Showing papers on "Lipase published in 2021"
TL;DR: This work will discuss how the immobilization of this enzyme through different strategies enhances its performance, that is, a properly designed immobilized Eversa biocatalyst may be more expensive, but it may have some advantages that overcome this drawback.
78 citations
TL;DR: This review intends to present some of the latest studies on the lipase A from Candida antarctica (CALA), which is among the most stable ones and has some capability to attack the sn-2 position of triglycerides.
67 citations
TL;DR: In this paper, an epoxy-activated cloisite (ECL) was prepared as a new heterofunctional carrier via a reaction between CL and epichlorohydrin and utilized for covalent immobilization of lipase from Candida rugosa.
62 citations
TL;DR: In this article, cloisite 30B (CL) was converted to tosylated cloisites (TCL) as new heterofunctional support and used to produce biodiesel from waste frying oil.
61 citations
TL;DR: This work has shown that the discovery of several new regulators such as glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), lipase maturation factor 1 (LMF1) and Sel-1 suppressor of Lin-12-like 1 (SEL1L), have completely transformed the understanding of LPL biology.
Abstract: Lipoprotein lipase (LPL) is one of the most important factors in systemic lipid partitioning and metabolism. It mediates intravascular hydrolysis of triglycerides packed in lipoproteins such as chylomicrons and very-low-density lipoprotein (VLDL). Since its initial discovery in the 1940s, its biology and pathophysiological significance have been well characterized. Nonetheless, several studies in the past decade, with recent delineation of LPL crystal structure and the discovery of several new regulators such as angiopoietin-like proteins (ANGPTLs), glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), lipase maturation factor 1 (LMF1) and Sel-1 suppressor of Lin-12-like 1 (SEL1L), have completely transformed our understanding of LPL biology.
57 citations
TL;DR: A low-cost liquid lipase from genetically modified Aspergillus oryzae (Eversa® Transform 2.0) was used in this study for biodiesel production as discussed by the authors.
57 citations
TL;DR: An overview on extremophilic microbial lipases, their diversity, structure, and classification can be found in this paper, where an overview on novel lipases which have been detected through analysis of the genomic dark matter (metagenome) has also been presented.
55 citations
TL;DR: In this paper, the authors highlight several aspects of lipase immobilization on the surface of chitosan support, including physical adsorption to covalent bonding and cross-linking with their benefits and drawbacks.
52 citations
TL;DR: Compared with free lipase, the MhNF exhibited high tolerance against methanol and storage stability, and could be easily recycled by magnet without obvious activity loss, indicating excellent reusability.
47 citations
TL;DR: TIR signaling promotes the interactions between lipase-like proteins EDS1/PAD4 and ADR1-L1 immune receptor, and oligomerization of ADR2-L3, leading to TIR signaling-dependent cell reprograming in mice with high TIR sensitivity.
Abstract: TIR signaling promotes the interactions between lipase-like proteins EDS1/PAD4 and ADR1-L1 immune receptor, and oligomerization of ADR1-L1.
47 citations
TL;DR: In this paper, the polydimethylsiloxane (PDMS) was used to immobilize lipase from Aspergillus oryzae (AOL) for biodiesel production.
TL;DR: In this paper, a review summarizes studies about structure, mechanistic approach of pancreatic lipase enzyme while emphasizing on the various synthetic pancreatIC lipase inhibitors with their structure activity relationship (SAR).
TL;DR: The unique structural and functional properties of a large number of polymers and nanomaterials as robust support matrices for lipase immobilization are outlined and the applications of immobilized lipases in different industries, such as biodiesel production, polymer synthesis, additives, detergent, textile, and food industry are discussed.
TL;DR: In this paper, the mesoporous silica magnetic nanoparticles (MNPs) were used for the immobilization of a rhizopus oryzae lipase (ROL) that was used for biodiesel synthesis.
TL;DR: In this paper, the authors co-immobilized Candida antarctica lipase B (CALB) and Thermomyces lanuginose lipase (TLL) on epoxy functionalized silica gel via an isocyanide-based multicomponent reaction.
