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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%.
Poly(trimethylene carbonate) (PTMC), as one of the representatives of biodegradable aliphatic polycarbonates, has been found to degrade in vivo via surface erosion. This unique degradation behavior and the resulting nonacidic products make it more competitive with aliphatic polyesters (e.g., polylactide) in clinical practice. However, this surface degradation mechanism is complicated and not fully understood to date despite the findings that several reactive oxygen species and enzymes can specifically degrade PTMC in vitro. Herein, the biodegradation mechanism of PTMC was investigated by using possible degradation factors, distinct cell lines, and the inhibitors of these factors. The results demonstrate that PTMC undergoes a specific macrophage-mediated erosion. Macrophages tend to fuse into giant cells and elicit a typical inflammatory response by releasing proinflammatory cytokines. In addition, macrophages are suggested to primarily secrete enzymes (lipase specifically) to erode the PTMC bulk extracellularly as inhibiting their activity effectively prevented this eroding process. The clarification of the biodegradation mechanism in this work suggests that the degradation of PTMC highly depends on the foreign body response. Thus, it reminds the researchers to consider the effect of the microenvironment on the degradation and drug release of PTMC-based implantation devices and localized drug delivery systems.
Herein, fatty acid esters were synthesized cost-effectively from various fatty acids using reusable lipase (L) immobilized with novel porous ionic polymer (PIP) ( l –PIP). The functionalized mesoporous PIP was synthesized through Friedel–Crafts alkylation reaction of 1, 4-bis(bromomethyl) benzene in the presence of ferric chloride as catalyst, and lipase was completely immobilized with PIP at varied time, forming l –PIP–6 H , l –PIP–12 H , l –PIP–18 H , l –PIP–24 H , l –PIP–30 H , and l –PIP–36 H , which were applied in ester production. l –PIP–30 H was characterized using FT–IR, SEM, XPS, solid–state 13 C NMR, and N 2 adsorption–desorption isotherms. The conversion of oleic acid reached 88.21 % under optimized conditions (12:1 ethanol/oleic acid molar ratio after 5 h at 45 °C with 250 wt% catalyst at 300 rpm). The stability and reusability of l –PIP–30 H were demonstrated by the sustained catalytic efficiency for at least six reaction cycles. Good catalytic activity during the esterification of various free fatty acids with ethanol was observed. This cost–efficient and effective lipase–immobilized PIP catalyst may have positive economic and environmental repercussions to inspire further academic and industrial research on biodiesel.
How to rapidly and accurately screen bioactive components from complex natural products remains a major challenge. In this study, a screening platform for pancreatic lipase (PL) inhibitors was established by combining magnetic beads-based ligand fishing and high-resolution bioassay profiling. This platform was well validated using a mixture of standard compounds, i.e., (-)- epigallocatechin gallate (EGCG), luteolin and schisandrin. The dose–effect relationship of high-resolution bioassay profiling was demonstrated by the standard mixture with different concentrations for each compound. The screening of PL inhibitors from green tea extract at the concentrations of 0.2, 0.5 and 1.0 mg/mL by independent high-resolution bioassay profiling was performed. After sample pre-treatment by ligand fishing, green tea extract at the concentration of 0.2 mg/mL was specifically enriched and simplified, and consequently screened through the high-resolution bioassay profiling. As a result, three PL inhibitors, i.e., EGCG, (-)-Gallocatechin gallate (GCG) and (-)-Epicatechin gallate (ECG), were rapidly identified from the complex matrix. The established platform proved to be capable of enriching affinity binders and eliminating nonbinders in sample pre-treatment by ligand fishing, which overcame the technical challenges of high-resolution bioassay profiling in the aspects of sensitivity and resolution. Meanwhile, the high-resolution bioassay profiling possesses the ability of direct bioactive assessment, parallel structural analysis and identification after separation. The established platform allowed more accurate and rapid screening of PL inhibitors, which greatly facilitated natural product-based drug screening.Keywords:high-resolution bioassay profiling;magnetic beads-based ligand fishing;high-performance liquid chromatography;pancreatic lipase;inhibitor screening
In this study, imidazolium-based ionic liquids (ILs) were used to modify carboxymethyl cellulose-coated Fe3O4 nanoparticles with graphene oxide deposition (ILs-MCMC/GO). The prepared composites were characterized and used to immobilize lipase. The prepared biocatalyst (PPL-ILs-MCMC/GO) exhibited higher activity, which was 3.55-fold that of free lipase and 1.41-fold that of immobilized lipase without IL (PPL-MCMC/GO). After reusing 10 times, the residual activity of PPL-ILs-MCMC/GO was 91.3%, which was higher than those of PPL-MCMC/GO (83.6%) and PPL-MCMC (73.6%). In addition, using kinetic analysis, we showed that the affinity between PPL-ILs-MCMC/GO and the substrate was improved. The secondary structures of free and immobilized lipase were analyzed to explain the mechanism by which the performance of PPL-ILs-MCMC/GO was improved. The introduction of imidazole-based IL was useful in improving the microenvironment of immobilized lipase. Furthermore, magnetic supports loaded with lipase could be recovered easily.
