ABSTRACT
The improvement of enzyme thermostability often accompanies the decreased activity due to the loss of the key regions' flexibility. As a representative structure, unlocking the potential of loop dynamics will not only provide new ideas for stabilization strategies, but also help to deepen the understanding of the relationship between enzyme structural dynamics and function. In this study, a creative "hook loop dynamics engineering" (HLoD) strategy was successfully proposed for simultaneously improving the thermostability and maintaining activity of the model enzyme, Candida Antarctica lipase B. A small and smart mutant library involving five key residues located at the "hook loop" was meticulously identified and systematically investigated and thus yielded a five-point multiple mutant M1 (L147S/T244P/S250P/T256D/N292D), demonstrating a remarkable 7.0-fold increase in thermostability at 60 °C compared to the wild-type (WT). Furthermore, the activity of M1 remained comparable to that of WT, effectively transcending the barrier of activity-stability trade-off. Molecular dynamics simulations revealed that the precise regulation of hook loop dynamics via intermolecular interactions, such as salt bridges and hydrogen bonding, curbed the excessive flexibility of the pivotal regions α5 and α10 at high temperatures, thus driving the substantial enhancement of the thermostability of M1. Refining the dynamics of the flexible region via HLoD, which transcended the barrier of activity-stability trade-off, exhibited to be a robust and potentially universal strategy for designing enzymes with outstanding thermostability and activity.
ABSTRACT
To fulfill the requirements of environmental protection, a magnetically recoverable immobilized laccase has been developed for water pollutant treatment. In order to accomplish this objective, we propose a polydopamine-coated magnetic graphene material that addresses the challenges associated with accumulation caused by electrostatic interactions between graphene and enzyme molecules, which can lead to protein denaturation and inactivation. To achieve this, we present a polydopamine-coated magnetic graphene material that binds to the enzyme molecule through flexible spacer arms formed by ionic liquids. The immobilized laccase exhibited a good protective effect on laccase and showed a high stability and recycling ability. Laccase-ILs-PDA-MGO has a wider pH and temperature range and retains about 80% of its initial activity even after incubation at 50 °C for 2 h, which is 2.2 times more active than free laccase. Furthermore, the laccase-ILs-PDA-MGO exhibited a remarkable removal efficiency of 97.0% and 83.9% toward 2,4-DCP and BPA within 12 h at room temperature. More importantly, laccase-ILs-PDA-MGO can be recovered from the effluent and used multiple times for organic pollutant removal, while maintaining a relative removal efficiency of 80.6% for 2,4-DCP and 81.4% for BPA after undergoing seven cycles. In this study, a strategy for laccase immobilization by utilizing ILs spacer arms to modify GO aims to provide valuable insights into the advancement of efficient enzyme immobilization techniques and the practical application of immobilized enzymes in wastewater treatment.
Subject(s)
Enzymes, Immobilized , Graphite , Ionic Liquids , Laccase , Water Pollutants, Chemical , Laccase/chemistry , Laccase/metabolism , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Graphite/chemistry , Ionic Liquids/chemistry , Water Pollutants, Chemical/chemistry , Indoles/chemistry , Catalysis , Polymers/chemistry , Hydrogen-Ion Concentration , Enzyme Stability , TemperatureABSTRACT
Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases' poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases' solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases.
Subject(s)
Lipase , Solvents , Lipase/chemistry , Lipase/metabolism , Solvents/chemistry , Protein Engineering , Enzyme Stability , Biocatalysis , Ionic Liquids/chemistryABSTRACT
The development of immobilized enzymes with high activity and stability is critical. Metal-organic frameworks (MOFs) have attracted much academic and industrial interest in the field of enzyme immobilization due to their unique properties. In this study, the amino-functionalized ionic liquid (NIL)-modified metal-organic framework (UiO-66-NH2) was prepared to immobilize Candida rugosa lipase (CRL), using dialdehyde starch (DAS) as the cross-linker. The results of the Fourier transform infrared (FT-IR) spectra, X-ray powder diffraction (XRD), and scanning electronic microscopy (SEM) confirmed that the NIL was successfully grafted to UiO-66-NH2. The CRL immobilized on NIL-modified UiO-66-NH2 (UiO-66-NH2-NIL-DAS@CRL) exhibited satisfactory activity recovery (79.33%), stability, reusability, and excellent organic solvent tolerance. The research results indicated that ionic liquid-modified UiO-66-NH2 had practical potential for application in enzyme immobilization.
