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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications o...
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... catalyze a wide array of reactions 21 and they are also ubiquitous. In general, lipases can be classified based on their specificities as well as sources as shown in Figure 1. A deeper insight of the availability, functionality and wide applicability of lipases can be realized through the classification of lipases as illustrated in the following sec- tions. ...
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Free fatty
acid, which is an important intermediate product in the oleochemical industry,
can be produced by hydrolysis of oil using lipase enzymes. This process is more
economical and less energy consuming than the conventional process, i.e.
noncatalytic thermal hydrolysis. While lipase from microorganisms requires a
complex separation step, that...
Citations
... These lipases (triacylglycerol hydrolases, EC 3.1.1.3) can catalyze the hydrolysis of triglycerides, releasing free fatty acids, diacylglycerols, monoacylglycerols, and glycerol [6]. ...
Omega-3 fatty acids, such as eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), offer numerous health benefits. Enriching these fatty acids in fish oil using cost-effective methods, like lipase application, has been studied extensively. This research aimed to investigate F. solani as a potential lipase producer and compare its efficacy in enhancing polyunsaturated omega-3 fatty acids with commercial lipases. Submerged fermentation with coconut oil yielded Lipase F2, showing remarkable activity (215.68 U/mL). Lipase F2 remained stable at pH 8.0 (activity: 93.84 U/mL) and active between 35 and 70 °C, with optimal stability at 35 °C. It exhibited resistance to various surfactants and ions, showing no cytotoxic activity in vitro, crucial for its application in the food and pharmaceutical industries. Lipase F2 efficiently enriched EPA and DHA in fish oil, reaching 22.1 mol% DHA and 23.8 mol% EPA. These results underscore the economic viability and efficacy of Lipase F2, a partially purified enzyme obtained using low-cost techniques, demonstrating remarkable stability and resistance to diverse conditions. Its performance was comparable to highly pure commercially available enzymes in omega-3 production. These findings highlight the potential of F. solani as a promising lipase source, offering opportunities for economically producing omega-3 and advancing biotechnological applications in the food and supplements industry.
... Lipazy, ze względu na dużą różnorodność i wydajność katalizowanych reakcji uważane są za jedne z najważniejszych biokatalizatorów wykorzystywanych w przemyśle [8,13,53,54]. Aplikacyjny sukces tych enzymów wiąże się nie tylko z szeroką specyficznością substratową, ale też z wysoką stabilnością enzymu w szerokim spektrum temperatury czy pH, oraz brakiem konieczności stosowania kofaktorów reakcji [55]. Zastosowanie w biotechnologii znalazły lipazy mikrobiologiczne, zwierzęce i roślinne, aczkolwiek lipazy mikrobiologiczne są stosowane najczęściej. ...
... Około połowa lipaz komercyjnych produkowana jest z drożdży i grzybów nitkowatych [56]. Przyczyną powszechności stosowania lipaz mikrobiologicznych jest szybki wzrost kultur i niskie koszty hodowli, oraz wysoka stabilność i szeroka specyficzność substratowa tych enzymów [8,13,53,54,57]. Niemniej jednak warto zaznaczyć, że koszty pozyskiwania i przetwarzania lipaz roślinnych są coraz niższe i stają się konkurencyjne w odniesieniu do lipaz mikrobiologicznych [9,54]. ...
... Przyczyną powszechności stosowania lipaz mikrobiologicznych jest szybki wzrost kultur i niskie koszty hodowli, oraz wysoka stabilność i szeroka specyficzność substratowa tych enzymów [8,13,53,54,57]. Niemniej jednak warto zaznaczyć, że koszty pozyskiwania i przetwarzania lipaz roślinnych są coraz niższe i stają się konkurencyjne w odniesieniu do lipaz mikrobiologicznych [9,54]. W porównaniu do lipaz mikrobiologicznych, lipazy roślinne mogą być ekstrahowane ze źródeł nisko kosztowych, takich jak biomasa [56] i mogą być używane bezpośrednio po pozyskaniu i częściowym tylko oczyszczeniu [58]. ...
