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Although the range of applications for enzymatic reactions in organic solvents is rapidly expanding, this study focused on the enzymatic activity in the esterification of lauric acid with benzyl alcohol, and thermostability of lipase using poly(ethylene glycol) (PEG)-lipase complex and molecular imprinting techniques. The catalytic activity was enhanced through molecular imprinting and the PEG-lipase complex. The imprinting operation was particularly effective for catalytic activity after forming the PEG-lipase complex. The kinetic analysis of the lipase-catalyzed esterification revealed that the increase in esterification rate with imprinted lipases was mainly due to the higher maximum rate achieved by the system. The thermostability of the lipases was significantly improved by imprinting at all temperatures (50~70 °C). After forming a PEG-lipase complex, the imprinted lipase exhibited much higher reactivity and thermostability compared to the native lipase and the imprinted PEG-lipase complex.

In this study, attempts were made to evaluate shells of egg and snail, crystal beads, and kaolin clay as suitable carriers for the immobilization of purified lipase produced by Aspergillus pseudotamarii. The free and immobilized lipases were characterized and applied in the synthesis of butyl butyrate. Snail shell yielded 84.17% immobilization efficiency, surpassing other carriers. Optimal activity occurred at 40°C and 45°C, yielding 2.0U/ml and 3.0U/ml for free and immobilized lipase, respectively. Immobilized lipase demonstrated superior thermal stability (62.6% vs. 0% at 300 min). pH influenced activity, with maxima at pH 7 and 6.5 for immobilized and free lipase. Kinetic parameters: Km, Vmax—3.17mM, 0.549 μM/min (free); 0.214mM, 0.894 μM/min (immobilized). Immobilized lipase exhibited better storage stability. Butyl butyrate synthesis favored immobilized lipase (71.85% vs. 52.38% yield). Optimization studies showed that the immobilized lipase achieved the highest conversion yield at a shorter reaction time and higher temperature compared to the free lipase. The immobilized lipase also exhibited excellent reusability, maintaining a stable conversion yield over multiple cycles. Overall, the immobilized lipase on snail shell showed promising characteristics and potential for butyl butyrate synthesis.

Abstract Generally wastewater such agricultural runoff is considered a nuisance; however, it could be harnessed as a potential source of nutrients like nitrates and phosphates in integrated biorefinery context. In the current study, microalgae Chlorella sp. S5 was used for bioremediation of agricultural runoff and the leftover algal biomass was used as a potential source for production of biofuels in an integrated biorefinery context. The microalgae Chlorella sp. S5 was cultivated on Blue Green (BG 11) medium and a comprehensive optimization of different parameters including phosphates, nitrates, and pH was carried out to acquire maximum algal biomass enriched with high lipids content. Dry biomass was quantified using the solvent extraction technique, while the identification of nitrates and phosphates in agricultural runoff was carried out using commercial kits. The algal extracted lipids (oils) were employed in enzymatic trans-esterification for biodiesel production using whole-cell biomass of Bacillus subtilis Q4 MZ841642. The resultant fatty acid methyl esters (FAMEs) were analyzed using Fourier transform infrared (FTIR) spectroscopy and gas chromatography coupled with mass spectrometry (GC–MS). Subsequently, both the intact algal biomass and its lipid-depleted algal biomass were used for biogas production within a batch anaerobic digestion setup. Interestingly, Chlorella sp. S5 demonstrated a substantial reduction of 95% in nitrate and 91% in phosphate from agricultural runoff. The biodiesel derived from algal biomass exhibited a noteworthy total FAME content of 98.2%, meeting the quality standards set by American Society for Testing and Materials (ASTM) and European union (EU) standards. Furthermore, the biomethane yields obtained from whole biomass and lipid-depleted biomass were 330.34 NmL/g VSadded and 364.34 NmL/g VSadded, respectively. In conclusion, the findings underscore the potent utility of Chlorella sp. S5 as a multi-faceted resource, proficiently employed in a sequential cascade for treating agricultural runoff, producing biodiesel, and generating biogas within the integrated biorefinery concept. Graphical Abstract

Lipases are enzymes of great application importance in the food industry, in the cosmetic and detergent industries, in pharmacy and medicine, and in organic chemistry. Among lipases of various origins, those from microorganisms are currently the most commonly used. An excellent producer of lipases seems to be the nonconventional Yarrowia lipolytica yeast, but the biosynthesis of valuable metabolites depends on many factors. This study aimed to investigate the biodiversity of extracellular enzymes produced by four strains of Y. lipolytica, and to determine the optimal conditions of catalysis for the enzymes, according to temperature and pH, in a model hydrolysis reaction. Based on the obtained results, the biodiversity and strain dependence in lipase biosynthesis were observed. Using a Central Composite Design, it was found that temperature is the main factor in determining lipase activity. The enzymes produced by four different strains exhibited other substrate specificity, which was investigated using Latin square design methodology. Only two examined yeast strains, KKP 379 and W29, produced extracellular lipases at a high activity level towards medium- and long-chain fatty acid esters. Moreover, extracellular lipase from wild-type strain KKP 379 was further characterized, followed by exploring the activity of whole-cell biocatalyst and lyophilized enzyme solutions, and it was acknowledged that it was a “true” lipase with the highest affinity to p-nitrophenyl oleate.

This report describes the asymmetric synthesis of a focused library of enantiopure structured triacylglycerols (TAGs) comprised of a single saturated fatty acid (C6, C8, C10, C12, C14 or C16), a pure bioactive n-3 polyunsaturated fatty acid (EPA or DHA) and a potent drug (ibuprofen or naproxen) intended as a novel type of prodrug. One of the terminal sn-1 or sn-3 positions of the glycerol backbone is occupied with a saturated fatty, the remaining one with a PUFA, and the drug entity is present in the sn-2 position. This was accomplished by a six-step chemoenzymatic approach starting from enantiopure (R)- and (S)-solketals. The highly regioselective immobilized Candida antarctica lipase (CAL-B) played a crucial role in the regiocontrol of the synthesis. All combinations, a total of 48 such prodrug TAGs, were prepared, isolated and fully characterized, along with 60 acylglycerol intermediates, obtained in very high to excellent yields.