Subject(s)
Enzymes, Immobilized , Ionic Liquids , Lipase , Metal-Organic Frameworks , Lipase/chemistry , Lipase/metabolism , Ionic Liquids/chemistry , Enzymes, Immobilized/chemistry , Metal-Organic Frameworks/chemistry , Enzyme Stability , Spectroscopy, Fourier Transform Infrared , X-Ray Diffraction , Starch/chemistry , Starch/analogs & derivatives , Saccharomycetales/enzymology , Phthalic AcidsABSTRACT
In advanced batteries, interphases serve as the key component in stabilizing the electrolyte with reactive electrode materials far beyond thermodynamic equilibria. While an active interphase facilitates the transport of working ions, an inactive interphase obstructs ion flow, constituting the primary barrier to the realization of battery chemistries. Here, a successful transformation of a traditionally inactive passivating layer on Mg-metal anode, characteristic of Mg-metal batteries with typical carbonate electrolytes, into an active and robust interphase in the Li-metal scenario is presented. By further strategically designing magnesiated Li+ electrolytes, the in situ development of this resilient interphase on Li-metal anodes, imparting enduring stability to Li-metal batteries with nickel-rich cathodes is induced. It is identified that the strong affinity between Mg2+ and anions in magnesiated Li+ electrolytes assembles ionic clusters with a bias for reducibility, thereby catalyzing the creation of anion-derived interphases rich in inorganic constituents. The prevalence of ionic clusters induced by magnesiation of electrolytes has brought properties only available in high-concentration electrolytes, suggesting a fresh paradigm of tailing electrolytes for highly reversible LMBs.
ABSTRACT
Phytosterols usually have to be esterified to various phytosterol esters to avoid their disadvantages of unsatisfactory solubility and low bioavailability. The enzymatic synthesis of phytosterol esters in a solvent-free system has advantages in terms of environmental friendliness, sustainability, and selectivity. However, the limitation of the low stability and recyclability of the lipase in the solvent-free system, which often requires a relatively high temperature to induce the viscosity, also increased the industrial production cost. In this context, a low-cost material, namely diatomite, was employed as the support in the immobilization of Candida rugosa lipase (CRL) due to its multiple modification sites. The Fe3 O4 was also then introduced to this system for quick and simple separation via the magnetic field. Moreover, to further enhance the immobilization efficiency of diatomite, a modification strategy which involved the octadecyl and sulfonyl group for regulating the hydrophobicity and interaction between the support and lipase was successfully developed. The optimization of the ratio of the modifiers suggested that the -SO3 H/C18 (1:1.5) performed best with an enzyme loading and enzyme activity of 84.8 mg·g-1 and 54 U·g-1 , respectively. Compared with free CRL, the thermal and storage stability of CRL@OSMD was significantly improved, which lays the foundation for the catalytic synthesis of phytosterol esters in solvent-free systems. Fortunately, a yield of 95.0% was achieved after optimizing the reaction conditions, and a yield of 70.0% can still be maintained after six cycles.
Subject(s)
Diatomaceous Earth , Enzymes, Immobilized , Phytosterols , Enzymes, Immobilized/metabolism , Esterification , Lipase/metabolism , Biocatalysis , Solvents , Phytosterols/metabolism , Sterols , Enzyme Stability , EstersABSTRACT
Ketogenic diet, characterized by high fat and low carbohydrate content, is gradually becoming a new perspective in the human diet; however, the mechanism of digestion of ketogenic diet remains unknown. In this study, we explored the oil-water interface to elucidate the digestion of a ketogenic diet based on typical representative medium- and long-chain triglycerides. The free fatty acids (FFAs) release indicated that glycerol trioctanoate with a shorter carbon chain (FFA = 920.55 ± 10.17 µmol) was significantly more digestible than glycerol tripalmitate (851.36 ± 9.48 µmol) and glycerol tristearate (805.81 ± 10.03 µmol). Particle size analysis revealed that the length of the carbon chain increased the size of triglycerides, resulting in a decreased contact area with lipase. The interfacial phenomenon indicated that the longer the carbon chain of triglycerides, the greater the reduction in binding capacity with salt ions in the digestive solution. Fluorescence spectroscopy analysis showed that the length of the carbon chain induced the displacement of the lipase peak, suggesting that the carbon chain length could alter the structure of lipase. Molecular dynamics simulation showed that the longer the carbon chain of triglycerides, the easier it was to loosen the structure of lipase. Bond energy analysis showed that the carbon chain length of triglycerides was positively correlated with the bond energy strength of the ester bonding. In conclusion, this study emphasizes that the ketogenic diet should primarily consist of shorter carbon chain triglycerides because carbon chain length can alter the digestion of triglycerides. This provides a new perspective on the quest for more effective ketogenic diet, in line with the current view of healthy diet.
