2,5-furanediformate Isooctyl is a potential new green biobased plasticizer. At present, most of the preparation methods are chemical methods, which not only have many by-products and are difficult to separate, but also cause environmental pollution. In this paper, the immobilized lipase Novozym435 was used as the catalyst to catalyze the transesterification of 2,5-furanediformate dimethyl ester and isooctyl alcohol to prepare 2,5-furanediformate isoocty in organic medium, and the reaction process was optimized. The optimal process conditions were determined by single factor experiment: in 10 mL toluene system, the additional amount of immobilized lipase Novozym435 was 0.02 g, the molar ratio of 2,5-furanediformate dimethyl ester (1 mmol) and isooctyl alcohol was 1:4, and 1 g 4Å molecular sieve was added to the reaction system, the reaction temperature was 50°C, the reaction time was 24 h, and the conversion rate of 2,5-furanediformate isoocty was 89.63%.
Sebacic esters have excellent lubricity, thermal stability, and biodegradability and therefore are widely used as aerospace lubricants, metal working oil, or engine oil. They are mainly produced by chemical synthesis which, however, may cause environmental pollution, its enzymatic synthesis represents a more environmentally friendly alternative. A few reports have described the synthesis of sebacic esters employing immobilised lipases, but these biocatalytic reactions were exclusively carried out in solvent-free systems and thus, could have been limited by slow reaction rates and high reaction temperatures due to poor enzyme dispersion, low substrate solubility, and high viscosity of the reaction mixture. The current study investigated the biosynthesis of dioctyl sebacate in toluene by Novozym 435, a commercial immobilised lipase. The reaction parameters were investigated using the single factor approach and an orthogonal array design. The optimal conditions obtained were as follows: 10 mL toluene, sebacic acid,1 mmol (202.25 mg); molar ratio of sebacic acid to 1-octanol, 1:3; Novozym 435, 0.03 g; 4 Å molecular sieves, 1.5 g; reaction temperature, 40 °C; reaction time, 30 h. A dioctyl sebacate conversion rate of 93% was achieved under these optimal conditions. In particular, the addition of molecular sieves to the reaction mixture markedly improved the product yield. The reaction temperature was low enough to make the operation easy and energy-efficient and therefore, well suited for large-scale production.
In this work, isocyanate-based strategy was developed for efficient immobilization of Candida antarctica lipase B (CALB). Of 41 commercial resins, EP109 was chosen and hydrophobized with hydroxyl-terminated polydimethylsiloxane (HTPDMS) for tert-butyl isocyanate (tBIC)-based CALB immobilization due to high loading amount and specific activity. The tBIC-based strategy exhibited shorter immobilization time, higher loading and activity than adsorption strategy by hydrophobic interaction. When compared with free CALB, EP109-HTPDMS-tBIC@CALB owned improved stability (against acid, alkali, and heat) and storability. Subsequently, EP109-HTPDMS-tBIC@CALB was employed in the bio-synthesis of 1,3-diacylglycerol in a solvent-free system with a yield of 76.31%, which was higher than commercial Novozym 435 (53.93%). EP109-HTPDMS-tBIC@CALB exhibited 76.34% of residual activity after 20 repeat uses.
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