Search

Selfish genetic elements contribute to hybrid incompatibility and bias or drive their own transmission1,2. Chromosomal drive typically functions in asymmetric female meiosis, whereas gene drive is normally post-meiotic and typically found in males. Here, using single-molecule and single-pollen genome sequencing, we describe Teosinte Pollen Drive, an instance of gene drive in hybrids between maize (Zea mays ssp. mays) and teosinte mexicana (Z. mays ssp. mexicana) that depends on RNA interference (RNAi). 22-nucleotide small RNAs from a non-coding RNA hairpin in mexicana depend on Dicer-like 2 (Dcl2) and target Teosinte Drive Responder 1 (Tdr1), which encodes a lipase required for pollen viability. Dcl2, Tdr1 and the hairpin are in tight pseudolinkage on chromosome 5, but only when transmitted through the male. Introgression of mexicana into early cultivated maize is thought to have been critical to its geographical dispersal throughout the Americas3, and a tightly linked inversion in mexicana spans a major domestication sweep in modern maize4. A survey of maize traditional varieties and sympatric populations of teosinte mexicana reveals correlated patterns of admixture among unlinked genes required for RNAi on at least four chromosomes that are also subject to gene drive in pollen from synthetic hybrids. Teosinte Pollen Drive probably had a major role in maize domestication and diversification, and offers an explanation for the widespread abundance of self small RNAs in the germ lines of plants and animals.

We report a multi-ancestry genome-wide association study on liver cirrhosis and its associated endophenotypes, alanine aminotransferase (ALT) and γ-glutamyl transferase. Using data from 12 cohorts, including 18,265 cases with cirrhosis, 1,782,047 controls, up to 1 million individuals with liver function tests and a validation cohort of 21,689 cases and 617,729 controls, we identify and validate 14 risk associations for cirrhosis. Many variants are located near genes involved in hepatic lipid metabolism. One of these, PNPLA3 p.Ile148Met, interacts with alcohol intake, obesity and diabetes on the risk of cirrhosis and hepatocellular carcinoma (HCC). We develop a polygenic risk score that associates with the progression from cirrhosis to HCC. By focusing on prioritized genes from common variant analyses, we find that rare coding variants in GPAM associate with lower ALT, supporting GPAM as a potential target for therapeutic inhibition. In conclusion, this study provides insights into the genetic underpinnings of cirrhosis.

Adipose tissue is the site of long-term energy storage. During the fasting state, exercise, and cold exposure, the white adipose tissue mobilizes energy for peripheral tissues through lipolysis. The mobilization of lipids from white adipose tissue to the liver can lead to excess triglyceride accumulation and fatty liver disease. Although the white adipose tissue is known to release free fatty acids, a comprehensive analysis of lipids mobilized from white adipocytes in vivo has not been completed. In these studies, we provide a comprehensive quantitative analysis of the adipocyte-secreted lipidome and show that there is interorgan crosstalk with liver. Our analysis identifies multiple lipid classes released by adipocytes in response to activation of lipolysis. Time-dependent analysis of the serum lipidome showed that free fatty acids increase within 30 min of β3-adrenergic receptor activation and subsequently decrease, followed by a rise in serum triglycerides, liver triglycerides, and several ceramide species. The triglyceride composition of liver is enriched for linoleic acid despite higher concentrations of palmitate in the blood. To further validate that these findings were a specific consequence of lipolysis, we generated mice with conditional deletion of adipose tissue triglyceride lipase exclusively in adipocytes. This loss of in vivo adipocyte lipolysis prevented the rise in serum free fatty acids and hepatic triglycerides. Furthermore, conditioned media from adipocytes promotes lipid remodeling in hepatocytes with concomitant changes in genes/pathways mediating lipid utilization. Together, these data highlight critical role of adipocyte lipolysis in interorgan crosstalk between adipocytes and liver.

The mechanism that triggers the progressive dysregulation of cell functions, inflammation, and breakdown of tissues during aging is currently unknown. We propose here a previously unknown mechanism due to tissue autodigestion by the digestive enzymes. After synthesis in the pancreas, these powerful enzymes are activated and transported inside the lumen of the small intestine to which they are compartmentalized by the mucin/epithelial barrier. We hypothesize that this barrier leaks active digestive enzymes (e.g. during meals) and leads to their accumulation in tissues outside the gastrointestinal tract. Using immune-histochemistry we provide evidence in young (4 months) and old (24 months) rats for significant accumulation of pancreatic trypsin, elastase, lipase, and amylase in peripheral organs, including liver, lung, heart, kidney, brain, and skin. The mucin layer density on the small intestine barrier is attenuated in the old and trypsin leaks across the tip region of intestinal villi with depleted mucin. The accumulation of digestive enzymes is accompanied in the same tissues of the old by damage to collagen, as detected with collagen fragment hybridizing peptides. We provide evidence that the hyperglycemia in the old is accompanied by proteolytic cleavage of the extracellular domain of the insulin receptor. Blockade of pancreatic trypsin in the old by a two-week oral treatment with a serine protease inhibitor (tranexamic acid) serves to significantly reduce trypsin accumulation in organs outside the intestine, collagen damage, as well as hyperglycemia and insulin receptor cleavage. These results support the hypothesis that the breakdown of tissues in aging is due to autodigestion and a side-effect of the fundamental requirement for digestion.