A novel lipase gene ( lipA ) from Serratia marcescens L1 was cloned and expressed in Escherichia coli . LipA was shown to consist of 614 amino acid residues with seven residues that are different from the other nine reported lipases from S. marcescens . The activity of recombinant lipA based on a 50-mL culture scale approached 28 U/mL, which was more than that of the endogenous extracellular lipase from strain L1. The purified lipA fusion with a His-tag exhibited optimum activity at 30 °C and pH 8.0. Four effective mutants of lipase were obtained by site-directed mutation (SDM). The replacement of residues Arg552 and Gly2 in the enzyme molecule may play an important role in the catalysis characteristics and be responsible for the changes in thermostability and catalytic efficiency in the mutants. Mut G2P had the highest catalytic efficiency ( k cat / K m ) which was enhanced by 2.4-fold compared with its wild-type predecessor. These results indicated that lipA from S. marcescens could be expressed at a high level in E. coli and could be optimized by SDM, which provides a feasible basis for further study of its application.
In this study, Novozym 435-catalyzed interesterification of ethyl ferulate (EF) with phosphatidylcholine (PC) in a two-phase system consisting of an ionic liquid (IL) and toluene was optimized to prepare feruloylated lysophospholipids (FLPs). Optimum conditions for the interesterification process were found to be [Bmim][Tf2N]/toluene ratio of 1:1 (v/v), solvent volume of 4 mL, molecular sieves (4 Å) concentration of 80 mg/mL, reaction temperature of 55°C, substrate molar ratio of 5:1 (PC/EF), Novozym 435 concentration of 50 mg/mL. Under these conditions, two FLPs products (1-FLP and 2-FLP) with total conversion rate of 50.79% were obtained. Because the formation of 1-FLP was significantly higher than 2-FLP, 1-FLP was purified and characterized by LC-MS and NMR. In addition, 1-FLP showed DPPH scavenging activity comparable with those of EF and BHT. Therefore, this study provides a good method for transformation of ferulic acid to improve its solubility and promote its application as functional ingredient in the food and pharmaceutical industries.
With a dramatic increase in the incidence of obesity, it is significant to screen lipase inhibitors from traditional herbal medicines as drugs to treat obesity. Lipase inhibitors currently used to treat obesity possess the defects of toxicity and off-target effects. Thus, there is an urgent need to explore more safe, effective and targeted anti-obesity drugs from traditional herbal medicines. In this work, amino functionalized magnetic cellulose microsphere was employed as a novel support to immobilize lipase through covalent bonding. Characterizations from fourier transform infrared spectroscopy, transmission electron microscopy and X-ray diffraction demonstrated the successful preparation of the support. In comparison with the free lipase, the immobilized lipase manifested the excellent properties of a wider range for pH and temperature endurance, better pH, thermal, storage stability and reusability. Through investigating the kinetics performances of the immobilized lipase, the Michaelis-Menten constant was calculated to be 2.05 mM and its inhibition constant for orlistat was ascertained to be 40.74 μM. Eventually, the established strategy was applied to screen lipase inhibitors from 7 traditional herbal medicines and Crataegus pinnatifida Bunge was screened out due to its significant lipase inhibitory activity. To sum up, our newly established method not only developed a platform for efficiently discovering novel anti-obesity drugs from traditional herbal medicines, but also laid a solid foundation for successfully exploring undiscovered medicinal value of the traditional herbal medicines.
To improve the performance of lipase in biosynthesis of benzyl cinnamate, a new immobilized lipase by entrapping enzyme into nano-molecular cages was designed. Consequently, the entrapped lipase showed a robust immobilization, which diminished the leakage of lipase notably in use. Moreover, the entrapped lipase exhibited higher activity (57.1 U/mg) than free lipase (50.0 U/mg), demonstrating that the native conformation of lipase was not destroyed during immobilization. Compared with the adsorbed lipase (half-life 40.7 min) and free lipase (half-life 29.8 min), the entrapped lipase (half-life 85.3 min) increased the stability by about 2–3 times. Furthermore, the entrapped lipase was applied in biosynthesis of benzyl cinnamate, where it showed excellent activity and re-usability. After 7 cycles, the yield of benzyl cinnamate catalyzed by the entrapped lipase remained 70.2%, while the yield catalyzed by the adsorbed lipase was only about 10%. These results indicated that the nano-molecular cages could inhibit denaturation of lipase and maintain its activity well.
In this study, a novel lipase M5 derived from Aspergillus oryzae WZ007 was prone to exhibit high hydrolytic activity and stereoselectivity towards racemic substrate ( R , S )-ethyl 2-bromoisovalerate. ( R )-ethyl 2-bromoisovalerate was obtained by enzymatic resolution, which is the key chiral intermediate for highly efficient enantiomerically fluvalinate. The results showed that the enzymatic reaction was carried out in 120mM racemic substrate for 3 hours, the enantiomeric excess reached 98.6%, the conversion was 51.7%, and E value above 120. Therefore, the novel lipase M5 has the ability to efficiently produce ( R )-ethyl 2-bromoisovalerate, which greatly reduces the industrial production cost of the highly efficient counterpart of fluvalinate.
This paper reports the kinetics resolution of ( R , S )-4-methoxymandelic acid (4-MMA) by lipase AK-catalyzed transesterification reaction, using vinyl acetate (VA) as acyl donor in methyl tert-butyl ether (MTBE). Considering the Ping-Pong bi-bi mechanism with 4-methoxymandelic acid inhibition, the kinetic model was established. Kinetic parameters were obtained by fitting time-concentration curves for different initial 4-methoxymandelic acid concentrations. The average relative error below 3.0% indicated that the model predictions were in good agreement with the experimental data. Furthermore, the kinetic model was employed to predict the effects of enzyme loading, initial vinyl acetate concentration and reaction time on enantiomeric excess (ee s ) and conversion of substrate (c), and to optimize the conditions. The excellent results with high conversion of 4-MMA (50.2%) and large enantiomeric excess of substrate (98.6%) were achieved under the optimal conditions.
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