Subject(s)
Diet, Ketogenic , Humans , Glycerol , Triglycerides/chemistry , Lipase/metabolism , Digestion , CarbonABSTRACT
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. © 2023 Society of Chemical Industry.
Subject(s)
Ionic Liquids , Lipase , Lipase/chemistry , Ionic Liquids/chemistry , alpha-Tocopherol , Succinic Acid , Succinates , Enzyme Stability , Enzymes, Immobilized/chemistryABSTRACT
Graphite oxide (GO) is an excellent laccase immobilization material. However, the electrostatic interaction between graphene leads to the accumulation of GO, as well as the interaction with the surface of enzyme molecules causing protein denaturation and deactivation, which limits its further industrial application. In this study, the ionic liquids (ILs) modification strategy was proposed to improve the stability and catalytic performance of immobilized laccase. The laccase-ILs-MGO exhibited remarkable enzymatic properties, with significant enhancements in organic solvent tolerance, thermal and operational stability. The laccase-ILs-MGO system exhibited a remarkable removal efficiency of 95.5% towards 2,4-dichlorophenol (2,4-DCP) within 12 h and maintained over 70.0% removal efficiency after seven reaction cycles. In addition, the efficient elimination of other phenolic compounds and recalcitrant polycyclic aromatic hydrocarbons could also be accomplished. Molecular dynamics simulation and molecular docking studies demonstrated that immobilized laccase exhibited superior structural rigidity and stronger hydrogen bond interactions with substrates compared to free laccase, which was beneficial for the stability of both the laccase and substrate degradation efficiency. Therefore, this study proposed a simple and practical strategy for modifying GO with ILs, providing novel insights into developing efficient enzyme immobilization techniques.
Subject(s)
Graphite , Ionic Liquids , Ionic Liquids/chemistry , Graphite/chemistry , Laccase/chemistry , Laccase/metabolism , Magnesium Oxide , Molecular Docking Simulation , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Oxides , Phenols , Magnetic PhenomenaABSTRACT
As some of the most widely used biocatalysts, lipases have exhibited extreme advantages in many processes, such as esterification, amidation, and transesterification reactions, which causes them to be widely used in food industrial production. However, natural lipases have drawbacks in terms of organic solvent resistance, thermostability, selectivity, etc., which limits some of their applications in the field of foods. In this systematic review, the application of lipases in various food processes was summarized. Moreover, the general structure of lipases is discussed in-depth, and the engineering strategies that can be used in lipase engineering are also summarized. The protocols of some classical methods are compared and discussed, which can provide some information about how to choose methods of lipase engineering. Thermostability engineering and solvent tolerance engineering are highlighted in this review, and the basic principles for improving thermostability and solvent tolerance are summarized. In the future, comput er-aided technology should be more emphasized in the investigation of the mechanisms of reactions catalyzed by lipases and guide the engineering of lipases. The engineering of lipase tunnels to improve the diffusion of substrates is also a promising prospect for further enhanced lipase activity and selectivity.
Subject(s)
Food Industry , Lipase , Lipase/chemistry , Enzyme Stability , Solvents/chemistry , ComputersABSTRACT
Vitamin E (VE) is a natural antioxidant which is widely used in the food fields, while the shortcomings of easy oxidative inactivation and poor water solubility limit its application. Vitamin E esters' (VEEs) derivatives, such as vitamin E acetate (VEA), are more stable and easier to be absorbed while have similar biological activities and physiological functions compared with VE. In this systematic review, the digestion, absorption and physiological function of VEEs were summarized. To promote their further industrial applications, the synthesis strategies of VEEs were also summarized in-depth. In particular, as a new generation of green solvents, ionic liquids (ILs) have been widely used in enzymatic reactions due to the stabilization and activation of enzymes. Their applications in enzymatic synthesis of VEEs were summarized and discussed. Finally, several future perspectives for developing more efficiency strategies of VEEs synthesis, such as enzyme engineering and design of novel ILs, were also discussed.