Lipases have drawn significant attention due to their crucial roles across various industries, including oil processing, food, medicine, and daily chemicals. Nevertheless, their catalytic efficiency is susceptible to fluctuations in external environmental conditions, which remains a major barrier to their broader application. In this research, chiral hydrogel microspheres (HMSs) are developed by incorporating L/D‐Co3O4 nanoparticles (NPs) into the synthetic process of HMSs, which are discovered to enhance the catalytic performance of lipases. The improved catalytic activity of lipases is observed to be influenced by the chiral environment of L/D‐Co3O4‐HMSs. Specifically, when 2 wt.% lipases are encapsulated in L‐Co3O4‐HMSs containing 10 wt.% L‐Co3O4 NPs, their catalytic activity is 2.11 times higher than when encapsulated in D‐Co3O4‐HMSs, resulting in a 2.62‐fold increase in catalytic activity compared to free lipase. Moreover, the L‐Lip‐HMS3, which contained 2 wt.% lipases and 10 wt.% L‐Co3O4 NPs, exhibited superior inhibitory capability over D‐Lip‐HMS3 in differentiating fibroblast mouse cells into adipocytes, owing to its enhanced catalytic capabilities. This study not only highlights the importance of chirality in improving the catalytic performance of natural enzymes but also provides a new perspective on developing catalytic systems that can endow natural enzymes with higher catalytic performances. [ABSTRACT FROM AUTHOR]

Introduction: The immune-mediated destruction of insulin-producing β-cells characterizes type 1 diabetes. Nevertheless, exocrine pancreatic enzymes, including amylase, lipase, and trypsin, are also significantly reduced in type 1 diabetes. With an immunotherapy now approved to treat early-stage type 1 diabetes, biomarkers to delineate response to treatment are needed. No study has yet evaluated whether serum exocrine pancreatic enzymes could delineate immunotherapy responders and non-responders. Methods: In this novel study, we sought to identify longitudinal trends in the most commonly measured circulating exocrine enzymes before and after treatment with anti-thymocyte globulin (ATG) and pegylated granulocyte colony-stimulating factor (GCSF) in individuals with new-onset type 1 diabetes (n=34). We defined response to immunotherapy as participants with at least 60% of baseline area under the curve (AUC) C-peptide levels after a 2-hour mixed meal tolerance test (MMTT) at two years post-treatment. In the overall study (n=89), 42% of treated and 17% of placebo participants met this definition. Due to constraints of sample availability, we compared longitudinal serum amylase, lipase, and trypsin levels in a subset of responders to therapy (n=4-6), placebo "responders" (n=2), treated non-responders (n=16), and placebo non-responders (n=10). Results: There were no differences in amylase levels between groups at baseline or six months post-treatment. Baseline levels of lipase and trypsin tended to be lower in responders; however, these variations were not significant in this small study sample. Lipase and trypsin improved to 115% of baseline in responders to immunotherapy six months after treatment and declined to 80-90% of baseline in non-responders and placebo participants (p=0.03). This difference was not present before the six-month time point. Discussion: Our findings provide preliminary evidence that the exocrine pancreatic enzymes lipase and trypsin may be useful biomarkers of response to immunotherapy in type 1 diabetes. Further studies with larger numbers of participants are warranted. [ABSTRACT FROM AUTHOR]

Polyethylene terephthalate (PET) pollution is a global challenge. Advancing the bioprospecting of PET‐degrading enzymes through metagenomics and using computational and functional methods to identify key positions influencing the catalytic rate and selectivity are part of the solution. Here, we report PETase activity in the metagenomic lipase LipMRD9, which exhibits peak activity at 30 °C and pH 9.0 and has a denaturation temperature of 42 °C. In addition to acting on long‐chain triglycerides (up to ∼13 units (U)/mg, pH 8.0, 30 °C) and a wide range of 34 other esters (up to ∼228 U/g), LipMRD9 hydrolyses mono(2‐hydroxyethyl) terephthalate (∼57 U/g) and bis(2‐hydroxyethyl) terephthalate (∼131 U/g). It also efficiently deconstructs GoodFellow amorphous submicro‐ and nanosized PET particles (∼984/2238 μM degradation products at 30/40 °C, pH 7.0, 21.5 h) and films (∼112/198 μM degradation products at 30/40 °C, pH 7.0, 7 days). Through molecular modelling and experimental analysis, the active site of LipMRD9 was revealed, identifying a key residue contributing to its PETase activity compared with those of its closest homologues. This residue plays a crucial role in determining the distinct profiles of degradation products from PET hydrolysis and should be studied in other PETases for its influence on the catalytic process. [ABSTRACT FROM AUTHOR]