TL;DR: The integration of GO-based biocatalyst assisted transesterification and multi-staged membrane system for downstream enrichment of fatty acid ethyl ester culminates in the development of a cost-effective, energy-intensive and eco-friendly system which represents a sustainable biofuel production process.
TL;DR: The fermentation conditions of Aspergillus Niger were optimized by single factor and response surface design, the enzymatic properties of the crude enzyme were studied and found that the optimum fermentation medium was soluble starch 4, (NH4)2SO4 0.1%, K2HPO4 0, MgSO4·7H2O 0, peptone 3, olive oil 1, and initial pH 7.0.
Abstract: To obtain the optimum fermentation medium and circumstances for extracellular lipase construction (as an important biocatalyst and promising industrial enzyme) by Aspergillus Niger, the fermentation conditions of Aspergillus Niger were optimized by single factor and response surface design, the enzymatic properties of the crude enzyme were studied. The results displayed that the optimum fermentation medium was soluble starch 4%, (NH4)2SO4 0.1%, K2HPO4 0.1%, MgSO4·7H2O 0.05%, peptone 3%, olive oil 1.05% and initial pH 7. The optimal fermentation conditions were 30℃, the sample size was 26 mL/250 mL and the shaking speed was 213 r/min. The optimized lipase activity was 1.55 U/mL, which was 7.75 times of the pre-optimized lipase. It was found that when the pH value of lipase was 7.0, the activity of lipase reached its maximum value of 79.3±6.82%. When pH value was between 6.0 and 8.0, the activity of lipase could be kept above 60% and the stability was good. At the same time, through temperature stability of lipase, found that the lipase was stable at 25℃- 35℃, its activity could reach more than 70%. When activity of enzyme reaches to maximum 107.6±9.57%, the temperature was 30℃.
TL;DR: In this article, the regenerated lipase catalyst was found to have better reusability up to the fourth cycle and the produced biodiesel was within the ASTM D6751 standard.
Abstract: In this study, process intensification was carried out using lipase catalyzed transesterification of waste cottonseed oil (WCSO) with ethanol in the presence of ultrasonication. A maximum conversion of 98.7% was observed for ultrasound assisted transesterification. The optimum process conditions were ethanol to oil molar ratio of 4.5:1, a reaction temperature of 45°C, enzyme loading of 5 wt%, a reaction time of 6 h, ultrasonic amplitude of 40% and the duty cycle of 15 s ON and 15 s OFF. The influence of ultrasound makes the process efficient because of an effective reduction in reaction time to 6 h with the least catalyst dosage and power consumption. Reusability tests of the catalyst were conducted after separating the immobilized Rhizopus oryzae lipase. The regenerated lipase catalyst was found to have better reusability up to the fourth cycle and the produced biodiesel was within the ASTM D6751 standard. Furthermore, the ultrasound assisted process under mild operating conditions did not affect the immobilized enzyme. It was clearly observed that ultrasonication is faster and effective for biodiesel conversion using the immobilized lipase catalyzed transesterification reactions.
TL;DR: The lubricant properties of the products were characterized, showing that it can be an environmentally friendly alternative for petrol lubricants.
TL;DR: Clinical studies revealed dysregulations of HSL expression and activity in disorders, such as lipodystrophy, obesity, type 2 diabetes and cancer-associated cachexia, which positions HSL as a pharmacological target for the treatment of metabolic complications.
TL;DR: The potent lipase producing strain of actinomycete was optimized for pH, temperature, inoculum size, carbon and nitrogen sources and Nocardiopsis alba was selected as the best lipase producer.
