantly impact the dyeing quality of a textile due to their hydrophobicity and must therefore be removed before dyeing. However, the solvents currently used for their removal pose an environmental risk, and biobased solutions are thus sought. A lipase-assisted pre-dyeing treatment for synthetic fibre textiles was developed in this study. Six lipases were tested for their ability to hydrolyse FAEs from a polyamide-with-elastane textile, and all were found to be active. The conditions for the washing of lipase-treated textiles were found to be crucial for the performance of the process. Among the possible lipid hydrolysis products of tripalmitin (selected as a model FAE), only palmitic acid removal improved during washing, in comparison with the original FAE. This improvement only occurred with washing solutions containing a monovalent base. A combination of lipase treatment and washing with a non-ionic surfactant and monovalent base was found to be effective in the removal of FAEs, with a performance similar to a current solvent-based pre-treatment process.

Several strategies can be employed for the identification of novel microbial lipases. Despite the increasing importance of metagenomics in bioprospecting, significant limitations in the expression of recombinant proteins, and lipases in particular, remain. Culture-based bioprospecting approaches are, therefore, still valuable. In this work, a collection of bacterial isolates, mainly of marine origin, was screened for lipase activity through a culture-based approach. Screening for lipolytic bacteria was performed in solid media containing olive oil emulsions and rhodamine B. Positive isolates were subsequently grown in liquid media, to confirm lipase production. Significant hydrolytic activity towards the triglyceride substrates tributyrin and triolein could be observed with the biomass produced, although no lipase activity could be detected in the culture supernatants. Six isolates presenting high activity were characterized as whole-cell biocatalysts, and all were found to be active at temperatures ranging between 25 and 65 °C, and at pH values between 6 and 10.5. Genomic analyses of two of these Gram-negative lipase-producing isolates revealed the presence of several hypothetical genes encoding for lipolytic enzymes, including outer cell-bound enzymes, predicted through the application of machine-learning tools. These natural isolates, containing cell-associated lipases, may therefore be of special interest for application as whole-cell biocatalysts.