Lipases are enzymes commonly found in microorganisms, fungi, plants and animals. Their main function in cell metabolism is the hydrolysis (lipolysis) of ester bonds between fatty acids and glycerol in mono-, di- and triacylglycerols. In plants, lipases play an important role in ontogeny, participating in both vegetative development and generative stages. These enzymes may also be a component of plant responses to biotic and abiotic stresses. Based on the similarity of the amino acid sequence and vacuolar localization of some plant lipases to yeast Atg15, we present a hypothesis about the participation of lipases in autophagy (precisely, in the degradation of the autophagic body) in plants. Despite the narrow substrate specificity and the type of reactions catalysed in cells, lipases find numerous biotechnological applications. The physicochemical features of lipases, which determine, for example, wide substrate specificity in vitro or high stability in a wide range of pH and temperature, make these enzymes the subject of applied research, and plant lipases show an increasing potential in this area of science and industry.
... Fungal lipases have a variety of industrial uses, including in the manufacture of detergents, cosmetics, and medicines as well as in the food, textile, and manufacturing sectors. Additionally, lipases may break down polyurethane and fatty waste (Sarmah et al. 2018). ...
Microplastic pollution has gained much more attention in the research field as it has created a greater threat to biota worldwide. A major source of these microplastic materials is derived from mismanaged wastes in the environment. Current approaches like recycling and incineration approaches do not provide a sustainable solution to tackle the huge amount of microplastic pollution. There is an urgent need to develop innovative approaches for their disposal. Fungal-based biodegradation (mycoremediation) of microplastic is primed focused since last decades. Fungi are diverse eukaryotic groups that can degrade microplastic by using it as a food source under the influence of temperature and pH. Fungi are paling crucial role in degradation by securing varieties of enzymes like cutinase, lipases, proteases, cellulolytic enzymes, and also pro-oxidant ions. The action of these enzymes on microplastic and enhance the hydrophilicity and in turn convert complex molecule into simple molecule which is an low molecular weight compound. Even though mycodegradation can be a promising tool for microplastic removal, it is highly demanding to finalize different parameters and determination of optimum conditions for successful degradation of plastics. This chapter summarizes different sources of microplastics along with their types. Furthermore, it focuses on different fungal isolates responsible for the biodegradation of microplastics, various modes of it, and different enzymes responsible for degradation. In addition, microplastic degradation is affected by varieties of biological and physiological factors. Therefore, different environmental factors like pH and temperature affecting microplastic degradation and degradation effects are discussed. Further, enhancing factors of microplastic degradation are briefly discussed. Finally, we have focused on future research directions and prospective for controlling microplastic pollution by mycodegradation. This chapter encompasses summary of the mycodegradation of microplastic degradation and a bunch of information for future innovative research to control microplastic pollution worldwide.
... Lipases (triacylglycerol acyl hydrolases E.C. 3.1.1.3), for example, are biocatalysts able of catalyzing a wide range of reactions, with high specificity for the substrate of interest [15,16]. The high versatility of lipases is recognized as the most important group of biocatalysts in biotechnology. ...
Molecular docking is an important computational analysis widely used to predict the interaction of enzymes with several starting materials for developing new valuable products from several starting materials, including oils and fats. In the present study, molecular docking was used as an efficient in silico screening tool to select biocatalysts with the highest catalytic performance in butyl esters production in a solvent-free system, an eco-friendly approach, via direct esterification of free fatty acids from Licuri oil with butanol. For such purpose, three commercial lipase preparations were used to perform molecular docking studies such as Burkholderia cepacia (BCL), Porcine pancreatic (PPL), and Candida rugosa (CRL). Concurrently, the results obtained in BCL and CRL are the most efficient in the esterification process due to their higher preference for catalyzing the esterification of lauric acid, the main fatty acid found in the licuri oil composition. Meanwhile, PPL was the least efficient because it preferentially interacts with minor fatty acids. Molecular docking with the experimental results indicated the better performance in the synthesis of esters was BCL. In conclusion, experimental results analysis shows higher enzymatic productivity in esterification reactions of 1294.83 μmol/h.mg, while the CRL and PPL demonstrated the lowest performance (189.87 μmol / h.mg and 23.96 μmol / h.mg, respectively). Thus, molecular docking and experimental results indicate that BCL is a more efficient lipase to produce fatty acids and esters from licuri oil with a high content of lauric acid. In addition, this study also demonstrates the application of molecular docking as an important tool for lipase screening to achieve more sustainable production of butyl esters with a view synthesis of biolubricants.