Abstract: Actinomycete strains from cottonseed soap-stock (a dark gelatinous waste from oil refinery) were obtained. Cultures were analyzed for the enzyme lipase, protease and cellulase production using plate assay(s). Best lipolytic isolates were further quantitatively analyzed for lipase production, using substrate p-nitrophenyl palmitate (p-NPP). Cultures were characterized by morphological and molecular studies. The potent lipase producing strain of actinomycete was optimized for pH, temperature, inoculum size, carbon and nitrogen sources. Further, the lipolytic strain of actinomycete was grown on synthetic media and growth factors were optimized by RSM (Response Surface Methodology) for maximum production of lipase. Total 49 cultures were obtained from enriched soap-stock samples; among them 7 isolates were strains of actinomycete. Potent actinomycete strains were identified as Nocardiopsis alba, Streptomyces leeuwenhoekii, Streptomyces caelestis, Streptomyces werraensis and Streptomyces sclerotialus. Based on quantitative lipase production study, Nocardiopsis alba was selected as the best lipase producer. Optimized results of process parameter studies for lipase production by Nocardiopsis alba were: 5mL inoculum size, temperature 40 ∘ C, shaking at 130 rpm, pH 8.0 and cottonseed oil as the best carbon source. Cottonseed oil, K2HPO4 and cellulose were noted as main factors as optimized by Central Composite Design (CCD), where the culture showed highest (65.78 U/mL/min) lipase production. Findings of the research would offer potential environmental benefits along with socio-economic benefits if implemented suitably.
TL;DR: In this article, Eversa® Transform 2.0 was used to produce trimethylolpropane triesters (TMPTEs) using free lipase extract from Candida rugosa (CRL).
Abstract: Trimethylolpropane triesters – TMPTEs (biolubricants) have been produced through enzymatic hydroesterification of refined soybean (RSO) or used soybean cooking (USCO) oils. In the first step, enzymatic hydrolysis has been performed using a crude free lipase extract from Candida rugosa (CRL) to produce free fatty acids (FFAs). Complete hydrolysis of the oils was achieved after 3 h of reaction. Then, CRL and the lipases from Thermomyces lanuginosus (Lipolase® 100L and Eversa® Transform 2.0) and Pseudomonas fluorescens (Amano AK) were immobilized via interfacial activation on polystyrene-divinylbenzene (PSty-DVB) beads. High enzyme loaded biocatalysts (immobilization yield above 85%) were obtained for all lipase preparations using an initial protein loading of 40 mg g−1. Then, free lipases (liquid or powder forms) or immobilized biocatalysts were employed to produce TMPTEs via enzymatic esterification of the produced FFAs with trimethylolpropane (TMP) in eco-friendly processes (solvent-free systems). The new heterogeneous biocatalyst prepared in this study (immobilized Eversa® Transform 2.0) was the most active biocatalyst in TMPTEs production and maximum OH conversion of ≈97% using both FFA sources was achieved after 4 h of reaction conducted in open reactors at 55 °C, TMP:FFA ratio of 1:3.25, 240 rpm, and 15% of mass of biocatalyst per mass of starting materials. Under similar conditions, OH conversion of ∼25% after 5 h of reaction was obtained using Novozym® 435 as biocatalyst. Immobilized Eversa® Transform 2.0 retained above 90% of its original activity after 13 consecutive reaction cycles. The produced TMPTEs presented good cold temperature properties (pour point values between −11 and −9 °C).
TL;DR: In this article, a low-cost feedstock, waste phoenix seed oil (PSO) with a high free fatty acid (FFA) content (30.1 − 0.6%), consisting of the main fatty acid, linoleic acid, oleic acid (22.2%), and palmitic acid(17.4%), was developed as a new feedstock to prepare biodiesel.
Abstract: Biodiesel is a typical renewable and green energy, that is usually produced by the transesterification of edible vegetable oils. However, the cost of edible vegetable oils as feedstock accounts for 60%–80% of the total cost of biodiesel production. To overcome these issues, in this work, a low-cost feedstock, waste phoenix seed oil (PSO) with a high free fatty acid (FFA) content (30.1 ± 0.6%), consisting of the main fatty acid, linoleic acid (30.2%), oleic acid (22.2%), and palmitic acid (17.4%), was developed as a new feedstock to prepare biodiesel. A novel one-step method including simultaneous esterification of FFAs and transesterification of the PSO to prepare biodiesel was developed. Free lipase was used as catalyst. The influences of the reaction parameters were explored and optimized by response surface methodology. The results showed that the free lipase Lipozyme TL100L from Thermomyces lanuginosus can simultaneously catalyze esterification and transesterification. Under the optimum conditions (enzyme load 9.7%, reaction time 6.9 h, reaction temperature 31 °C and substrate ratio (methanol/PSO) 4.3: 1 (mol/mol)), the maximum biodiesel yield (93.8 ± 0.5%) was achieved. The activation energy from biodiesel preparation using PSO with a high FFA content was 39.7 kJ/mol. Furthermore, the kinetic values for K'm and Vmax were 0.18 mol/L and 0.043 mol/(L·min), respectively. The reaction mechanism of the simultaneous esterification and transesterification was also proposed. These results indicate that PSO with a high FFA content can be used as a potential feedstock for biodiesel production.