Generally, an esterase lipase enzyme can hydrolyze specific substrates called esters in an aqueous solution. Herein, we investigate how a G‐quadruplex self‐assembly affects the hydrolysis equilibrium in reverse. The biocatalyst, lipase, activates the individual building‐blocks through fuel consumption, causing them to undergo a higher degree of self‐organization into nanofibers within spheres. We have synthesized five peptide‐lipid‐conjugated guanine base functionalized molecules to explore how the equilibrium can be shifted through reverse hydrolysis. Among these, NAC5 self‐assembled into a G‐quadruplex structure which has been confirmed by various spectroscopic techniques. The wide‐angle powder XRD, ThT dye binding assay and circular dichroism study is carried out to support the presence of the G‐quadruplex structure. The biocatalytic formation of nanofibers enclosed spheres is analyzed using CLSM, FE‐SEM and HR‐TEM experiments. Additionally, we assess the biocompatibility of the enzyme fueled dissipative self‐assembled fibers enclosed spheres, as they have potential applications as a biomaterial in protocells. MTT assay is performed to check the cytotoxicity of G‐quadruplex hydrogel, using HEK 293 and McCoy cell lines for viability assessment. Finally, the utility of the novel NAC5 hydrogel as a wound repairing biomaterial is demonstrated by cell migration experiment in a scratch assay. [ABSTRACT FROM AUTHOR]

Leather industry is traditionally characterized by the use of large amounts of chemical agents, some of which are toxic to human health and the environment. However, during the last years, many efforts have been made with the aim of successfully implement enzymes as agents for different leather production stages. The lipopeptides produced by the Bacillus spp. genus have excellent surfactants and antibacterial properties and may collaborate in the soaking stage of leather processing as well as in leather preservation. Moreover, Bacillus sp. proteases and lipopeptides can be co-produced in one culture medium, saving the production costs. In the present work, a screening of enzymatic activities was performed on 11 strains of the Bacillus sp. genus that have been isolated from samples of an artisan tannery from Salta, Argentina. In particular, the ability of B. amyloliquefaciens B65 to degrade α-type (nails, hair, wool) and β-type (feathers) keratin was demonstrated by scanning electron microscopy (SEM). The co-production of proteases, keratinases, glycosidases, and lipopeptides of this strain was conducted at 37 °C in mineral media supplemented with chicken feathers. In these nutrient-deficient media, the strain secreted amylases, pectinases, proteases, keratinases, and collagenases. A MALDI-TOF study also revealed that the strains secreted homologues of kurstakins, iturins, surfactins, and fengycines lipopeptides families. Therefore, B. amyloliquefaciens B65 presents great industrial potential applications, not only for tanneries but also for other industries such as pharmaceuticals, food, textiles, and detergents, among others. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

The immobilization of enzymes increases their stability and allows their reuse, and bacterial cellulose (BC) is a material that can be used in this technique. This work aims to produce an enzymatic product to degrade oils and fats using BC as a matrix. Komagataeibacter hansenii bacteria produce BC membranes, and lipase is immobilized on the membranes by ex situ method. Then, the surface of the membranes is modified with zein, a hydrophobic corn protein. The membranes are characterized by TGA, FTIR, scanning electron microscopy (SEM) analysis and oil degradation test. TGA demonstrates higher stability for the membranes with lipase and zein. The FTIR spectrum of pure BC membrane and zein‐modified membrane are very similar because of the high zein coating. SEM analysis shows that zein‐modified membranes with lipase present smaller amounts of pores. Finally, using soy oil, lipase degrades oil even after immobilization during the degradation test. [ABSTRACT FROM AUTHOR]

The spillage of petroleum hydrocarbons, one of the most versatile energy resources, leads to disastrous environmental pollution. The present study aims to degrade oil using enzymes from bacterial strains. A total of 39 bacteria were isolated from six different soil samples collected from Ullal Beach, Mangalore, Karnataka, located at 12°52′N latitude and 74°49′E longitude, India. All 39 bacterial isolates were screened for the production of four industrially important extracellular enzymes. Among these isolates, ten showed the highest lipase production. These cultures were further screened for bio-surfactant assays, including oil displacement and drop collapse assay and Emulsification Index. EBPL0613-F2 exhibited the best reaction in crude oil degradation. A polyphasic taxonomical approach identified the crude oil-degrading bacterium EBPL0613-F2 as Bacillus licheniformis and submitted in NCBI and the Accession Number is PP059616. It was then cultivated in ocean water media with tween 20 and 1% crude oil as the sole carbon and energy source. The strain was screened for lipase quantitative and qualitative assay and the protein content was also estimated. The identified bacterial strain Bacillus licheniformis EBPL0613-F2 demonstrated moderate lipase activity, with 76 U/ml and 24 U/ml, respectively, after 48–72 h of incubation in the crude oil substrate. For Tween 20 substrates, it exhibited 36 U/ml and 34 U/ml, respectively. FTIR analysis was used to examine the properties of crude oil following the biodegradation. The results suggest that, EBPL0613-F2 recorded the highest degradation rate so this culture has the potential for use in the degradation of crude oil in a greener manner. [ABSTRACT FROM AUTHOR]