Legumes are a rich source of polyphenolic compounds known for their ability to promote health. Under stress conditions, legumes have been shown to produce higher levels of secondary metabolites, as a defensive mechanism. Hence, the present study aimed to induce legume seeds (e.g., soybean, chickpea, green pea, and red kidney bean) by inoculating them with Aspergillus sojae (A. sojae) and to evaluate the extracts for phytoalexins, phenolics, and antioxidant, antiobesity, and antidiabetic potentials. The UPLC-DAD findings of A. sojae-induced legumes showed medicarpin and maackiain in chickpea, pisatin in green pea, glyceollin I-III in soybean, and kievitone and phaseollin in red kidney bean. All induced legumes exhibited a higher total polyphenol content compared to the non-induced ones. Among induced legumes, soybean exhibited a higher (4.85 mg GAE/g) polyphenol content. The UPLC-ESI-QTOF-MS/MS findings established that legumes contained substantial levels of protocatechuic acid, vanillic acid, ferulic acid, chlorogenic acid, coumaric acid, 4-hydroxybenzoic acid, and caffeic acid. The results of antioxidant assays revealed a significantly higher level of activity in induced red kidney bean and soybean, whereas the level of activity in non-induced legumes was markedly lower. Moreover, induced red kidney bean effectively inhibited α-glucosidase (87.2%) and α-amylase (63.90%) at 5 mg/mL. Additionally, the maximum lipase inhibitory effects were displayed by induced soybean (72.54%) at 20 mg/mL.

The present study highlights the true potential of Rhizopus oligosporus IIB-08 to produce lipase enzyme under solid-state fermentation and focuses on improving the properties of lipase by immobilizing it on biogenic aluminium oxide nanoparticles (Al-NPs) for better resolution of active homochiral 2-octanol. For this purpose, almond meal substrate showed 10.44 ± 0.36 U·g−1 lipase activity. The immobilization of lipase on biogenic Al-NPs prepared using Mentha spicata leaf extract led towards improved stability and catalytic efficiency, resulting in a 9.3% increase in activity compared to free enzyme. This study also examined the potential of the immobilized lipase in the effective resolution of 2-octanol. Gas chromatography-mass spectrometry confirmed the presence of lipase-catalysed fatty acids, such as linolenic acid (C18:3), linoleic acid (C18:2), palmitic acid, and oleic acid (C18:1), with palmitic acid exhibiting the highest concentration (142 μg·ml−1) at a retention time of 23.2 min. This study concludes that R. oligosporus IIB-08 is a promising source for lipase production and demonstrates the significant potential of nanoparticle-immobilized lipase in resolving pharmaceutically important organic chemicals, thereby making it a promising approach for different industrial applications. However, further scaling up is needed for better implementation in the industry.

Ethyl hydrocinnamate is an ester with a sweet, fruity, honey-like scent commonly used as a flavor and fragrance agent. Due to its chemical structure, it can be easily obtained through enzymatic reactions without the need for harsh substances and processes. This study investigated the immobilization of the commercial lipase Sustine® 131 onto spent coffee grounds (SCG) as a low-cost support for the enzymatic synthesis of ethyl hydrocinnamate. Spent coffee grounds underwent pretreatment with water, hexane, and ethanol to serve as a lipase adsorption platform and extract valuable bioactive compounds such as polyphenols. The immobilized lipase displayed both hydrolytic and synthetic activities during 12 weeks of storage at room temperature. The optimal reaction conditions for the synthesis of ethyl hydrocinnamate were determined using a Box–Behnken plan. It was shown that the enzyme concentration and the temperature were crucial for achieving high yields of ethyl hydrocinnamate with a conversion rate above 92%. Specifically, at least 18% enzyme concentration and a temperature of 45 °C were necessary. This eco-friendly approach utilized abundant food waste residue as an inexpensive and renewable immobilization support, enabling efficient biocatalytic production of the high-value flavor ester ethyl hydrocinnamate.

Despite mounting evidence of micro-nanoplastics (MNPs) in food and drinking water, little is known of the potential health risks of ingested MNPs, and nothing is known of their potential impact on nutrient digestion and absorption. We assessed the effects of environmentally relevant secondary MNPs generated by incineration of polyethylene (PE-I), on digestion and absorption of fat in a high fat food model using a 3-phase in vitro simulated digestion coupled with a tri-culture small intestinal epithelium model. The presence of 400 μg/mL PE-I increased fat digestion by 33% and increased fat absorption by 147 and 145% 1 and 2 h after exposure. Analysis of the PE-I lipid corona during digestion revealed predominantly triacylglycerols with enrichment of fatty acids in the small intestinal phase. Protein corona analysis showed enrichment of triacylglycerol lipase and depletion of β-casein in the small intestinal phase. These findings suggest digestion of triacylglycerol by lipase on the surface of lipid-coated MNPs as a potential mechanism. Further studies are needed to investigate the mechanisms underlying the greater observed increase in fat absorption, to verify these results in an animal model, and to determine the MNP properties governing their effects on lipid digestion and absorption.

Pancreatitis after Esophagogastroduodenoscopy (EGD) is not a common occurrence, particularly in the setting of a normal serum lipase. The lack of commonality may delay diagnosis and treatment in some patients presenting to the emergency department with abdominal pain after an otherwise uncomplicated procedure. This case report serves to bring awareness to this potential procedural complication and the possibility of pancreatitis with a normal serum lipase.