Subject(s)
Esters , Ionic Liquids , Vitamin E , Solvents , SolubilityABSTRACT
BACKGROUND: Pine sterol ester is a type of novel food source nutrient with great advantages in lowering blood cholesterol levels, inhibiting tumors, preventing prostate enlargement, and regulating immunity. Macroporous resins with large specific surface area, stable structures, and various functional groups (epoxy, amino, and octadecyl groups) have been selected for immobilization of Candida rugosa lipase (CRL) to improve its stability and efficiency in the synthesis of pine sterol esters. A solvent-free strategy using oleic acid (substrate) as an esterification reaction medium is an important alternative for avoiding the use of organic solvents. RESULTS: The immobilization conditions of CRL immobilized on several types of commercial macroporous resins were optimized. Fortunately, by adsorption (hydrophobic interaction), a high immobilization efficiency of CRL was obtained using macroporous resins with hydrophobic octadecyl groups with an immobilization efficiency of 86.5%, enzyme loading of 138.5 mg g-1 and enzyme activity of 34.7 U g-1 . The results showed that a 95.1% yield could be obtained with a molar ratio of oleic acid to pine sterol of 5:1, an enzyme amount of 6.0 U g-1 (relative to pine sterol mass) at 50 °C for 48 h. CONCLUSION: The hydrophobic macroporous resin (ECR8806M) with a large specific surface area and abundant functional groups was used to achieve efficient immobilization of CRL. CRL@ECR8806M is an efficient catalyst for the synthesis of phytosterol esters and has the potential for further large-scale applications. Therefore, this simple, green, and low-cost strategy for lipase immobilization provides new possibilities for the high-efficiency production of pine sterol esters and other food source nutrients. © 2023 Society of Chemical Industry.
Subject(s)
Enzymes, Immobilized , Lipase , Lipase/chemistry , Solvents/chemistry , Enzymes, Immobilized/chemistry , Oleic Acid , Biocatalysis , Candida/metabolism , Sterols , Hydrophobic and Hydrophilic Interactions , Enzyme Stability , EstersABSTRACT
The bio-enzyme degradation technology is a promising approach to sustainably remove pollution in the water and laccase is one of the most widely used enzymes in this area. Nevertheless, the further industrial application of laccase is limited by low stability, short service, low reusability and high price. The immobilization technology can significantly improve the stability and reusability of enzymes and thus promoting their industrial applications. Nanocomposite materials have been developed and applied in the efficient immobilization of laccase due to their superior physical, chemical, and biological performance. This paper presents a comprehensive review of various nanocomposite immobilization methods for laccase and the consequent changes in enzymatic properties post-immobilization. Additionally, a comprehensive analysis is conducted on the factors that impact laccase immobilization and its water removal efficiency. Furthermore, this review examines the effectiveness of common contaminants' removal mechanisms while summarizing and discussing issues related to laccase immobilization on nanocomposite carriers. This review aims to provide valuable guidance for enhancing laccase immobilization efficiency and enzymatic water pollutant removal.
Subject(s)
Environmental Pollutants , Nanocomposites , Water Pollutants, Chemical , Wastewater , Laccase/chemistry , Enzymes, Immobilized/chemistry , Water , Water Pollutants, Chemical/metabolismABSTRACT
Ionic liquids (ILs) have been widely used as chemical modifiers to modify the carriers and thus improve the efficiency, activity and stability of the enzymes. However, as thousands of ILs have been found up to date, it's a huge work for screening and designing suitable ILs for immobilization of enzymes. Moreover, the mechanism of improving enzymes catalytic performance is still remain ambiguous. Thus, this study investigated the impact of ILs with different chain lengths on the enzymatic properties of Candida antarctica lipase B (CALB). Molecular dynamics simulations were employed to examine the interaction between ILs modified CNTs and CALB, as well as their effects on CALB's structure. The results revealed that ILs with different chain lengths significantly influenced the absorption orientation of CALB. Tunnel analysis identified a key role for Leu278 in regulating the open or closed state of Tunnel 2 during CALB's catalytic cycle. The weak interaction analysis demonstrated that ILs with suitable chain lengths provided spatial freedom and formed strong interactions with CNTs and ILs (vdW and hbond). This led to a conformational flip of Leu278, stabilizing the open state of Tunnel 2 and improving the activity and stability of immobilized CALB. This study provides novel insights into the design of new green modifiers to modulate carrier performance and obtain immobilized enzymes with better performance, and establishes a theoretical basis for the design and selection of modifiers for ILs in future work.
