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Abstract: A novel lipase-catalyzed synthesis of aliphatic polyesters has been achieved successfully by using Candida sp.99-125 with diethyl sebacate and 1,4-butanediol as starting substrates in absence of organic solvents. The lipase from Candida sp.99-125 was employed for the first time to catalyze synthesis of poly(butylene sebacate) and showed high catalytic activity for bulkpolymerization under mild reaction conditions. The eco-friendly processes, without any environmental pollution, avoided both phase separation of the reactants and the use of toxic solvents effectively. The polycondensation reactions were performed in two stages: first stage reaction under atmospheric pressure to convert the monomers to oligomers followed by second stage reaction under vacuum process, with a highest molecular weight of 15,800 obtained in molar ratio of 1:1 at 70°C. The corresponding polyesters determined by thermogravimetric analysis (TGA) were much thermally stable up to 300°C. Differential scanning calorimetry (DSC) and wide-angle X-ray diffraction (WAXS) analysis demonstrated the polymers had a strong ability to crystallize with the degree of crystallinity up to 66%. [Copyright &y& Elsevier]

Abstract: Nonwoven fabrics of polypropylene (PP), polyethylene terephthalate (PET) and viscose fiber were used as novel and inexpensive support membranes for the immobilization of lipase. The use of a co-solvent during the immobilization process improved the activity of the coupled protein and the operational stability of PP and PET membranes. Covalent methods of immobilization caused the support membranes to become fragile and the lipase was easily deactivated. A hydrophobic treatment improved the protein-coupled content of silk cotton, viscose and PET surfaces more than threefold. Viscose prepared with the hydrophobic treatment could be reused up to 44 times and retained a static water contact angle of 131.8°. The initial rate of esterification remained high even when the amount of added water was increased to 10%. In a model application reaction of oleic acid and ethanol with 8% (v/v) added water, the acid conversion rate of post-hydrophobic treated immobilized lipase improved by at least 10% in each of five batches. These results suggest that a hydrophobic surface results in a lower amount of adsorbed water on the support membrane and provides a more suitable microenvironment for the enzymes. Nonwoven viscose could be a potential enzyme immobilization matrix for industrial processes. [Copyright &y& Elsevier]

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]

Glycerol waste from the biodiesel production can be used as a carbon source in the production of 1,3-propanediol (1,3-PD) through microbial fermentation. However, downstream processing is a major bottleneck that restricts its biological production. Here, we investigated an environmentally-friendly method to enzymatically separate 1,3-PD. The transformation of 1,3-PD to an ester was achieved by exploiting the esterification reaction with fatty acids under lipase catalysis. The reaction efficiency was optimized using different poly-alcohols that were existed in the fermentation broth reacted with a fatty acid. Whereas the 1,3-PD conversion reached 62%, only a 0.06% and 0.08% conversion was reached for 2,3-butanediol and glycerol, illustrating the former’s more efficient separation. The recovery efficiency of 1,3-PD was 96%. Finally, 1,3-PD was obtained by lipase-directed ester hydrolysis. Taken together, the bio-catalyzed separation process presented here is a novel and promising method for recovering 1,3-PD. [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]

We have developed an improved and effective method to immobilize Yarrowia lipolytica lipase Lip2 (YLIP2) on an epoxy poly-(glycidylmethacrylate-triallyisocyanurate-ethyleneglycoldimethacrylate) (P GMA-TAIC-EGDMA ) support structure with or without amine or/and protein modifications. Our results show that there is an increase in the activity of the immobilized lipase on n-butylamine (BA) modified support (420 U/g support) and the biocompatible gelatin modified support (600 U/g support) when compared to the support without modification (240 U/g support). To further study the influences of BA and gelatin modification on the activity of the immobilized lipase, gelatin and BA were concurrently used to decorate the support structure. Lipase immobilized on 2% BA/gelatin (1:1) modified support obtained the highest activity (1180 U/g support), which was five-fold higher than that on a native support structure. These results suggest that the activity of a support-immobilized lipase depends on the support surface properties and a moderate support surface micro-environment was crucial for elevated activity. Collectively, these data show that a combined gelatin and BA modification regulates the support surface more suitable for immobilizing YLIP2. [ABSTRACT FROM AUTHOR]