This study aimed to isolate, purify, and characterize a lipase from the gut symbiont Bacillus megaterium F25 (GenBank accession: MF597792) of the aquatic insect Rhantus suturalis, with a focus on its potential applications in biodiesel and food industries. Under optimized culture conditions, B. megaterium F25 could produce 583 U/L of lipase in shaking flask culture. The purified lipase (PL) exhibited a specific activity with 113.89 U/mg, and its molecular weight was determined as 34 kDa. The activity of PL was enhanced by methanol, ethanol, Tween‐80, Triton X‐100, Ca2+, and Mg2+, while β‐mercaptoethanol, EDTA, SDS, Fe2+, Mn2+, and Cu2+ were inhibitory. PL showed optimal activity and stability at neutral and slightly acidic pHs, as well as in a temperature range of 20°C–30°C. PL displayed strong hydrolytic activity toward plant oils and animal fats, indicating its potency for both the food industry and the remediation of oil‐contaminated environments. When tested as a catalyst, PL provided biodiesel production with a transesterification yield of 86.8% under optimized conditions (36 h reaction time, 4 mL enzyme solution, 30°C, pH 7.0, and waste cooking oil:methanol ratio of 10 mL/40 mL). This is the first report on the lipase‐producing potential of gut microbial symbionts of aquatic insects. Furthermore, B. megaterium lipase was tested for the first time as a biocatalyst for biodiesel production. [ABSTRACT FROM AUTHOR]

Lipase inhibitors are used in the treatment of candidiasis, obesity, and acne problems. Therefore, the investigation of new natural lipase inhibitors has generated great interest. Juniperus phoenicea is a small Mediterranean tree considered an important medicinal plant. Through this work, we investigated the composition and inhibition effect of J. phoenicea extract on Candida rugosa and human lipases; and we analyzed the interactions between detected compounds and lipases using molecular docking, ADME-T, and dynamic studies. We extracted the secondary metabolites from the plant aerial parts and tested their activities against lipase. We examined major components of J. phoenicea , using Autodock vina for molecular docking, Desmond from Schrodinger suite 2021–1 for dynamics, and evaluating its drug-likeness and toxicity properties using ADMET webserver. We found that the IC 50 values of ethyl acetate and methanol extracts are 1.33±0.10 and 1.731 mg/mL. Using HPLC quantitative analysis we identified in ethyl acetate extract the following phenolic compounds gallic acid, rutin, apigenin-7-O-glucoside, cinnamic acid, and quercetin. The complex apigenin-7-O-glucoside-lipase is stabilized by four hydrogen bonds and hydrophobic interactions, and the binding energy equals -10 Kcal/mol , which is better than the interactions saved for orlistat. Dynamic Simulation demonstrated better stability in the ligand-protein complex apigenin-7-O-glucoside-1lpb within 100 ns than the orlistat-1lpb complex. This study is described in this work for the first time. The results indicated that apigenin-7-O-glucoside from J. phoenicea L could be a good choice to develop a new drug candidate against candidiasis, obesity, and other lipase-related diseases. [Display omitted] ● Phytochemical profiling of Juniperus phoenicea metabolites using LC-MS/MS. ● Apigenin-7-O-glucoside inhibits lipases. ● In silico methods confirm apigenin-glucoside's strong affinity towards lipase. [ABSTRACT FROM AUTHOR]