TL;DR: The results suggested that PPL@ZIF-90 can be used as a potential effective biocatalyst for synthesis of isoamyl butyrate.
TL;DR: In this article, an extracellular lipase was partially purified from the culture broth of Rhizopus oryzae R1 isolate to apparent homogeneity using ammonium sulfate precipitation followed by desalting via dialysis.
TL;DR: In this article, a mild and quick one-pot strategy was used to achieve the successful encapsulation of lipase (CRL) and Fe3O4 nanoparticle into ZIF-8 to form CRL/MNP@ZIF-6 with 88.4 % immobilization yield.
TL;DR: In this work, the combination of different lipases was employed for the production of biodiesel, using the Free Fatty Acids from Residual Chicken Oil (RCO) as a substrate and the Taguchi method was used to optimize the esterification reaction parameters.
Abstract: In this work, the combination of different lipases was employed for the production of biodiesel, using the Free Fatty Acids (FFAs) from Residual Chicken Oil (RCO) as a substrate. As biocatalysts, lipases A and B from Candida antarctica (CALA and CALB, respectively) and lipase from Rhizomucor miehei (RML) were used in different combinations; as a result, the best lipase cocktail was composed of 67% CALB and 33% RML, which was used to optimize the esterification reaction parameters (molar ratio (FFAs/ ethyl alcohol), biocatalyst content, temperature and time) by the Taguchi method. Under optimized conditions (1:5, 15% of lipase cocktail, 30 °C and 3 h), it was possible to achieve 89.95 ± 0.3% of conversion.
TL;DR: In this paper, a low-cost liquid lipase (Eversa® Transform 2.0) produced from a genetically modified Aspergillus oryzae was determined to be 9600 IU mL−1.
TL;DR: In this article, the authors characterized the involvement of two major metabolic lipases, adipose triglyceride lipase (ATGL) and hormone-sensitive lipase(HSL), in TAG estolide and FAHFA degradation.
Abstract: Branched esters of palmitic acid and hydroxy stearic acid are antiinflammatory and antidiabetic lipokines that belong to a family of fatty acid (FA) esters of hydroxy fatty acids (HFAs) called FAHFAs. FAHFAs themselves belong to oligomeric FA esters, known as estolides. Glycerol-bound FAHFAs in triacylglycerols (TAGs), named TAG estolides, serve as metabolite reservoir of FAHFAs mobilized by lipases upon demand. Here, we characterized the involvement of two major metabolic lipases, adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL), in TAG estolide and FAHFA degradation. We synthesized a library of 20 TAG estolide isomers with FAHFAs varying in branching position, chain length, saturation grade, and position on the glycerol backbone and developed an in silico mass spectra library of all predicted catabolic intermediates. We found that ATGL alone or coactivated by comparative gene identification-58 efficiently liberated FAHFAs from TAG estolides with a preference for more compact substrates where the estolide branching point is located near the glycerol ester bond. ATGL was further involved in transesterification and remodeling reactions leading to the formation of TAG estolides with alternative acyl compositions. HSL represented a much more potent estolide bond hydrolase for both TAG estolides and free FAHFAs. FAHFA and TAG estolide accumulation in white adipose tissue of mice lacking HSL argued for a functional role of HSL in estolide catabolism in vivo. Our data show that ATGL and HSL participate in the metabolism of estolides and TAG estolides in distinct manners and are likely to affect the lipokine function of FAHFAs.
TL;DR: In this paper, the interaction between lipase and quercetin 3-rhamnoside was studied by fluorescence spectroscopy, enzyme kinetics, and molecular dynamics simulation.