ExtracellularYarrowia lipolyticalipase Lip2 (YLIP2) demonstrated an (R)-enantiopreference for efficient resolution of (R,S)-1-phenylethanol by solvent engineering with different kinds of binary solvent. The enantioselectivity was significantly improved by the addition of 1, 4-dioxane. The reaction parameters including co-solvent concentration, reaction temperature, and the reaction time were optimized. When the reaction was carried out with n-hexane in the presence of 0.8% 1,4-dioxane at 50°C for 72 h, the enantiomeric excess of product markedly increased to 99.1% from 66% in pure n-hexane; the enantiomeric ratio was higher than 200, which was 500-fold compared with that in pure n-hexane. The results indicated that it is very important to design the proper co-solvents, especially to create appropriate micro-environment for YLIP2 for catalyzing the resolution of (R,S)-1-phenylethanol. [ABSTRACT FROM AUTHOR]

An enzymatic process using a packed bed bioreactor with recirculation was developed for the scale-up synthesis of 2-ethylhexyl palmitate with a lipase fromCandidasp. 99–125 immobilized on a fabric membrane by natural attachment to the membrane surface. Esterification was effectively performed by circulating the reaction mixture between a packed bed column and a substrate container. A maximum esterification yield of 98% was obtained. Adding molecular sieves and drying the immobilized lipase both decreased the water content at the reactor outlet and around the enzyme, which led to an increase in the rate of esterification. The long-term stability of the reactor was tested by continuing the reaction for 30 batches (over 300 h) with an average esterification yield of about 95%. This immobilized lipase bioreactor is scalable and is thus suitable for industrial production of 2-ethylhexyl palmitate. [ABSTRACT FROM AUTHOR]

Finishing of silk fabric was achieved by using amino-functional polydimethylsiloxane (PDMS) and lipase from Candida sp. 99-125 was immobilized on the treated silk fabrics. Hydrophobic fabrics were obtained by dipping the native fabric in 0.125-0.25% (w/v) PDMS solution and dried at 70°C. The direct adsorption on PDMS-treated fabric was verified to be a better strategy for lipase immobilization than that by covalent binding. Compared to unfinished fabrics, the hydrolytic activity of immobilized enzyme on the finished fabric was improved by 1.6 times. Moreover, the activity of immobilized enzymes on hydrophobic fabrics was significantly improved in different concentrations of strong polar solvents such as methanol and ethanol, and in common organic solvents with different octanol-water partition coefficients (LogP). Enzymatic activity and stability in 15% water content system (added water accounted for the total reaction mixtures, v/v) showed more than 30% improvement in each batch. The amino-silicone finished fabric surface was investigated by scanning electron microscopy and X-ray photoelectron spectroscopy. The hydrophobic fabric immobilized enzyme could be recycled for more than 80 times with no significant decrease in esterification activity. PDMS-treated woven silk fabrics could be a potential support for lipase immobilization in catalytic esterification processes. [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]

Methanol is regularly used as a substratefor biodiesel synthesis.Excess methanol can however inhibit the lipase activity. In the presentwork, the activity and conformational changes of Yarrowialipolyticalipase (LIP2) at different concentrationsof methanol were investigated by measuring fluorescence, UV–visspectra, and molecular dynamics simulations. The lipase tended toexpand at higher concentrations of methanol, and the methanol moleculeswere able to enter into the LIP2, leading to microenvironment changesaround the aromatic amino acids. More hydrophobic groups were exposedto the solvents at high methanol concentrations, and the originalhydrophobic interaction in the protein was destroyed, thus resultingin the tertiary structure change of the lipase. [ABSTRACT FROM AUTHOR]

Highlights: [•] A simple, efficient immobilization protocol on polyurethane foam was developed. [•] Polyethyleneimine (PEI) was used to regulate the micro-environment. [•] Immobilized lipase exhibited a long operational stability in esterification system. [Copyright &y& Elsevier]

Abstract: Diesters and diols were successfully converted into aliphatic polyesters by enzymatic lipase Candida sp.99-125 catalysis, with β-cyclodextrin acting as supporting architecture (in a similar way as chaperone proteins). No organic solvents were used. The polytransesterification was a much greener process, being solvent-free and without metal residues. Lipase Candida sp.99-125 showed a high catalytic activity for bulkpolymerization of diesters and diols with various numbers of methylene groups in their chains. β-Cyclodextrin encircled the linear polymer chain and maintained the chain in a proper configuration to avoid its coagulation. Lipase initiated the polymerization and β-cyclodextrin threaded onto the polymer chain to control the structure for producing high molecular weight polyesters. From a combination of diesters and diols, polyesters with a high molecular weight of 62,100Da were obtained at 70°C. The corresponding polyesters showed an excellent thermal stability till 350°C and had a strong ability to crystallize with up to 72% crystallinity, contributing to their high storage modulus. [Copyright &y& Elsevier]