Subject(s)
Ionic Liquids , Ionic Liquids/chemistry , Leucine , Lipase/chemistry , Enzymes, Immobilized/chemistry , Fungal Proteins/chemistryABSTRACT
Phytosterol esters have attracted widespread academic and industrial interests due to their advantages in lowering cholesterol, as antioxidants, and in preventing or treating cancer. However, the generation of by-products limits the application of phytosterol esters in food fields. In this study, deep eutectic solvents (DESs), a series of green, nontoxic, low-cost and biodegradable solvents, were adopted as the catalyst for the synthesis of pine sterol esters. The results showed that the acidic DES which was prepared with choline chloride (ChCl) and p-toluene sulfonic acid monohydrate (PTSA) with a molar ratio of 1:3 performed best in the prescreening experiments. To further improve the efficiency of the pine sterol ester, the molar ratio of substrates, the amount of catalyst, the reaction temperature and the reaction time were optimized, and its yield was improved to 94.1%. Moreover, the by-products of the dehydration side reactions of the sterol can be efficiently inhibited. To make this strategy more universal, other fatty acids were also used as the substrate for the synthesis of pine sterol esters, and a yield of above 92.0% was obtained. In addition, the reusability of DES was also investigated in this study, and the efficiency of DES was well maintained within five recycled uses. Finally, DFT calculations suggested that the suitable H-bonds between ChCl and PTSA decreased the nucleophilic capacity and increased the steric hindrance of the latter, and further prevented the attack on ßH and reduced the generation of by-products. This study developed a reliable and eco-friendly strategy for the preparation of high-quality phytosterol esters with low-dosage catalyst usage and high selectivity.
ABSTRACT
Chronic and persistent inflammation associated with excessive high mobility group protein 1 (HMGB1) is a risk factor for various diseases. Dietary intake of kaempferol has been proven to be effective in reducing HMGB1 levels and the degree of inflammation, but the structural mechanism remains unclear. In this context, we first investigated the interaction between bioactive kaempferol and HMGB1 using multi-spectroscopic and molecular simulation techniques. The surface plasmon resonance (SPR) data indicated that kaempferol binds directly to HMGB1 with a Kd value of 2.89 × 10-5 M. Binding of kaempferol with HMGB1 led to the intrinsic fluorescence quenching and modest secondary structure change of HMGB1 supported by fluorescence spectrometry and circular dichroism (CD). Using dynamic light scattering (DLS), it was found that kaempferol induced the aggregation of HMGB1 protein complex to form larger particles. On HMGB1-activated RAW264.7 cells, kaempferol co-incubation exhibited a remarkable inhibitory effect on nitric oxide (NO) release with an IC50 value of 5.02 µM, which was lower than that of quercetin. In silico, kaempferol binds to HMGB1 mainly through hydrogen bonds and hydrophobic forces. Collectively, our study showed kaempferol as a potential HMGB1 inhibitor, mainly acting by direct binding to HMGB1 and inducing its conformational changes, which provides clues for the treatment of chronic inflammation by kaempferol.
Subject(s)
HMGB1 Protein , Humans , HMGB1 Protein/chemistry , HMGB1 Protein/metabolism , Kaempferols , Circular Dichroism , Spectrometry, Fluorescence , Inflammation , Molecular Docking Simulation , Protein BindingABSTRACT
In this study, several kinds of metal chloride hydrates were added into NADESs (natural deep eutectic solvents) and a series of three constituent-NADESs (3c-NADESs) were successfully developed. The results suggested that the addition of metal chloride hydrates can significantly enhance the solubility of starch, such as, the solubility in MgCl2-CGly-1 is 90.12 ± 3.49 g/100 g, which is 65 times higher than C-Gly (choline chloride-glycerol) (1.38 ± 0.65 g/100 g). The density functional calculation (DFT) suggested that a lower chloride occupancy of 3c-NADESs can provide more chloride ions used for the formation of hydrogen-bonding interaction with starch. Moreover, the molecular dynamic (MD) study demonstrates that Cl- may play a key role as "chisel" during the dissolution of starch, which can efficiently destroy the intra- and intermolecular hydrogen bonds (HOâ¯O) of starch, allowed the penetration of other components and prevent the recovery crystal of starch.
