Showing papers on "Lipase published in 2022"
TL;DR: In this paper , the authors provide an overview about the different barriers for oral peptide and protein delivery, highlight the progress made on lipid-based nanocarriers in order to overcome them and discuss strengths and weaknesses of these delivery systems in comparison to other technologies.
72 citations
TL;DR: In this paper, the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from CALB in glutaraldehyde activated chitosan (CHI) was optimized using the Taguchi method.
Abstract: In the present communication, the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from Candida antarctica (CALB) in glutaraldehyde (GLU) activated chitosan (CHI) was optimized using the Taguchi method. Under optimized conditions (pH 9, 5 mM, 6:1 (protein load/g of support and 1 h), it was possible to reach 80.00 ± 0.01% for the immobilization yield (IY) and 46.01 ± 0.35 U/g for the activity of the derivative (AtD); in this case, load protein and ionic strength were the only statistically significant parameters and, therefore, those that most influenced the immobilization process. Furthermore, at pH 7, CALA-CALB-CHI had a half-life 2–6 times longer than the mixture of CALA and CALB for a temperature range of 50−80 °C. CALA-CALB showed the highest activity at pH 7, whereas CALA-CALB-CHI, except at pH 7, was more active than the soluble lipase mixture in the pH range (5–9), especially at pH 9. CHI, CHI-GLU, and CALA-CALB-CHI were characterized by X-ray powder diffraction (XRPD), Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscope (SEM), Thermogravimetry (TGA), and Energy Dispersive Spectroscopy (EDS), proving the immobilization of CALA and CALB in chitosan. CALA-CALB-CHI derivative evaluated in the kinetic resolution of halohydrins acetates rac-2-bromo-1-(2-chlorophenyl) ethyl acetate (2a) and rac-2-chloro-1-(2,4-dichlorophenyl) ethyl acetate (2b), to produce the corresponding halohydrins 3a-b, which are intermediates in the synthesis of the drugs chlorprelanine (antiarrhythmic) and luliconazol (antifungal), respectively. (S)-bromohydrin 3a was obtained with 79% enantiomeric excess (ee), whereas (S)-chlorohydrin 3b produced with 98% ee, conversion of 46% and E > 200. Additionally, molecular docking was performed to elucidate the hydrolysis interaction reaction between β-halohydrin acetates and lipases CALA-CALB.
52 citations
TL;DR: In this paper , the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from CALB in glutaraldehyde activated chitosan (CHI) was optimized using the Taguchi method.
Abstract: In the present communication, the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from Candida antarctica (CALB) in glutaraldehyde (GLU) activated chitosan (CHI) was optimized using the Taguchi method. Under optimized conditions (pH 9, 5 mM, 6:1 (protein load/g of support and 1 h), it was possible to reach 80.00 ± 0.01% for the immobilization yield (IY) and 46.01 ± 0.35 U/g for the activity of the derivative (AtD); in this case, load protein and ionic strength were the only statistically significant parameters and, therefore, those that most influenced the immobilization process. Furthermore, at pH 7, CALA-CALB-CHI had a half-life 2–6 times longer than the mixture of CALA and CALB for a temperature range of 50−80 °C. CALA-CALB showed the highest activity at pH 7, whereas CALA-CALB-CHI, except at pH 7, was more active than the soluble lipase mixture in the pH range (5–9), especially at pH 9. CHI, CHI-GLU, and CALA-CALB-CHI were characterized by X-ray powder diffraction (XRPD), Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscope (SEM), Thermogravimetry (TGA), and Energy Dispersive Spectroscopy (EDS), proving the immobilization of CALA and CALB in chitosan. CALA-CALB-CHI derivative evaluated in the kinetic resolution of halohydrins acetates rac-2-bromo-1-(2-chlorophenyl) ethyl acetate (2a) and rac-2-chloro-1-(2,4-dichlorophenyl) ethyl acetate (2b), to produce the corresponding halohydrins 3a-b, which are intermediates in the synthesis of the drugs chlorprelanine (antiarrhythmic) and luliconazol (antifungal), respectively. (S)-bromohydrin 3a was obtained with 79% enantiomeric excess (ee), whereas (S)-chlorohydrin 3b produced with 98% ee, conversion of 46% and E > 200. Additionally, molecular docking was performed to elucidate the hydrolysis interaction reaction between β-halohydrin acetates and lipases CALA-CALB.
52 citations
TL;DR: In this paper , a modified Fe 3 O 4 magnetic nanoparticle was used for converting waste cooking oil (WCO) to biodiesel, which achieved a high yield of 96% at a temperature of 40 °C, molar ratio of 4:1, contact time of 30 h, and catalyst dosage of 1 g.
