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Biolubricants produced by chemically modifying vegetable oils are promising to replace mineral-based lubricants. However, the performances of biolubricants synthesized through traditional chemical modification routes, such as transesterification/esterification, epoxidation with further ring opening, and estolide formation, cannot satisfy the demands of extreme conditions. Meanwhile, complicated multi-step reactions cause expensive costs, which hinders their large-scale application. In this study, pelargonic acid (PA) derived from the cleavage of oleic acid was esterified with trimethylolpropane (TMP) to produce branched-chain esters (tri-TMP esters) catalyzed by the lipase (Candida sp. 99–125), focusing on batch stability of the lipase, thermal-oxidation stability and lubrication performance of the product. The lipase maintained high activity for 4 continuous batches in 5 L enzyme reactor with the conversion of PA > 96% and the accumulation of tri-TMP esters > 84% in each batch. The obtained tri-TMP esters had a pour point of − 56 °C, a viscosity index of 137, and a flash point of 276 °C. Anti-oxidation stability test and thermogravimetric behaviors showed that the biolubricant had favorable thermal-oxidative stability. Friction tests verified that the product displayed excellent lubrication performance with a minimum coefficient of friction (COF) of 0.099 and an average wear spot diameter (WSD) of 221.5 µm. The green and high-selective synthetic pathway fills the defect of existing routes for the preparation of biolubricants from chemically modified vegetable oils. [Display omitted] • Lipase-catalyzed synthesis of branched-chain esters based on PA and TMP was proposed. • The lipase maintained high activity for 4 continuous batches. • The tri-TMP esters has superior low-temperature performance and thermal-oxidative stability. • This biolubricant displayed excellent lubrication performance in HFRR tests. [ABSTRACT FROM AUTHOR]

In this work, the acetone-butanol-ethanol (ABE) fermentation was upgraded in order to improve its economy. Fed-batch fermentation was integrated with two-stage gas stripping-pervaporation unit. The permeated ABE condensate was used as substrate for oleates production. Candida sp. 99–125 cells, being rich in lipase activity, were used as full-cell catalyst. Different ABE feeding strategies in the esterification process were compared. As results, 10.1%, 68.6% and 72.5% of butyl oleate were obtained in the one-step added scenario, the stepwise-added scenario, and the simultaneous fed-batch scenario, respectively. The novel hybrid process was energy-saving, environmentally friendly and profitable, showing promise in future industrialization. [ABSTRACT FROM AUTHOR]

In this work, phytosterol ester was synthesized using Yarrowia lipolytica lipase Ylip2 that had been immobilized on inorganic support in a solvent-free system and reacted in a computer-aided water activity controlled bioreactor. The immobilization of Ylip2 on celite led to a remarkable increase in the phytosterol conversion compared to that of free lipase. An investigation of the reaction conditions were oleic acid as the fatty acid variety, 10,000 U/g substrate, and a temperature of 50 °C for phytosterol ester synthesis. Controlling of the water activity at a set point was accomplished by the introduction of dry air through the reaction medium at a digital feedback controlled flow rate. For the esterification of phytosterol ester, a low (15%) water activity resulted in a considerable improvement in phytosterol conversion (91.1%) as well as a decreased reaction time (78 h). Furthermore, Ylip2 lipase immobilized on celite retained 90% esterification activity for the synthesis of phytosterol oleate after reused 8 cycles, while free lipase was only viable for 5 batches with 90% esterification activity remained. Finally, the phytosterol oleate space time yield increased from 1.65 g/L/h with free lipase to 2.53 g/L/h with immobilized lipase. These results illustrate that the immobilized Yarrowia lipolytica lipase Ylip2 in a water activity controlled reactor has great potential for the application in phytosterol esters synthesis. [ABSTRACT FROM AUTHOR]

Highlights: [•] Lipase was absorbed on surface hydrophobic modified silk fibers. [•] Immobilized lipase and feeding methods improve synthesis of tri-TMP esters. [•] Immobilized lipas showed increase esterification activity and decrease hydrolysis activity. [•] TMP-feeding methods kept a high molar ratio of fatty acid to TMP during process. [Copyright &y& Elsevier]