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... Our S. aureus strains did not show a reaction to "negative" enzymes; however, they showed high resistance to methicillin and other tested antibiotics (Simonová et al. 2007). Although staphylococci are also known as producers of microbial lipases and esterases for their use as catalysts in the cosmetic, medicinal, food, or detergent industries (Sarmah et al. 2018), our isolates possessed only slight lipase and higher, but still moderate esterase production. Determination of the prevalence of phenotypic virulence factors among the tested MRSA revealed that the majority of ...
There is a major problem with the rising occurrence of highly virulent and multiply-resistant strains, including methicillin-resistant Staphylococcus aureus (MRSA), because of their difficult treatment. This study aimed to evaluate the antibacterial and antibiofilm effect of new enterocins (Ent) against potential pathogenic MRSA strains isolated from rabbits. Staphylococci were identified with PCR and screened for methicillin/oxacillin/cefoxitin resistance (MR) using the disk diffusion method and the PBP2’ Latex Agglutination Test Kit. Enzyme production, hemolysis, DNase activity, slime production, and biofilm formation were tested in MRSA strains. The susceptibility of MRSA to eight partially-purified enterocins (Ent) produced by E. faecium and E. durans strains was checked using agar spot tests. The antibiofilm activity of Ents was tested using a quantitative plate assay. Out of 14 MRSA, PBP testing confirmed MR in 8 strains. The majority of MRSA showed DNase activity and β-hemolysis. Slime production and moderate biofilm formation were observed in all strains. MRSA were susceptible to tested Ents (100–12,800 AU/mL; except Ent4231). The antibiofilm effect of Ents (except Ent4231) was noted in the high range (64.9–97.0%). These results indicate that enterocins offer a promising option for the prevention and treatment of bacterial infections caused by biofilm-forming MRSA.
... When using NaOH as an alkali catalyst, researchers have achieved a greater lipid yield with a weight conversion rate of 55 % compared to 48 % when using H 2 SO 4 [138]. Due to their adaptability, high catalytic activity, substrate specificity, and region selectivity under standard conditions, lipases have a significant advantage over acid and alkali catalysts [139]. A few lipases are unable to hydrolyze ester bonds in ancillary positions, whereas another group of enzymes can hydrolyze both primary as well as secondary esters. ...
... catalyze the hydrolysis of triacylglycerols to glycerol and long-chain fatty acids 20 . These enzymes play essential roles as biocatalysts for biotechnological applications such as in detergent, dairy, food, fat and oil, cosmetics, and pharmaceutical industries 21,22 . Lipases appear to offer an environmentally friendly alternative to decreasing the usage of commonly employed chemicals 23 . ...
Lipopeptides, derived from microorganisms, are promising surface-active compounds known as biosurfactants. However, the high production costs of biosurfactants, associated with expensive culture media and purification processes, limit widespread industrial application. To enhance the sustainability of biosurfactant production, researchers have explored cost-effective substrates. In this study, crude glycerol was evaluated as a promising and economical carbon source in viscosinamide production by Pseudomonas fluorescens DR54. Optimization studies using the Box − Behnken design and response surface methodology were performed. Optimal conditions for viscosinamide production including glycerol 70.8 g/L, leucine 2.7 g/L, phosphate 3.7 g/L, and urea 9.3 g/L were identified. Yield of viscosinamide production, performed under optimal conditions, reached 7.18 ± 0.17 g/L. Preliminary characterization of viscosinamide involved the measurement of surface tension. The critical micelle concentration of lipopeptide was determined to be 5 mg/L. Furthermore, the interactions between the viscosinamide and lipase from Candida rugosa (CRL) were investigated by evaluating the impact of viscosinamide on lipase activity and measuring circular dichroism. It was observed that the α-helicity of CRL increases with increasing viscosinamide concentration, while the random coil structure decreases.
... Lipase (EC.3.1.1.3) is a highly efficient biocatalyst that has been widely used in the modification of fats and oils, synthesis of pharmaceutical intermediates, food processing, and biodiesel production [1][2][3][4][5]. Especially for the industrial production of biodiesel, the bio-enzyme-catalyzed method offers milder reaction conditions, higher yields, and less industrial waste than the traditional acid/base-catalyzed method [6,7]. ...