BACKGROUND: An increasing incidence of metabolic disorders emphasizes the need to explore natural treatments. Spirulina, a microalga with a rich nutrient profile, offers a promising solution for obesity, diabetes, and inflammation. This study provides a meticulous analysis of spirulina powder, evaluating its physicochemical attributes and technofunctional properties through the use of advanced analytical techniques. RESULTS: Spirulina powder demonstrated strong flowability, substantial water and oil absorption capacity, and moderate foaming characteristics. The ethanolic extract of spirulina was found to be a repository of phenolic (6.93 mg GAE/g) and flavonoid (7.17 mg QE/g) compounds, manifesting considerable antioxidant activity with a 58.49 g kg−1 inhibition of 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) radicals. The extract also exhibited pronounced inhibitory effects on lipase and amylase enzymes, with inhibition percentages of 72.05 g kg−1 and 70.28 g kg−1, respectively, and displayed a glucose retention capacity of 1.28 mg dL−1 (68.52 g kg−1) in a dialysis membrane assay. These results suggest its efficacy in modulating obesity and glycemic control. The powder also showed a potent anti‐inflammatory response by mitigating protein denaturation. CONCLUSION: Spirulina powder is a potent natural agent with multiple health benefits, meriting its incorporation into functional foods. It could be suitable for application in the food industry, offering a natural strategy to combat metabolic diseases. This research adds to the scientific literature on spirulina, paving the way for future research into its utilization. © 2024 The Author(s). Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Dioctyl sebacate is a long carbon chain dibasic acid ester with methylene as the main body. It is widely used in plasticizers because of its good cold resistance and high viscosity. And it has excellent properties of non-toxicity and easy biodegradation, so it can be used as a potential new green bio-based plasticizer. At present, most of the preparation methods of dioctyl sebacate are chemical methods, which have many by-products and cause environmental pollution. In this article, cellulose microspheres were used as a carrier to immobilize Candida antarctica lipase B (CALB) to catalyse the esterification of sebacic acid and n-octanol to prepare dioctyl sebacate. Through single factor experiments, the lipase immobilized on cellulose microspheres was optimized to determine the best process conditions: add 500 µL CALB to the erlenmeyer flask, and then add 0.02 mol/L PBS buffer (pH 8.0). After being prepared into a 5 mL system, 0.1 g of cellulose microspheres were added as a carrier and reacted for 3 h at 35 °C and 180 r/min. Added 0.5 vt% polyethylene glycol diglycidyl ether (PEGDEG) to the system for crosslinking. The final immobilization rate of lipase immobilized on cellulose microspheres was 80.06%, and the enzyme activity was 288.07 U/g. Using the cellulose-immobilized lipase as a catalyst, in the toluene system, the molar ratio of n (sebacic acid)/n (n-octanol) substrate was 1:3.5, the amount of immobilized enzyme was 0.04 g, 4 Å molecular sieve 1.5 g, 40 °C, and 150 r/min for 30 h, the conversion rate of dioctyl sebacate was 76.45%. [ABSTRACT FROM AUTHOR]

This study investigates the transesterification of isoflavones puerarin and β-D-fructofuranosyl-(2→6)-puerarin to enhance their lipophilicity for specific pharmacological applications. The process achieved high yields (80-100%) in the isoflavones conversion when commercial lipases from Candida antarctica (CALB) and Thermomyces lanuginosus (TL IM) were used. The acylation patterns between CALB and TL IM varied depending on the substrate; both enzymes yielded principally monoacylated products from puerarin and β-D-fructofuranosyl-(2→6)-puerarin. However, TL IM also produced di- and triacylated derivatives of β-D-fructofuranosyl-(2→6)-puerarin in substantial amounts. Structural characterization by NMR identified puerarin-6ʹʹ-O-laurate and β-D-fructofuranosyl-(2→6)-puerarin-6ʹʹʹ-O-laurate as the primary products in CALB and TL IM reactions. These acyl derivatives presented improved lipophilicity (Log P from −1.0 − 0.16 to 3.26 − 3.58) and antioxidant activity (67.2-97.3 to 102.5-131.4 µM TE/mmol). Therefore, these compounds have potential pharmacological applications. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

Aims: Acute heart failure (AHF) is associated with end‐organ dysfunction. The effect of AHF on the pancreas has not been studied. We aim to evaluate serum markers of pancreatic damage during hospitalization for AHF. Methods and results: In data from the Pragmatic Urinary Sodium‐based treatment algoritHm in Acute Heart Failure (PUSH‐AHF) study, amylase and lipase values were extracted from available serum samples at baseline, and at 24 and 72 h after hospitalization. The differences between pancreatic enzymes between timepoints were evaluated using the Friedman test. Associations with N‐terminal pro‐B‐type natriuretic peptide (NT‐proBNP) were tested using linear regression analysis. The study population consisted of 274 patients. Mean age was 73 ± 11 years, and 117 (43%) were women. Mean left ventricular ejection fraction (LVEF) was 38 ± 14%; 53 (19%) patients had HF with a preserved LVEF (≥50%). At baseline, median amylase and lipase were within normal range (47 [33–63] U/L and 30 [21–44] U/L, respectively). Both enzymes significantly increased in the first 72 h (P‐value for trend <0.001); mean change was 9 ± 22 U/L for amylase, and 10 ± 22 U/L for lipase. Moreover, NT‐proBNP at baseline showed a positive correlation with mean change in pancreatic enzymes in 72 h (P = 0.02 for amylase and P = 0.006 for lipase). Conclusion: Patients admitted for AHF exhibited a significant increase in serum values of pancreatic enzymes in the first 72 h, suggesting that an episode of AHF affects the pancreatic tissue. This rise in pancreatic enzymes was associated with HF severity, as reflected by NT‐proBNP. [ABSTRACT FROM AUTHOR]