41 citations
TL;DR: In this paper , a technical review focused on exploring the state-of-the-art of industrial applications of immobilized lipases in different reactor systems is presented, and the most common reactor configurations are discussed, as well as their advantages and disadvantages.
Abstract: Lipases are efficient biocatalysts with numerous applications in different industrial sectors, such as pharmaceutical, food, and fine chemistry industries. Enzyme immobilization further extends the applications of lipases by enhancing stability, selectivity, and half-life. However, obtaining high catalytic efficiency in reactions catalyzed by immobilized lipases requires optimization of reaction conditions (presence or absence of organic solvents, temperature, medium viscosity) and operational characteristics. This is a technical review focused on exploring the state-of-the-art of industrial applications of immobilized lipases in different reactor systems. Articles published between 2015 and 2020 were selected and analyzed to identify the major factors affecting the application of immobilized lipases, such as types of enzyme support, enzyme–support interactions (immobilization methods), substrate characteristics, and reactor configurations. The most common reactor configurations are discussed, as well as their advantages and disadvantages. In the current literature, studies on immobilized lipases and enzymatic reactors focus on developing strategies to minimize mass transfer limitations and eliminate the need for organic solvents.
37 citations
TL;DR: In this article , enzymatic hydrolysis of a biodegradable polyester by Amano Lipase PS in an aqueous (buffer) environment yielded rapidly an excessive number of microplastic particles; merely 0.1 g of poly(ε-caprolactone) film was demonstrated to yield millions of particles.
36 citations
TL;DR: In this article, five chlorogenic acid derivatives with different lipophilicities were synthesized using acylation catalyzed by lipase and the inhibitory activities and mechanisms of CA and its derivatives on α-amylase and α-glucosidase were determined.
27 citations
TL;DR: In this article , five chlorogenic acid derivatives with different lipophilicities were synthesized using acylation catalyzed by lipase and the inhibitory activities and mechanisms of CA and its derivatives on α-amylase and α-glucosidase were determined.
26 citations
TL;DR: In this article , magnetic chitosan beads were synthesized by phase-inversion method, and grafted with polydopamine (PDA) and then used for direct immobilization of Candida rugosa lipase by Schiff base reaction.
26 citations
TL;DR: In this paper, magnetic chitosan beads were synthesized by phase-inversion method, and grafted with polydopamine (PDA) and then used for direct immobilization of Candida rugosa lipase by Schiff base reaction.
26 citations
TL;DR: In this article, the authors present summaries of the results of research findings on the application of probiotics on the activities of digestive enzymes including amylase, lipase, and protease.
Abstract: Digestive enzymes are found in the digestive tract of animals which assist in the breakdown of larger food molecules into more easily absorbed particles that can then be used by the body. The ability of fish to break down a diet is highly dependent on the availability of suitable digestive enzymes which mediate specific degradation pathways and on both the physical and chemical nature of food. Probiotics are known to produce helpful enzymes that aid in digestion and protect the gastrointestinal tract (GIT) of animals. When applied appropriately, probiotics improve intestinal microbial balance which also improves digestive enzyme activities, food absorption, and decrease pathogenic issues in the GIT. They work hand-in-hand with the digestive enzymes in the GIT of animals as supplements thereby improvings nutrition. This in turn leads to higher feed efficiency and growth as well as the prevention of antinutritional factors present in the ingredients, intestinal disorders, and pre-digestion. This review seeks to present summaries of the results of research findings on the application of probiotics on the activities of digestive enzymes including amylase, lipase, and protease. Further, this review points out gaps in available literature and suggests ideas that could be explored in further investigations to better understand and enhance the activities of these digestive enzymes to increase feed and nutrient utilization and the production of aquaculture species.
TL;DR: In this article , the authors highlight the most promising techniques for producing microbial lipases and the recent applications of these lipases in dairy, oils and fats, bakery and confectionery, meat, flavors and aromas and other food industries.
Abstract: Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) are one of the largest groups of enzymes and are used in various industrial processes. Lipases of microbial origin are currently receiving increased attention for industrial application as microorganisms grow quickly and are easily genetically manipulated. Furthermore, they offer several advantages, such as catalysis of diverse reactions, high specificity, high yields, low energy consumption and reduced processing time and production costs. There is a relentless ongoing effort to optimise the production of microbial lipases for potential application in the food industry. In this context, this review highlights the most promising techniques for producing microbial lipases and the recent applications of these lipases in dairy, oils and fats, bakery and confectionery, meat, flavours and aromas and other food industries. Microbial lipases are normally obtained by fermentation, but the high costs of carbon and nitrogen sources limit the process. To overcome this problem, low-cost agro-industrial residues in the lipase production process are explored. To obtain lipases with high yields and improved characteristics, the technique of protein engineering is described as promising, and the immobilization method that allows the recycling of lipases to improve their catalytic performance is focused. Due to their catalytic properties and versatility, lipases of microbial origin are considered extremely important catalysts in the food industry, meeting the demand for tastier foods with pleasant aromas and textures. Therefore, microbial lipases are considered safe and sustainable biocatalysts. • Microbial lipases are considered promising biocatalysts for industrial application. • Advances in protein engineering and immobilization techniques increase the use of lipases. • Agro-industrial residues can be used for both production and lipase immobilization. • Lipases are of great importance in enhancing the flavor, aroma, and texture of foods. • The use of microbial lipases in industries represents a safe and promising green tool.
