Alternative strategies are required to develop the optimized production of fatty acids using biocatalysis; molecular docking and response surface methodology are efficient tools to achieve this goal. In the present study, we demonstrate a novel and robust methodology for the sustainable production of fatty acids from Moringa oleifera Lam oil using lipase‐catalyzed hydrolysis (without the presence of emulsifiers or buffer solutions). Seven commercial lipases from Candida rugosa (CRL), Burkholderia cepacia (BCL), Thermomyces lanuginosus (TLL), Rhizopus niveus (RNL), Pseudomonas fluorescens (PFL), Mucor javanicus (MJL), and porcine pancreas (PPL) were used as biocatalysts. Initial screening showed that CRL had the highest hydrolytic activity (hydrolysis degree of 81%). Molecular docking analysis contributed to the experimental results, showing that CRL displays more stable binding free energy with oleic acid (C18:1), which is the fatty acid of highest concentration in Moringa oleifera Lam oil. To evaluate and optimize the hydrolysis process, response surface methodology (RSM) was used. The effect of temperature, mass ratio oil:water, and hydrolytic activity on enzymatic hydrolysis was evaluated by central composite design using RSM. Under the optimized conditions (temperature of 37 °C, mass ratio oil:water of 25%, and hydrolytic activity of 550 U goil−1), the maximum hydrolysis degree (100%) was achieved. The present study provides a robust method for the enzymatic hydrolysis of different oils for efficient and sustainable fatty acid production.

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Guava seed biochar appears as a new alternative of the effective support to the immobilization of Burkholderia cepacia lipase (BCL) by physical adsorption. The objective of this work was to evaluate the potential of this immobilized biocatalyst in the transesterification reaction of crude coconut oil and ethanol and to understand the mechanism of the reaction through the study of molecular docking. The best loading of BCL was determined to be 0.15 genzyme/gsupport having a hydrolytic activity of 260 U/g and 54% immobilization yield. The products of transesterification reaction produced a maximum yield at 40 °C under different reaction conditions. The monoacylglycerols (MAGs) conversion of 59% was using substrate molar ratio oil:ethanol of 1:7 with the reaction time of 24 H. In addition, the highest ethyl esters yield (48%) had the molar ratio of 1:7 with the reaction time of 96 H and maximum conversion of diacylglycerols (DAGs) was 30% with the molar ratio of 1:6 with the reaction time of 24 H. Molecular Docking was applied to clarify the mechanisms of transesterification reaction at the molecular level. MAGs and DAGs are compounds with excellent emulsifying properties used in industrial production of several bioproducts such as cosmetic, pharmaceuticals, foods, and lubricants.

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Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a biocatalyst with an activity of 1197 U/gsupport at pH 7.0 and 50 °C in the hydrolysis of olive oil. The biocatalyst BCL-OS showed to be 9-fold more stable than the free lipase at 60°C in buffer solution (absence of substrates), with an increase of half-life from 16 to 144 h. The physical-chemical characterization of silica, octyl silica, and BCL-OS biocatalyst allowed confirming the immobilization of BCL onto the modified silica. The biocatalyst had an excellent performance in the synthesis of flavor esters, yielding more than 85% esterification yield (based on acid consumption) for acetic and butyric acids as acyl donors, and ethanol, butanol and hexanol as acyl acceptors. The biocatalyst could be recycled by ten 5 h-cycles of butyl butyrate syntheses at 37°C in heptane, retaining around 80% of its initial activity. Therefore, these results indicate that the BCL immobilized onto silica modified with octyl groups is a promising biocatalyst for application in organic syntheses.

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