BACKGROUND: The relative low stability, reusability and activity of enzymes made the industrial production of vitamin E succinate (VES) can only be performed with complex processes and high cost using chemical methods. To address these issues, in the present study, an ionic liquids (ILs) modification strategy was developed to improve the activity and stability of lipases in VES synthesis. RESULTS: The results showed that the [1-butyl-3-methyl imidazole] [N-acetyl-L-proline] ILs modified Candida rugosa lipase (CRL) has the highest modification degree (48.28%), activity (774 U g-1), thermostability and solvent tolerance in three selected modifiers. Additionally, after reaction condition optimization, the highest yield of VES can be improved to 95.18% at 45 °C for 15 h, which was significantly improved compared to some previous studies. CONCLUSION: In the present study, a high-efficiency VES synthesis strategy was successfully developed via modification of lipase. Moreover, the mechanism by which ILs modification can enhance the activity and stability of lipase was investigated via both experimental and computational-aided methods. Molecular dynamics simulation suggested that ILs modification changed the geometry of Phe344 from flat to upright, which significantly reshaped and enhanced the size of substrate binding pocket of CRL. It is also agreement with our circular dichroism and fluorescence spectroscopy results, which suggested that the modification changed the secondary structure of CRL to a certain extent. The larger pocket also endowed the suitable binding pose of succinate, which made the hydrogen bonds between succinate and active site Ser209 become stronger, and thus improving the yield of VES. [ABSTRACT FROM AUTHOR]

Ursodeoxycholic acid (UDCA) and acetoacetate are natural compounds present in the human intestine and blood, respectively. A number of studies highlighted that besides their well-known primary biological roles, both compounds possess the ability to influence a variety of cellular processes involved in the etiology of various diseases. These reasons suggested the potential of acetoacetate–UDCA hybrids as possible therapeutic agents and prompted us to develop a synthetic strategy to selectively derivatize the hydroxyl groups of the bile acid with acetoacetyl moieties. 3α-acetoacetoxy UDCA was obtained (60% isolated yield) via the regioselective transesterification of methyl acetoacetate with UDCA promoted by the Candida antarctica lipase B (CAL-B). 3α,7β-bis-acetoacetoxy UDCA was obtained instead by thermal condensation of methyl acetoacetate and UDCA (80% isolated yield). This bis-adduct was finally converted to the 7β-acetoacetoxy UDCA (82% isolated yield) via CAL-B catalyzed regioselective alcoholysis of the ester group on the 3α position. In order to demonstrate the value of the above new hybrids as UDCA-based scaffolds, 3α-acetoacetoxy UDCA was subjected to multicomponent Biginelli reaction with benzaldehyde and urea to obtain the corresponding 4-phenyl-3,4-dihydropyrimidin-2-(1H)-one derivative in 65% isolated yield. [ABSTRACT FROM AUTHOR]

In the present work, the biocompatible sulfobetaine‐type zwitterionic surfactant (SB‐n) was selected to construct hydrophobic ionic liquid (HIL)‐based bicontinuous microemulsion (BME). It is shown that the [C8mim][PF6] (1‐octyl‐3‐methylimidazolium hexafluorophosphate)‐based BME stabilized by mixed SB‐8/SB‐16 is more suitable for the expression of lipase activity than that stabilized by a single SB‐12. It is also demonstrated that the lipase activity in the present BME is higher than in the corresponding droplet‐type microemulsion. The lipase‐catalyzed hydrolysis of racemic α‐phenylethyl esters was used as a model reaction. It is found that the yield and the enantiomeric excess (ee) value of the product α‐phenylethanol depend on the lipase sources. In the SB‐8/SB‐16‐stabilized BME, Candida antarctica lipase (B) has the best hydrolysis activity and stereoselectivity toward α‐phenylethyl esters. It is also found that the surfactant content, buffer pH and substrate chain length affect the yield and the ee value of the product. Under optimized conditions, a yield of 41 % and an ee value of ~100 % were obtained. The present study is helpful for the development of an effective and environmentally benign medium for lipase‐based conversions. [ABSTRACT FROM AUTHOR]

Here in this work we successfully designed and synthesized a library of some novel pyrrolidine-triazole-aurone hybrids i.e. (Z)-2-benzylidene-6-((1-(2-(pyrrolidin-1-yl)ethyl)-1H-1,2,3-triazol-4-yl)methoxy)benzofuran-3(2H)-one derivatives 5(a-k). The structures of all the synthesized hybrid aurones were confirmed based on their spectral (FT-IR, 1H NMR, 13C NMR) and HRMS data. In biological studies, the impact of synthesized compounds on digestive enzymes, amylase, lipase, and trypsin was analyzed. These compounds exhibited varying effects on these enzymes as both trypsin and amylase were activated, but a significant inhibition was achieved for the lipase enzyme. Upon examining the binding energies of the synthesized compounds with the enzymes, it was observed that the experimental findings partially aligned with the docking results. These in vitro and in silico results of these hybrid aurones against digestive enzymes, signify their potential as anti-inflammatory and anti-obesity agents. [ABSTRACT FROM AUTHOR]

Summary: Lipid metabolism due to lipid hydrolysis and oxidation considerably contributes to the final product quality of fermented fish products and especially impacts its flavour. Lipase and lipoxygenase (LOX) are key enzymes involved in lipid metabolism. Endogenous lipases (lipase from fish muscle and adipose tissue) and/or exogenous lipases (lipase from microorganisms, the added lipase) catalyse the hydrolysis of lipids, producing numerous free fatty acids. LOX in fish gills and skin tissues plays an important role in lipid oxidation. During the catalysis by LOX, polyunsaturated fatty acids having cis, cis‐1,4‐pentadiene structure are oxidised, finally leading to the generation of flavour precursors or compounds such as alcohols, aldehydes, ketones, esters and acids. The addition of lipase effectively enhances the content of acidic components. Simultaneously, fermented fish products with a start culture capable of producing both lipase and LOX exhibit higher levels of flavour and aroma. In this process, the collaborative action of lipase and LOX generates a rich array of volatile flavour components. This review offers a comprehensive overview of the distinct functions and effects of both endogenous and exogenous lipase, along with LOX, in fermented fish products, as well as their roles in lipid metabolism. The study also explores their effects on the main volatile flavour compounds of fermented fish products. Moreover, the article discusses the prospects of applying lipase and LOX in fermented fish products, highlighting some limitations in current research and offering recommendations for future studies. [ABSTRACT FROM AUTHOR]