Sono-enzymatic biodiesel synthesis from different feedstocks has been significantly investigated in recent years, which reports the impact of ultrasound (US) on the structure of lipases. However, the links between alteration in the structure of lipases due to US and its activity enhancement have yet to be established. This study reveals the molecular mechanism of US-induced enhancement of lipase-catalyzed reactions in biodiesel synthesis. Using molecular simulations, we first analyzed the 3D structures and amino acid (aa) composition of the binding pockets of two lipases, viz. CALB and TLL. Next, docking analysis of different ligands (substrates and products of the reactions) with lipases was performed to reveal the interacting residues. We identified the US-induced alteration in the secondary structure of lipase from previous reports. Our analysis revealed that most binding pockets are located in the α-helix and random coil motifs, and binding interactions are mainly hydrogen bonding and hydrophobic interactions. We observed a rise in α-helix and random coils of lipase with sonication. The net effect of sonication is the widening of the catalytic cavity, thus easy substrate accessibility to the active site. Thus, enhanced enzymatic activity is manifested as faster kinetics of the reactions with higher yields. [ABSTRACT FROM AUTHOR]

The Pacific fat sleeper, Dormitator latifrons, is an omnivorous freshwater fish that primarily feeds on detritus. Our understanding of the digestive physiology of this species still needs to be completed, particularly concerning the characterization of its digestive enzymes. This information is crucial in guiding the design of diets that promote optimal digestion of this species, which has the potential for aquaculture. Thus, this study aimed to optimize enzymatic methods and characterize the digestive enzymes of the digestive tract regions: anterior region (AR), middle region (MR), posterior region (PR), and hepatopancreas (HP). Total acid protease, total alkaline protease, amylase, and lipase activities were measured. The enzymatic methods were optimized at an eco-physiological temperature of 25 °C based on extract volume, extract dilution, incubation time, pH, and CaCl2 concentration to determine specific activity (U/mg of protein). The optimal pH for acid protease (AR) was pH 2.0; while for alkaline protease, the optimal pH was between 7.5 and 11.0. For AR, chymotrypsin was pH 7.0; for the remaining digestive regions, it was pH 9.0–11.0. The optimal pH for amylase was 6.0 to 7.5 (all regions), and for lipase, it was between 7.0 and 11.0, with two apparent in vitro activity peaks (PR). HP experimental samples showed low or no chymotrypsin, amylase, and lipase activity. CaCl2 did not affect enzyme activity except for amylase and lipase (only in PR and HP, respectively). The acid proteolytic activity (pH 2.0) found in AR and the proteolytic inhibition by pepstatin suggest the presence of a stomach. [ABSTRACT FROM AUTHOR]

Graphene oxide (GO) is the most sought-after constituent in developing solutions for problems across biosensing and diagnostics to implants, automotive to space missions, and manufacturing to waste rehabilitation. GO is costly if procured externally and time-intensive if produced by conventional processes. In this paper, GO is synthesized using an efficient, cost-effective method at a much faster rate. The quality of GO is at par with the standards, and techno-economic analysis reveals that the proposed method took 20–25% less time for synthesis than practised methods. The proposed method is profitable, and the payback period is around 6 to 7 months. Lipase, successfully immobilized on synthesized GO, showed four times free enzyme activity with 75% enzyme loading. This work indicates that the GO from the proposed method, on ultrasonication generates nanometric GO (nano-GO) that are highly biocompatible for lipase-immobilized biosensor applications. The biorecognition module fabricated using GO showed a response time of under 10 min and compatibility with samples with pH between 6 and 9 with a temperature range of 20–45 °C. The biosensor showed a 5.28 µg/mL limit of detection (LOD) and a 1 U/µg/mL sensitivity with a limit of quantitation (LOQ) of 5–250 µg/mL. Retention of 60% activity when stored at 10 °C after ten days was observed. The biorecognition module showed resilience to up to 30 mg/L of metal interferents and contaminants. The biorecognition was found to be significant for colorimetry-based paper biosensing. A colorimetric biorecognition module to detect triglyceride (TG) was designed using graphene oxide (GO) nanomaterial, synthesized by modifying previously reported methods. The method reported in the study is 20 to 25% fast and simultaneously provides an excellent quality product. The proposed method was 200% more economical. It was observed that as part of the solid matrix, the GO NPs are an excellent candidate for lipase-immobilized colorimetric biosensors for triglyceride detection. The matrix met the necessary benchmarks of a colorimetric biosensor. [ABSTRACT FROM AUTHOR]