Subject(s)
Glycerol , Starch , Anions , Chlorides , Choline/chemistry , Deep Eutectic Solvents , Glycerol/chemistry , Hydrogen , Solvents/chemistry , Starch/chemistryABSTRACT
Objective: Fasting is considered to be a food structure that can improve body health. Several randomized clinical trials (RCTs) have investigated the effects of fasting in patients with metabolic syndrome (MS). In this review, we performed a meta-analysis to assess the effects of fasting on patients with MS. Methods: Following PRISMA guidelines, a systematic literature search was conducted in PubMed, Embase, and Cochrane Central updated to September 2021. The quality evaluation and heterogeneity detection of the included research literature were carried out by Revman and Stata software through a random-effects model. Results: A total of 268 subjects were included. The pooled results revealed that fasting significantly reduced body weight (WMD: -2.48 kg, 95% CI: -3.22, -1.74), BMI (WMD = -2.72 cm; 95%CI: -4.04, -1.40 cm), body fat percent (WMD: -1.57%, 95%CI: -2.47, -0.68), insulin level (WMD: -2.45 mmol/L; 95%CI: -4.40, -0.49 mmol/L) and HOMA-IR (WMD:-0.65 mmol/L; 95%CI: -0.90, -0.41 mmol/L) in patients with MS, whereas had no effect on glucose, blood pressure and lipids profile. Conclusions: Our findings provide insights into the effect of fasting on the anthropometric outcomes, insulin resistance, and gut microbiota in MS.
ABSTRACT
As a new generation of green solvents, deep eutectic solvents (DESs) have been considered as a promising alternative to classical organic solvents and ionic liquids (ILs). DESs are normally formed by two or more components via various h-bonds interactions. Up to date, four types of DESs are found, namely, type I DESs (formed by MClx, namely FeCl2, AlCl3, ZnCl2, CuCl2 and AgCl et al., and quaternary ammonium salts); type II DESs (formed by metal chloride hydrates and quaternary ammonium salts); type III DESs (formed by choline chlorides and different kinds of HBDs) and type IV DESs (formed by salts of transition metals and urea). DESs share many advantages, such as low vapor pressure, good substrate solubility and thermal stability, with ILs, and offering a high potential to be the medium of biocatalysis reactions. In this case, this paper reviews the applications of DESs in enzymatic reactions. Lipases are the most widely used enzyme in DESs systems as their versatile applications in various reactions and robustness. Interestingly, DESs can improve the efficiency of these reactions via enhancing the substrates solubility and the activity and stability of enzymes. Therefore, the directed engineering of DESs for special reactions such as degradation of polymers in high temperature or strong acid-base conditions will be one of the future perspectives of the investigation DESs.
Subject(s)
Ionic Liquids , Deep Eutectic Solvents , Ionic Liquids/chemistry , Quaternary Ammonium Compounds , Salts , Solvents/chemistryABSTRACT
Extraction technology can influence the vegetable oil functional quality. Polyphenols in rapeseed oil have been proved to be beneficial for cardiovascular health. In this study, we evaluated the effect of extraction methods on the functional quality of rapeseed oil from the perspective of phenolic compounds. The results showed that hot pressing produces the highest amount of phenolic compounds in rapeseed oil. Its most abundant phenolic compound, sinapine (9.18 µg g-1), showed the highest activity in inhibiting anaerobic choline metabolism with an EC50 value of 1.9 mM, whose downstream products are related to cardiovascular diseases. Molecular docking and molecular dynamics (MD) simulations revealed that sinapine exhibits good binding affinity toward CutC, and CutC-sinapine is a stable complex with fewer conformational fluctuations and similar tightness. Taken together, hot pressing can be considered the best extraction method for rapeseed oil from the perspective of phenolic compounds.