• Thermal stability of polysorbate-degradative enzymes was assessed with chemical proteomics and biophysical studies. • Brief heat treatment inactivated polysorbate-degradative enzymes and had minimal impact on the therapeutic antibody. • Heat inactivation of protein-A pool decelerated polysorbate degradation. Polysorbate degradation in biotherapeutics formulations is an industry-wide problem and mainly caused by residual host cell-derived enzymes. We present a proof-of-concept study of a control strategy which takes advantage of lower thermal stability of such enzymes relative to therapeutic proteins. We profiled heat sensitivity of host cell–derived enzyme activity with chemical proteomics and observed that PLA2G7 became inactive after brief heating. Further biophysical studies indicated that these enzymes were less thermally stable than a monoclonal antibody. Importantly, brief heat treatment had minimal impact on the stability of the antibody. Consequently, heat inactivation of polysorbate-spiked protein-A pool decelerated polysorbate degradation. This study suggests that heat inactivation of host cell–derived enzymes could be a control stragy for polysorbate degradation. [ABSTRACT FROM AUTHOR]

Enzymes play an important role in numerous natural processes and are increasingly being utilized as environmentally friendly substitutes and alternatives to many common catalysts. Their essential advantages are high catalytic efficiency, substrate specificity, minimal formation of byproducts, and low energy demand. All of these benefits make enzymes highly desirable targets of academic research and industrial development. This review has the modest aim of briefly overviewing the classification, mechanism of action, basic kinetics and reaction condition effects that are common across all six enzyme classes. Special attention is devoted to immobilization strategies as the main tools to improve the resistance to environmental stress factors (temperature, pH and solvents) and prolong the catalytic lifecycle of these biocatalysts. The advantages and drawbacks of methods such as macromolecular crosslinking, solid scaffold carriers, entrapment, and surface modification (covalent and physical) are discussed and illustrated using numerous examples. Among the hundreds and possibly thousands of known and recently discovered enzymes, hydrolases and oxidoreductases are distinguished by their relative availability, stability, and wide use in synthetic applications, which include pharmaceutics, food and beverage treatments, environmental clean-up, and polymerizations. Two representatives of those groups—laccase (an oxidoreductase) and lipase (a hydrolase)—are discussed at length, including their structure, catalytic mechanism, and diverse usage. Objective representation of the current status and emerging trends are provided in the main conclusions. [ABSTRACT FROM AUTHOR]

Background: Naringin is one of the main flavonoids in citrus fruits and byproducts. This flavanone has been shown to be a good antioxidant nutraceutical component, and it also has potential as a gut microbiome modulator, although its applications in final formulations represent a challenge due to its low solubility, both in water and in organic solvents. This work addresses this problem by functionalizing naringin through enzymatic acylation. Results: The enzymatic acylation catalyzed by the lipase Novozym® 435 and using acyl donors of different chain lengths, acetate (C2), propionate (C3), and laurate (C12), yielded in conversions of 95% at 24 h and 100% at 48 h, generating a monoacylated product. Both the aqueous and solvent solubility of acylated naringin products were improved while maintaining or even increasing their antioxidant activity. Conclusions: This acylation process significantly enhanced both the water and solvent solubility of the acylated naringin products while preserving or even enhancing their antioxidant activity. In addition to the gut-modulating properties of flavonoids, acylating them with short- and medium-chain fatty acids could enhance their potential applications in the emerging field of research dedicated to understanding and modulating gut health. [ABSTRACT FROM AUTHOR]

Cold-active enzymes are extremozymes produced by psychrophiles, and have attracted much attention as biocatalysts due to their capacity to resist extreme reaction conditions in industrial processes. This study aimed to isolate bacterial strains from Arctic fjord sediments and screen them for lipase enzyme production. Out of 73 isolates, 8 were identified as good lipase producers. Bacillus cereus I13 exhibited the highest activity of 11.42 U/mL on the 4th day of incubation at 20 °C, along with the large zone of clearance of 27 mm. Optimum conditions for lipase production were identified as pH 7.0, a temperature of 20 °C, and 96 h of incubation, with glucose as a carbon source, yeast as a nitrogen source, and olive oil as a substrate. Bacillus cereus I13 has the potential to be used for the industrial production of cold-active lipase, and this study provides evidence that potent isolates can effectively increase lipase production. [ABSTRACT FROM AUTHOR]

Background and Objective: Maize is the major staple in sub‐Saharan Africa. Whole‐grain maize meal (WGMM) is highly susceptible to rancidity development. This work investigated whether rancidity development in micronutrient‐fortified WGMM is retarded by drying the grain of safe moisture content to below this level using a commercial hot‐air grain dryer before milling. Findings: Fat acidity (hydrolytic rancidity measure) of WGMM from maize dried to 11.6% moisture and stored for 47 days at 40°C was only 61% of meal from the undried grain control (13.3% moisture). Peroxide value (oxidative rancidity measure) was only 53%. With the exception of riboflavin, there was no reduction in fortificant micronutrients during meal storage. Descriptive sensory evaluation indicated greater similarity to the control for stored maize meal and its stiff porridge from dried maize than for meal and porridge from undried maize. Conclusions: Drying maize grain to 11.6% moisture substantially retards rancidity development in fortified WGMM development, probably by inactivating the grain's lipase and oxidative enzymes, providing a shelf life of at least 20 weeks at 25°C. Significance and Novelty: This simple process to extend the shelf life of whole‐grain maize meal is implementable by any mill with access to a hot‐air grain dryer. [ABSTRACT FROM AUTHOR]