Lipids perform a diverse and unique array of functions in insects. Lipases are key enzymes in lipid metabolism, and their metabolic products are crucial for development and reproduction of insects. Here, a total of 110 lipase genes were identified in the genome of Spodoptera frugiperda. Cluster analysis indicated that neutral lipases constitute the majority of lipases. Tissue expression profile analysis displayed that most lipase genes were highly expressed in the larval gut of S. frugiperda. Some lipases exhibited a diet‐specific expression pattern, which implied their roles in host adaptation. Key domain analysis proved that none of the neutral lipases highly expressed in the gut has an integrated lid domain, while most lipases highly expressed in the fat body contained both the integrated lid domain and β9 loop, indicating the activity loss of neutral lipases in guts. The assay of triacylglycerol (TAG) hydrolytic activity confirmed that the gut had the lowest activity when compared to that of fat body and epidermis. Interestingly, the opposite TAG hydrolytic activity trends across mating were observed between adult males and females, implying that lipase played different roles in the reproduction of both sexes. In conclusion, neutral lipases lost TAG hydrolytic activity in S. frugiperda guts, but retained the activity in fat body. Neutral lipases would play vital roles in many physiological processes in insects, especially in insect reproduction, which provides palpable targets for novel insecticide development to control insect population growth. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

The oleaginous yeast Lipomyces starkeyi is an attractive industrial yeast that can accumulate high amounts of intracellular lipids. Identification of genes involved in lipid accumulation contributes not only to elucidating the lipid accumulation mechanism but also to breeding industrially useful high lipid-producing strains. In this study, the suppressed lipid accumulation-related gene (SLA1) was identified as the causative gene of the sr22 mutant with decreased lipid productivity. Suppressed lipid accumulation-related gene mutation reduced gene expression in lipid biosynthesis and increased gene expression in β-oxidation. Our results suggest that SLA1 mutation may leads to decreased lipid productivity. Suppressed lipid accumulation-related gene deletion also exhibited decreased gene expression in β-oxidation and increased lipid accumulation, suggesting that SLA1 deletion is a useful tool to improve lipid accumulation in L. starkeyi for industrialization. [ABSTRACT FROM AUTHOR]

Background: Aspartame is a low-calorie artificial non-sugar sweetener and is commonly used as a sugar substitute in foods and beverages. Pancreas has a vital role in carbohydrate metabolism. The aim of the study was to study the effect of aspartame on the structure of pancreas. Methods: Eighteen albino Wistar rats (200-250gm) were divided into three groups; control group, aspartame-treated group, was treated with aspartame (250 mg/kg/day) for six months and withdrawal group: was treated with aspartame (250 mg/kg/day) for six months then left without treatment for another month. Serum amylase and lipase were measured, and histological study of the pancreas was conducted. Results: histopathological changes were detected in both pancreatic acini and islets of Langerhans, increased collagen deposition around the acini and blood vessels. Additionally, aspartame supplementation resulted in elevated levels of serum amylase and lipase. Upon withdrawal of aspartame, an obvious improvement was noticed in the withdrawal group in comparison with the aspartame-treated group. Conclusions: Aspartame produces degenerative changes in the pancreas of the rats and causes uprising of serum pancreatic enzymes. Withdrawal of aspartame results in partial restoration of the histological structure of the pancreas. From these results, it is recommended to spot a light on the dangerous impacts of the usage of aspartame in clinical studies. [ABSTRACT FROM AUTHOR]

Streptomyces sp. A3301, which produces lipase isolated by Panyachanakul et al. [1]. This optimization was done for the subsequent purification and characterization of the biological lipase produced by the isolate. The results showed that the strain produced lipase with a maximum activity of 321 U/mL using the optimal medium and conditions (1.5% (w/v) xylose and 2% (w/v) yeast extract, pH 7.0 at 30 °C, 150 rpm for 3 days). The specific activity of the purified lipase was 27,000 U/mg, which was 544 times the pre-purification level, based on hydrophobic chromatography. After ion-exchange chromatography, the specific activity was 5,600 U/mg, which was 113 times the pre-purification level, with a single-peak purification profile. The purified lipase had a single band based on SDS-PAGE analysis and the molecular mass was 45 kDa. The optimum temperature and thermo-stability of A3301 lipase were 60 and 30 - 55 °C, respectively. The optimum pH of the purified enzyme was pH 9.0, and the enzyme was stable in the pH range of 8.0 - 9.0. The purified lipase was stable in acetone, chloroform and toluene, with a high relative activity of 63 - 76%. The immobilized strain was then applied to oily-wastewater treatment. The strain can remove oil and grease in synthetic wastewater containing oil at 1 - 3% (v/v), with removal rates of 100, 99.82 and 99.68%, respectively, after incubation for 6 days. It was then applied to oily-wastewater treatment from a restaurant, achieving the highest degradation rates of 98.53% after treatment for 6 days. In addition, it also affected the Biochemical Oxygen Demand (BOD) and Chemical Oxygen Demand (COD) values decreasing. [ABSTRACT FROM AUTHOR]