TL;DR: In this paper , the authors present summaries of the results of research findings on the application of probiotics on the activities of digestive enzymes including amylase, lipase, and protease.
Abstract: Digestive enzymes are found in the digestive tract of animals which assist in the breakdown of larger food molecules into more easily absorbed particles that can then be used by the body. The ability of fish to break down a diet is highly dependent on the availability of suitable digestive enzymes which mediate specific degradation pathways and on both the physical and chemical nature of food. Probiotics are known to produce helpful enzymes that aid in digestion and protect the gastrointestinal tract (GIT) of animals. When applied appropriately, probiotics improve intestinal microbial balance which also improves digestive enzyme activities, food absorption, and decrease pathogenic issues in the GIT. They work hand-in-hand with the digestive enzymes in the GIT of animals as supplements thereby improvings nutrition. This in turn leads to higher feed efficiency and growth as well as the prevention of antinutritional factors present in the ingredients, intestinal disorders, and pre-digestion. This review seeks to present summaries of the results of research findings on the application of probiotics on the activities of digestive enzymes including amylase, lipase, and protease. Further, this review points out gaps in available literature and suggests ideas that could be explored in further investigations to better understand and enhance the activities of these digestive enzymes to increase feed and nutrient utilization and the production of aquaculture species.
TL;DR: A review on the preparation of cross-linked enzyme aggregates (CLEAs) from lipases is presented in this article , where the authors focus on the cross-linking step and its problems in preparation, and solve them using an aminated feeder.
TL;DR: In this article , the decyl esterification with decanol in solvent-free systems was performed using lipase from Thermomyces lanuginosus (TLL) immobilized by physical adsorption on silica particles extracted from rice husk, an agricultural waste.
TL;DR: In this paper, the lipase from Bacillus licheniformis NCU CS-5 was immobilized onto β-cyclodextrin (CD) grafted and aminopropyl-functionalized chitosan-coated Fe3O4 magnetic nanocomposites.
TL;DR: Wang et al. as discussed by the authors showed that N. nucifera leaf extracts significantly promoted the glucose consumption of HepG2 cells, and exhibited remarkable inhibitory activities against α-glucosidase, pancreatic lipase, and COX-2.
TL;DR: A review of extremophilic lipases with emphasis on thermophilic, psychrophilic, acid and alkali resistant and active acidophilic and alkaliphilic lipase can be found in this paper .
TL;DR: In this article , cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase™ and Pronase-E for 3 and 6 hours and investigated for their potential to inhibit key lipid digesting enzymes i.e., pancreatic lipase (PL) and cholesteryl esterase (CE).
TL;DR: In this article, cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase™ (cwCA and CaCA) and Pronase-E (CWCP and CaCP) each for 3 and 6 hours, respectively, and investigated for their potential to inhibit key lipid digesting enzymes i.e., pancreatic lipase (PL) and cholesteryl esterase (CE).
TL;DR: In this paper , the analysis and modeling of the synthesis reactions of biolubricants derived from oleic acid via the use of n-octanol and isoamyl alcohol, with lipase Eversa® Transform 2.0 is presented.
TL;DR: In this article , the authors discuss and review the limited studies on the use of lipases in wastewater treatment and potential research gaps, which gives a typical understanding of the lipid waste management.
Abstract: Microbial lipases hold an unquestionable role among biocatalysts due to the broad spectrum of catalytic reactions in both aqueous and non-aqueous media. Lipases are preferred over chemical catalysts due to their high specificity and stability. The global demand of microbial lipases, especially bacterial and fungal lipases, is based on their application in various processes and industries engaged in meat, dairy, fats and oils, surfactant, tannery, cosmetics, and pharmaceuticals production. Lipases also have potential application in treatment of lipid-rich wastewater. Excessive lipids in wastewater cause serious environmental problems like clogging of sewer line, and oily layer generation on the water surface which prevents oxygen and sunlight penetration affecting the aquatic life. Existing physico-chemical treatment methods for lipid-rich wastewater are costly, non-ecofriendly and pose secondary pollution problem. Microbial lipase mediated bioremediation presents an attractive alternate approach to overcome these issues, but it is an under-explored area. Hence, this article attempts to discuss and review the limited studies on the use of lipases in wastewater treatment and potential research gaps. The review mainly focuses on the sources of lipids discharged in the wastewater and associated concerns, existing techniques for lipid removal, applicability of lipase mediated treatment for lipid containing wastewater, which gives a typical understanding of the lipid waste management. This review also summarizes the commercially available microbial lipases and need for further development for environmental application.