Background and Objectives: Oil contamination can be treated by physical, chemical and biological approaches. The first two methods have limitations such as high costs, inefficacy and altering natural ecosystem. Today, biological treatment is a more interesting process to remove petroleum contamination. Bioremediation is a technique in which biological systems such as microorganisms are applied to degrade or transform harmful chemicals. In recent years, employing hydrocarbon degrading bacteria to cleaning a petroleum contaminated soil has become a prevalent, efficient and cost-effective technique that converts toxic wastes to non-toxic end products. Soil contamination with oil compounds such as heavy naphtha can threaten soil, environmental and human health. In bioremediation process, soil microorganisms use these hydrocarbons as a carbon source and, while making a microbial biomass, play a role in its decomposition and conversion to carbon dioxide. Furthermore, this type of contamination can affect soil microbial population and its enzyme activity. Soil microbiome, in turn, has effect on this contamination using relevant enzymes. Application and comparison of various bioremediation methods such as biostimulation, bioaugmentation and integrated treatment were the main aims of this study to bio-remove heavy naphtha from contaminated soil. Moreover, mmonitoring of soil enzyme activity changes (including dehydrogenase and lipase) in this condition under different bioremediation treatments was another goal of this research. For this purpose, in a heavy naphthacontaminated sandy loam, a variety of bioremediation treatments, including biostimulation (including supply of nitrogen and phosphorus elements, addition of manure and Tween 80), bioaugmentation treatment (using a consortium of efficient bacteria) and integrated treatment (including all biostimulation and bioaugmentation treatments together) were tested. Methodology: In this study, a sandy loam soil was used. Heavy naphtha was applied at a rate of 7% V/W to soil samples and various bioremediation treatments were performed as mentioned above. This experiment was carried out in a pot scale (containing 3 kg soil) based on split plot factorial design (pollution factor, bioremediation factor and time) with 3 replications, at room temperature for 120 days. During the experiment, the pots were aerated once a week and the soil moisture content was adjusted to 70-80% (W/W) of the soil water holding capacity twice a week. For bioaugmentation of bacterial isolates, a bacterial suspension (108 cfu mL-1) having a consortium of Arthrobacter sp. COD2-3, Stenotrophomonas nitritireducens COD5-6 ، Stenotrophomonas asidamainiphila COD1-1 with a ratio of 5% V/W were used. In biostimulation treatment, cow manure with 5% W/W was used. In NP treatment, N and P elements from ammonium nitrate and potassium phosphate (K2HPO4), were used with a ratio of 20:5:1 (C: N: P), considering soil organic carbon. Tween 80 as surfactant in the relevant treatments, was used at a rate of 0.3% V/W. In the integrated treatment, all the mentioned treatments were used together. On days 0, 5, 10, 15, 30, 45, 60, 90 and 120, subsamples were taken from each pot to measure the activity of dehydrogenase and lipase enzymes. Findings: The results showed that during the experiment, bioremediation treatments reduced heavy naphtha contamination and the highest value for removal rate of this compound was 81% in the integrated treatment. Contamination also affected the enzymatic activity of soil so that the activity of dehydrogenase and lipase in all bioremediation treatments showed a decreasing trend. Dehydrogenase enzyme activity in cow manure treatment decreased from 1.67 to 0.59 (μg TPF g-1 h-1) and activity of soil lipase enzyme decreased from 33.82 to 26.24 (mU g-1) in the integrated treatment during the experiment. Among the bioremediation treatments, cow manure and integrated treatment had a greater effect on the elimination of heavy naphtha contamination than other treatments (p <0.01). It seems that the use of the above treatments were able to remove more heavy naphtha by providing optimal nutritional, moisture and aeration conditions while intensifying the activity of soil microorganisms. Conclusion: In this study, to reduce heavy naphtha contamination in the soil, bioremediation treatments including biostimulation, bioaugmentation and integrated approaches were used. According to the results of changes in dehydrogenase and lipase activity in naphtha-contaminated soil, each treatment was able to reduce contamination individually, while the integrated treatment was both biostimulatory and bioenhancing treatments. However, in the integrated treatment, the efficiency of bioremediation process was higher, due to the simultaneous use of biostimulation and bioaugmentation treatments. The use of integrated treatment in soils contaminated with petroleum compounds, including heavy naphtha, can help to biologically eliminate these contaminants. [ABSTRACT FROM AUTHOR]

Lipases (triacylglycerol acylhydrolases, E.C. 3.1.1.3) are enzymes widely applied in industry and medicine. Our previous study showed that Candida catenulata produced much higher lipase activity in presence of 150 mg fluconazole than that in untreated control. Consequently in this study, optimization of fluconazole-treated C. catenulata for maximum lipase production was carried out. Fluconazole-treated C. catenulate cultured on medium containing 2.5% Tween 80 as carbon source, 0.7% yeast extract as nitrogen source, and 10 mM CuSO4.5H2O. pH 5.5, dark incubation at 37 °C under dark agitation for 3 days expressed the optimum physiological variables for maximum lipase production. Transmission electron microscopy (TEM) of the native cell (control) of C. catenulata declared a typical morphology of Candida cell with a uniform central density, typical structured nucleus, and a cytoplasm with several elements of endomembrane system and enveloped by a regular intact cell wall. The TEM photomicrograph of 150 mg fluconazole-treated cells of C. catenulata showed that the ultrastructures of treated C. catenulata displayed many noticeable morphological changes. The effect of mutagens [sodium azide (SA), ethidium bromide (EtBr), ethanol (EtOH)] was assayed on the lipase activity from C. catenulata. All mutagenic compounds with different concentrations decreased the lipase activity. Yeast specific activity, protein concentrations, and dry biomass gradually reached their highest decline at mutagen-elevated concentrations. Combination of lower concentrations of mutagen (0.1 µg/ml EtBr + 0.5 mM SA + 10% EtOH, Comb-Fl) exerted synergistic inhibition action and reduced C. catenulata virulent factor (lipase) over their single treatment. When 150 mg fluconazole was added to the mutagen's combination mixture (Comb + Fl), an increase in the production of the virulence factor lipase by C. catenulata was detected. This action indicated the antagonistic effect of fluconazole over the mutagen combination mixture in increasing the fungal pathogenicity. [ABSTRACT FROM AUTHOR]