Metal–organic framework materials (MOFs) and their derivatives are considered ideal immobilization carrier materials because of their large specific surface area, high porosity and excellent structural designability. Among them, ZIF-8 has great potential for immobilization of enzymes due to mild synthesis conditions, and good biocompatibility. However, conventional ZIF-8 crystals have poor separation and recovery efficiency due to their small pore size and poor acid stability, greatly limiting their application in enzyme immobilization and further application. Although the carbonization of ZIF-8 by pyrolysis has been shown to be one of the approaches that can enhance its chemical stability, this still does not effectively solve the problem of the difficulty of recycling. Herein, we developed a strategy of pre-carbonization immersion (immersion in aqueous FeSO4 solution before carbonization) to synthesize ordered macroporous ZIF-8-derived carbon materials with stable ferromagnetism (denoted as CZ-x-M-y, where x denotes the carbonization temperature and y denotes the concentration of the impregnated FeSO4 solution) and used them to immobilize lipases for biodiesel production. XRD analysis showed that the magnetic properties in the materials came from Fe3C species. We found that the magnetic carbon materials obtained by carbonization at 600 °C showed the best immobilization effect, where CZ-600-M-0.3 (using 0.3 mol·L−1 FeSO4 aqueous solution to soak ZIF-8 and carbonized at 600 °C) had the highest enzyme loading of 183.04 mg·g−1, which was 49.7% higher than that of the non-magnetic CZ-600. In addition, CZ-600-M-0.5 maintained the highest enzyme activity, which was 81.9% of the initial activity, after five batches of reuse. The stable magnetic support materials reported in this study have promising potential for the industrial application of immobilized lipase.
... Different sources are available for lipases, including plants, animals, and microorganisms, and, specifically, the versatility of microbial lipases with relatively easy production makes them more attractive for industrial applications [6]. Among various microbial sources, lipases from thermophilic bacteria can have high application possibilities because of their high stability and activity at higher temperatures than non-thermophilic enzymes. ...
Lipases can catalyze synthesis reactions in a micro aqueous system, producing useful partial glycerides (mono- and diglycerides), and these compounds are commonly utilized in different products as surfactants. Depending on the microbial sources for lipases, immobilization conditions, and starting substrates for synthesis reaction, the composition and yields of the resulting partial glycerides could be variable. These differences could lead to the final efficacy of partial glycerides as surfactants in targeted products. Therefore, it is necessary to establish a group of immobilized lipases from different microbial sources with information about substrate specificity to produce effective partial glycerides for various product types. Here, lipases from thermophilic Geobacillus stearothermophilus and Anoxybacillus flavithermus were prepared with a simple partial purification method, and after immobilization, these lipases were tested to synthesize partial glycerides using different types of decanoic acids. The distinct product patterns were analyzed using HPLC. Both immobilized lipases showed the highest substrate selectivity to decanoic acids in common, producing mainly glyceryl monodecanoate. However, commercial immobilized lipases from Thermomyces lanuginosus produced the largest glyceryl monodecanoate from methyl decanoate. These results indicate the importance of immobilization conditions like different microbial sources and substrates and the need for their optimal combination.
... [199,200]. Additionally, lipases are widely applied in treatment of fat-containing effluent released from food processing, paper, cellulose and tanneries, industries [201]. ...
Huge quantities of the agricultural wastes are produced from practices related to industrial processing, which are mainly burned and thrown in landfills, becoming a threat to the human health and causing environmental pollution. Agro-industrial residues, such as sugarcane bagasse, orange peel, wheat bran, corn straw, barley, rice straw, corn cob, husk, soy bran, and coffee husk were considered as valuable raw materials that can be converted into products of biotechnological interest using microorganisms. Agro-industrial wastes rich in nutrients, such as proteins, minerals, and sugars that, used as possible low cost substrates, for the fungal cultivation, thus considered as an alternative eco-friendly tool for many biological products of economic value, such as enzymes. Fungi organisms are capable of synthesizing a wide range of relevant oxidative and hydrolytic extracellular enzymes, such as peroxidases, laccases, xylanases, and cellulases. The enzymes secreted fungi, are proteins that function as bio-catalysts, responsible for carrying out various biochemical reactions, which applied in food, detergent, cellulose, paper, cosmetics and textile industries, etc. Thus, the replacement of raw materials with lignocellulosic-sources can result in reducing environmental problems and resolving the pollution associated with their disposal, in addition a higher investment will be gained. Therefore, a review was carried out on the important value of agro-industrial wastes, and the cultivation of fungal isolates for economic production of the industrially important enzymes, based on submerged and solid-state fermentation processes, as well as the important application of these enzymes.