TL;DR: In this article , the authors focused on the relationship between content levels of phytochemicals and the biological activities of noni (Morinda Citrifolia L.) fruit extracts (NFEs) prepared with traditional solvents and deep eutectic solvent (DESs).
TL;DR: In this article , the lipase from Bacillus licheniformis NCU CS-5 was immobilized onto β-cyclodextrin (CD) grafted and aminopropyl-functionalized chitosan-coated Fe3O4 magnetic nanocomposites.
TL;DR: In this paper , the enzyme inhibition of newly synthesized sulfonate derivatives (3a-3i) for tyrosinase and pancreatic lipase was evaluated by 1H NMR, 13C NMR and HR-MS analyses.
TL;DR: In this paper , the presence of only 2 wt% designer surfactant, TPGS-750-M, assists in a 100% selective enzymatic process in which only primary alcohols participate (in a 1 : 1 ratio with carboxylic acid).
Abstract: Esterification in an aqueous micellar medium is catalyzed by a commercially available lipase in the absence of any co-factors. The presence of only 2 wt% designer surfactant, TPGS-750-M, assists in a 100% selective enzymatic process in which only primary alcohols participate (in a 1 : 1 ratio with carboxylic acid). An unexpected finding is also disclosed where the simple additive, PhCF3 (1 equiv. vs. substrate), appears to significantly extend the scope of usable acid/alcohol combinations. Taken together, several chemo- and bio-catalyzed 1-pot, multi-step reactions can now be performed in water.
TL;DR: In this paper , a straightforward synthetic strategy mediated by triethylamine to prepare the target salicylaldehyde functional group's bearing bis(sulfonate) derivatives was presented.
TL;DR: In this article , the Taguchi method was used to obtain an IY of 97.1 ± 0.10% with a mass activity (AtD) of 83.81 ± 0 0.50 U/g for the hydrolysis of p -nitrophenyl butyrate.
TL;DR: In this paper , a comprehensive study on lipase immobilization on ZIF-67, Zif-8, and HKUST-1 and their use in biodiesel production were performed.
Abstract: A comprehensive study on lipase immobilization on ZIF-67, ZIF-8, and HKUST-1 and their use in biodiesel production were performed. The highest adsorption capacity of 26.9 mg/g was achieved using ZIF-67 at 45 °C and an initial protein concentration of 0.6 mg/mL. Adsorption equilibrium data suggested that lipase adsorbed physically on ZIF-67 and ZIF-8 and chemically of HKUST-1. The data were best fitted with the Langmuir isotherm model for the three supports. Whereas, adsorption kinetics data were best fitted using Elovish’s model for ZIF-67 and ZIF-8, and the pseudo-second-order model for HKUST-1. It was also found that the process was influenced by intraparticle and film diffusion. The prepared bio-catalyst was successfully used to catalyze biodiesel production in a co-solvent medium. The ZIF-8 and ZIF-67 showed better catalytic activity, achieving 88% and 90% conversion, whereas HKUST-1 showed better reusability due to the stronger chemical adoption. In addition, diffusion-reaction kinetics of biodiesel production using adsorbed lipase on ZIF-8 have been analysed. The investigation provided an insight into adsorption pathways and probable mechanisms involved and a better understanding of their application in biodiesel production. Mathematical diffusion-reaction modeling of lipase-MOFs biocatalyst used in biodiesel production, similar to the one presented in this work, is not found in literature.
TL;DR: The enantioselective oxidative cross-coupling of secondary amines with ketones by combining the non-natural catalytic activity of lipase with electrosynthesis is described, and the reaction can be carried out in organic solvents with a broad substrate scope and good stereoselectivity.
Abstract: We describe the enantioselective oxidative cross-coupling of secondary amines with ketones by combining the non-natural catalytic activity of lipase with electrosynthesis. Various 2,2-disubstituted 3-carbonyl indoles with a stereogenic quaternary carbon center were synthesized from 2-substituted indoles in yields up to 78% with good enantio- and diastereoselectivities (up to 96:4 e.r. and > 20: 1 d.r.). This unprecedented protocol demonstrated that hydrolase catalysis is compatible with electrosynthesis, and the reaction can be carried out in organic solvents with a broad substrate scope and good stereoselectivity. This work provides insights into enzymatic electrosynthesis.