This study assessed the application of whole lipolytic cells in the pretreatment of slaughterhouse wastewater to reduce its lipid content. The fungal biomass of Rhizopus oryzae was evaluated in the hydrolysis of slaughterhouse wastewater containing high lipid concentrations, focusing on the biomass's concentration and the effect of using an emulsifier and surfactant. The use of the whole-cells lipase of Rhizopus oryzae grown in a residual vegetable oil medium proved effective in the hydrolysis of slaughterhouse wastewater, generating concentrations of free fatty acids (FFA) ranging from 40.36 to 90.14 mM. The action of lipase in the hydrolysis of slaughterhouse residues indicated its effectiveness in pretreating lipid-rich liquid residues, potentially boosting the microbiota of this anaerobic treatment. The results showed that lipase activity without surfactant exhibited a similar performance to that of Triton X-100 in the hydrolysis of liquid residues. However, the combination of lipase and surfactant could represent a promising strategy to optimize free fatty acid production from slaughterhouse residues, strengthening anaerobic treatment processes and potentially enhancing the overall efficiency of waste management systems. [ABSTRACT FROM AUTHOR]

The detergent formulations and the ingredients used in the formulations are variable in the entire world depending on the climate, cost, results, laundry trends and other multiple factors. The impact of detergent components on lipase (enzyme) activity was evaluated after incubation at 20 °C for 1 h and 2 h. Tween-80 demonstrated the highest residual activity, with percentages of 90.3 % and 74.6 %, respectively, inhibiting lipase activity by approximately 10 %–25 % compared to the control. Testing five laundry detergents for lipase production over various time intervals (12–16 h) and temperatures (4 °C, 20 °C, and 50 °C) indicated that "brite" detergent displayed the highest residual activity, with percentages of 84.2 %, 82.5 %, and 80.8 %, respectively, inhibiting lipase activity by approximately 15 %–20 % compared to the controls. These findings suggest that laundry detergents have a slight inhibitory effect on lipase production compared to the crude enzyme, and longer incubation periods result in decreased lipase production. [ABSTRACT FROM AUTHOR]

Biodiesel is synthesized by the transesterification of triglycerides of oils with short-chain alcohols, such as methanol and ethanol. According to the Renewable Energy Directive guidelines (RED II 2018/2001/EU) the contribution of advanced biofuels, which do not include edible oils, towards the overall EU target, is at 1% in 2025 and at least 3.5% in 2030. Bioprocesses that valorize non-edible oils for the production of second-generation biodiesel could play a critical role in achieving this goal. Immobilized lipases, as well as other enzyme classes, such as cutinases and acyltransferases, are utilized as biocatalysts for this process. For the sustainability of the process, renewable materials can be used as immobilization matrices, or even enzymes anchored on the cells as wholecell biocatalysts. Membrane reactors can also be employed to facilitate the enzymatic transesterification by conducting a continuous enzymatic reaction and simultaneously separate the products in a single operation. The advances on the aforementioned fast-pacing fields are presented in this work. [ABSTRACT FROM AUTHOR]

Pickering emulsions (PE) are liquid-liquid systems that are stabilized by solid (nano)particles at the fluid interface. They offer higher stability, easier separation and lower toxicity compared to classical emulsions stabilized by surfactants. Common applications range from food science to drug delivery. In the last decade they have become of more interest in the field of multiphasic biocatalysis. First, this study aims to present the influence of pH, salt strength and particle charge on enzyme activity. The different behavior of two lipases (CaLA and CRL) is shown. While the activity optimum of CaLA changed from pH 6.5 to pH 5 by applying particles with negative instead of positive surface charge, the CRL activity optimum stayed at pH 5–5.5. This enables particle charge as an additional parameter to optimize biocatalytic reactions in PEs. Second, the resulting drop sizes were measured to elucidate further interactions between the enzymes and particles in PEs. Drop sizes in PEs prepared with CaLA were not influenced by pH, but increased for positively and decreased for negatively charged particles upon the addition of CaLA. Electrostatic attraction between particles and CRL increased the droplet diameter from 10 μm up to 30 μm and therefore destabilized the PE for both particle types. • Influence of pH, salt strength and particle charge on CaLA and CRL activity inside Pickering emulsions. • activity optimum of CaLA can be shifted to a different pH with varying particle charge. • activity optimum of CRL close to IEP. • CaLA may stabilize or destabilize Pickering emulsions depending on particle charge. [ABSTRACT FROM AUTHOR]

Obesity is a source of significant pathologies and deadly diseases, including heart disease, diabetes, and cancer. One of the most intriguing strategies in the hunt for new anti-obesity medications is the inhibition of pancreatic lipase (PL). This study presents a novel application of short α and β-mixed peptides as pancreatic lipase inhibitors. These peptides were synthesized in the solution phase and characterized using FTIR and 1H-NMR. L-proline is present in a high percentage of natural anti-lipase peptides and was used as a β-amino acid in this study to enhance anti-lipase activity and proteolytic stability. Moreover, L-α-proline was converted to β-amino acid derivatives using the Arndt–Eistert method with the advantage of stereo control at the α-carbon. The synthesized peptides with anti-lipase activity are N-Boc-β-Pro-Gly-OBz (93%), N-Boc-O-Bz-Tyr-β-Pro-β-Pro-Gly-OBz (92%), N-Boc-O-Bz-Tyr-β-Pro-COOH (91%), N-Boc-Phe-β-Pro-OCH3 (90%), and N-Boc-O-Bz-Tyr-β-Pro-OCH3 (89%). These peptides may function as lead molecules for further modification to more significant molecules, which can help control obesity. [ABSTRACT FROM AUTHOR]

Poly (butylene adipate-co-terephthalate) (PBAT) has been extensively used in every field of life, but the PBAT hydrolyzing microorganisms had rarely been studied. In this project, the synergistic degradation effect of bacteria identified from the farm soil of Shaanxi village yuan Jia cun was studied. To improve the degradation of PBAT, a co-culture system was made using SUST B1, SUST B2, and SUST B3. It was noted that the synergistic degradation of PBAT days was greater as compared to the monoculture system. Maximum lipase activity was observed after 6 days of incubation, the lipase activity (24.3 U/mL) of the co-culture surpassed the monoculture which was substantially complex as compared to individual bacterium SUST B1 (9.42 U/mL), SUST B2 (10.1 U/mL), and SUST B3 (8.7 U/mL) degrading 26.1% of PBAT. These results were further confirmed using XRD, FTIR, and SEM analysis. The mechanism of PBAT degradation was also studied using LC/MS. PBAT degradation is comprised of numerous phases that generate oligomers, dimers, and monomers. The microorganisms secreted the PBAT-degrading lipase that catalyzes the ester bonds present in the PBAT backbone and convert it into respective monomers like terephthalic acid, 1, 4-butanediol, and adipic acid. Microbes then uptake them to fulfill their carbon need and degrade them. Hence, PBAT bioremediation can be accomplished by a co-culture system. This is the first study to report the synergistic degradation of PBAT in the co-culture system. [ABSTRACT FROM AUTHOR]

The use of poly (butylene adipate-co-terephthalate) (PBAT) has increased widely but PBAT-degrading bacteria have rarely been studied. During this study, we used farm soil to isolate and identify PBAT-degrading bacteria. We then accessed the effect of growth factors on PBAT degradation as well as the lipase activity of PBAT-degrading bacteria. The serial dilution method was used to isolate the PBAT-degrading microbes from the farm soil of Xinjiang. Microbial colonies were spread and streaked many times to get pure colonies. Xin-A and Xin-B were gram-positive bacteria. Lipase production of these strains was studied using para nitrophenyl palmitate as a substrate which showed that both bacteria were lipase producing and the lipase production of Xin-B (14 U/mL) was superior to Xin-A (11.7 U/mL) degrading almost 13.7% PBAT in 14 days. The activity and degradation of both strains was superior than previously reported species. Among all the available methods, enzymatic hydrolysis is considered to be the best technique to treat the generated plastic waste and this is the most attractive and emerging technique discovered so far. These results provide technical support for the highly efficient degradation of PBAT by lipase in the environment. [ABSTRACT FROM AUTHOR]

Purpose Short bowel syndrome is a malabsorptive condition that occurs due to surgical removal or a congenital absence of a significant portion of the small intestine. Patients with short bowel syndrome often rely on parenteral support for extended periods or even their entire lives. Teduglutide, a glucagon-like peptide-2 analog, has shown promising results in reducing dependency on parenteral support in these patients by promoting intestinal adaptation and enhancing nutrient absorption. However, the long-term safety of teduglutide remains a concern, particularly with respect to its potential for the development of hyperamylasemia and hyperlipasemia. Methods This study involved patients who received teduglutide from December 2012 to December 2022 at Boston Medical Center. We evaluated outcomes and adverse events, focusing on hyperamylasemia and hyperlipasemia, through chart review. Results Thirteen eligible patients were identified who had used teduglutide. Of these, the majority (84.6%) experienced a reduction in parenteral support. A high incidence (72.7%) of nonpathological pancreatic enzyme elevation was observed in patients treated with teduglutide. These elevations were often dose dependent and were not associated with any clinical signs of acute pancreatitis or abnormal imaging findings. Conclusion This study highlights the need for further investigations into the long-term safety of teduglutide and the importance of closely monitoring amylase and lipase levels in patients undergoing treatment with teduglutide. [ABSTRACT FROM AUTHOR]

Background: Biolubricants represent a category of lubricating substances derived from sustainable sources such as vegetable oils, animal fats, and other bio-based materials. They are considered more environmentally friendly than mineral-based lubricants because they are biodegradable and nontoxic. Biolubricants derived from vegetable oils or animal fats were used as first-generation biolubricants. They have limited performance at extreme temperatures, both high and low, as well as low oxidative stability. Substitution of the double bonds by branching improves the performance and stability of the resulting second-generation biolubricants. Methods: In the past, the production of these compounds has relied on the chemical pathway. This method involves elevated temperatures and inorganic catalysts, leading to the necessity of additional purification steps, which decreases environmental sustainability and energy efficiency. A more environmentally friendly alternative, the enzymatic route, has been introduced, in accordance with the principles of "Green Chemistry". Results: In this paper, the esterification of 2-methylhexanoic acid with 2-octyl-1-dodecanol and its optimization were developed for the first time. The synthesis was conducted within a jacketed batch reactor connected to a thermostatic bath in a solvent-free reaction medium and using Lipozyme® 435 as biocatalyst. Conclusions: The high viscosity index value of this new hyperbranched ester (>200, ASTM D2270) suggests that it may be an excellent biolubricant to be used under extreme temperature conditions. Regarding sustainability, the main green metrics calculated point to an environmentally friendly process. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The utilization of lipase in synthesis structured lipids (SLs) from natural oils confers additional health properties and effectively enhances their value-added potential. This paper provided a comprehensive review of recent studies on the enzymatic preparation of SLs, summarizing the advancements in structural design and immobilized enzyme engineering technology to improve the efficiency of their synthesis by enzymatic approaches. The sn-1,3 regiospecific lipase enabled the precise synthesis of SLs, while employing stepwise variable temperature reactions, supercritical fluid reactions, vacuum reactions, and ultrasonic-assisted methods could inhibit the acyl migration effects and further enhance product yield. Furthermore, structural design could enhance the catalytic efficiency, stability, and substrate specificity of lipases to elevate the efficiency and yield in enzymatic synthesis of SLs. Immobilized enzyme technology could enhance enzyme reactivity and stability while reducing the costs of enzymatic synthesis of SLs. In the future, the high-performance enzymes should be developed by combining structural modification and novel immobilization technology on the basis of the clearer understanding of their structure-function characteristics. These insights would contribute to innovation and advancement in efficient and precise enzymatic synthesis processes for SLs. [ABSTRACT FROM AUTHOR]

An efficient microbial conversion for simultaneous synthesis of multiple high-value compounds, such as biosurfactants and enzymes, is one of the most promising aspects for an economical bioprocess leading to a marked reduction in production cost. Although biosurfactant and enzyme production separately have been much explored, there are limited reports on the predictions and optimization studies on simultaneous production of biosurfactants and other industrially important enzymes, including lipase, protease, and amylase. Enzymes are suited for an integrated production process with biosurfactants as multiple common industrial processes and applications are catalysed by these molecules. However, the complexity in microbial metabolism complicates the production process. This study details the work done on biosurfactant and enzyme co-production and explores the application and scope of various statistical tools and methodologies in this area of research. The use of advanced computational tools is yet to be explored for the optimization of downstream strategies in the co-production process. Given the complexity of the co-production process and with various new methodologies based on artificial intelligence (AI) being invented, the scope of AI in shaping the biosurfactant-enzyme co-production process is immense and would lead to not only efficient and rapid optimization, but economical extraction of multiple biomolecules as well. [ABSTRACT FROM AUTHOR]

α‐Sulfinyl esters can be readily prepared through thiol substitution of α‐bromo esters followed by oxidation to the sulfoxide. Enzymatic resolution with lipoprotein lipase provides both the unreacted esters and corresponding α‐sulfinyl carboxylic acids in high yields and enantiomeric ratios. Subsequent decarboxylative halogenation, dihalogenation, trihalogenation and cross‐coupling gives rise to functionalized sulfoxides. The method has been applied to the asymmetric synthesis of a potent inhibitor of 15‐prostaglandin dehydrogenase. [ABSTRACT FROM AUTHOR]

In this study, lipase‐catalyzed resolution of N‐acetyl‐DL‐methionine methyl ester (N‐Ac‐DL‐MetOMe) was evaluated. A lipase from Brucella thiophenivorans was prone to exhibit high activity and excellent enantioselectivity toward N‐Ac‐DL‐MetOMe to produce the key chiral intermediate N‐acetyl‐L‐methionine methyl ester (N‐Ac‐L‐MetOMe). The results showed that the enzymatic reaction was carried out in 100 g/L racemic substrate for 2 h, the conversion reached 51.3%, the enantiomeric excess value N‐Ac‐L‐MetOMe exceeded 99%, and the enantiomeric ratio value >200. Therefore, the lipase from B. thiophenivorans has potential prospects for the resolution of N‐Ac‐DL‐MetOMe to produce the important intermediate N‐Ac‐L‐MetOMe. [ABSTRACT FROM AUTHOR]

Simple Summary: The increasing presence or contamination of various everyday-life products (including foodstuffs) by graphene oxides and silver nanoparticles (GOs and AgNPs, respectively) raises a risk of their possibly deleterious effects on digestive functions and, consequently, nutrient and energy intake by an organism. The study addresses this issue by considering various NP concentrations and exposure times. The scarcity of relevant data makes such studies necessary for the reliable assessment of NP effects. This study on a model insect species—adult house crickets—revealed a changed profile of digestive enzymes' activities in the gut, mainly when a high content of NPs was present in the food: stimulated digestion of carbohydrates and lipids but inhibited digestion of proteins. These changes were more pronounced in AgNP-treated than in GO-treated insects and increased with exposure time. Disturbed digestion led to decreased food consumption with exposure time in AgNP-treated crickets. Food assimilation was also affected—the cumulative food assimilation (CFA) was higher and lower compared with the control in crickets exposed to the lowest and moderate concentrations of AgNPs, respectively. These findings confirmed weak or no effects of low amounts of NPs in food and revealed that their higher concentrations may adversely influence digestive processes and resulting nutrient and energy intakes, particularly during prolonged exposure of an organism. The advancement of nanotechnology poses a real risk of insect exposure to nanoparticles (NPs) that can enter the digestive system through contaminated food or nanopesticides. This study examines whether the exposure of model insect species—Acheta domesticus—to increasing graphene oxide (GO) and silver nanoparticle (AgNP) concentrations (2, 20, and 200 ppm and 4, 40, and 400 ppm, respectively) could change its digestive functions: enzymes' activities, food consumption, and assimilation. We noticed more pronounced alterations following exposure to AgNPs than to GO. They included increased activity of α-amylase, α-glucosidase, and lipase but inhibited protease activity. Prolonged exposure to higher concentrations of AgNPs resulted in a significantly decreased food consumption and changed assimilation compared with the control in adult crickets. A increase in body weight was observed in the insects from the Ag4 group and a decrease in body weight or no effects were observed in crickets from the Ag40 and Ag400 groups (i.e., 4, 40, or 400 ppm of AgNPs, respectively), suggesting that even a moderate disturbance in nutrient and energy availability may affect the body weight of an organism and its overall condition. This study underscores the intricate interplay between NPs and digestive enzymes, emphasizing the need for further investigation to comprehend the underlying mechanisms and consequences of these interactions. [ABSTRACT FROM AUTHOR]