The thermo-solvent-tolerant lipase-producing actinomycete, Streptomyces sp. A3301, was utilized as a biocatalyst for poly (lactic acid) or PLA polymerization. The study aimed to optimize lipase immobilization conditions, characterize the immobilized lipase and apply it for PLA polymerization. The results showed using a sponge as the immobilizing matrix was the most effective method, achieving a maximum activity of 277 U/g of sponge. The optimal sponge size was determined to be 0.125 cm³ and pre-soaking the sponge in 0.1 M phosphate buffer at pH 7.0 for 24 h before use proved advantageous. Immobilization significantly enhanced the thermo-stability of the enzyme, with a relative activity ranging from 140 to 190% within the temperature range of 30 to 60 °C. In contrast, the crude lipase exhibited thermo-stability only within the 30 - 50 °C range. The immobilized lipase demonstrated stability under PLA polymerization conditions, which involved a reaction mixture containing toluene and lactic acid and performed at 60 °C for 8 h. The immobilized lipase maintained its activity under this condition for 5 h, retaining a relative activity of 230%, which was 1.2 times higher than the activity of the crude lipase. When the immobilized lipase was used in PLA polymerization, the resulting PLA product exhibited a molecular weight of 5,333 ± 0.02 Da, and the degree of polymerization was approximately 72. These findings underscore the potential of the immobilization technique to enhance lipase activity for PLA polymerization. [ABSTRACT FROM AUTHOR]

Lipase, a type of enzyme that decomposes and synthesizes triglycerides, plays an important role in lipid processing. In this study, a heat-resisting lipase gene (lip4) from Thermomyces lanuginosus was subcloned into the pPICZαA vector and then transformed into Pichia pastoris X33. The recombinant yeast cell concentration reached the maximum (119.5 g/L) at 144 h, and the lipase (Lip4) activity reached the maximum (3900 U/mL) at 168 h in 10 L bioreactor. Through bioinformatics analysis, S168, as the key site of Lip4, participated in the formation of the catalytic triads S168-D223-H280 and G166-H167-S168-L169-G170. Furthermore, S168 and seven conserved amino acids of G104/288, S105, A195, P196, V225 and I287 constitute the active center of Lip4. Specifically, the structure modeling showed two α-helices of the lid domain, outside the active pocket domain, controlling the entry of the substrate on Lip4. The potential glycosylation of Asn-33 may be involved in exhibiting the high stable temperature for lipase activity. Therefore, the eukaryotic system was constructed to express Lip4 efficiently, and the amino acid sites related to the catalytic efficiency of Lip4 were clarified, providing a new way for its subsequent property research and industrial application. [ABSTRACT FROM AUTHOR]

The use of enzymes or microorganisms for the synthesis of aroma compounds is a valuable strategy to meet the growing consumers' demand for natural products. Short-to-medium chain esters are widely used in the industry to provide fruity and floral flavors and fragrances to foods, cosmetics and pharmaceutical products. We present an extensive bibliometric analysis of the literature between 2000 and 2023 dealing with the biotechnological synthesis of aroma esters based on the review of 644 scientific documents retrieved from the Scopus database. The VOSviewer software was applied to analyze the bibliometric indicators of quantity and quality. The results showed the strategic distribution map of the different journals and countries where research groups developed this topic. It became evident that the research focused mainly on isoamyl acetate, 2-phenylethyl acetate and other acetate esters. We review recent progress regarding native microorganisms and recombinant enzymes that produce esters by esterification, Baeyer-Villiger oxidation, alcohol acylation and hemiacetal dehydrogenation. As a concluding remark, it is worth mentioning that lipases are the most frequently reported biocatalysts for the synthesis of aroma esters but the use of other enzymes has grown significantly in the last years, especially as part of cascades or modified metabolic pathways. • Short-to-medium chain esters are molecules with fruity and floral fragrances. • Aroma esters are used in foods, cosmetics, cleaning and pharmaceutical products. • Lipases, acyltransferases and Baeyer-Villiger monooxygenases can produce esters. • Biotechnological synthesis of aroma esters has the potential to become competitive. [ABSTRACT FROM AUTHOR]

Vanillyl alcohol (VA) possesses potent antioxidant activity, yet its applicability is hindered by its limited solubility in emulsions or non-polar organic solvents. Conversely, long-chain polyunsaturated fatty acids exhibit antibacterial properties. The combination of these compounds offers the prospect of developing novel phenolic lipid compounds with dual antioxidant and antibacterial activities, alongside enhanced solubility capabilities. In this investigation, linolenic acid vanillyl ester (LAVE) was synthesized from VA and linseed oil (LO) through a transesterification reaction employing immobilized lipase. Optimization of LAVE production was achieved by varying reaction temperature, substrate concentration, and reaction time. LAVE demonstrated efficacy in scavenging both 2,2-diphenyl-1-picryhydrazyl and 2,2'-azino-bis (3-ethylbenthiazoline-6-sulphonic acid) radicals in organic solvents. Antioxidant testing via lipid oxidation analysis revealed that LAVE, when distributed within emulsions, effectively impeded the formation of conjugated dienes and conjugated trienes. Furthermore, LAVE exhibited antibacterial activity against four strains of spoilage bacteria: Bacillus subtilis, Bacillus coagulans, Pseudomonas fluorescens, and Alcaligenes faecalis. Zeta potential analysis substantiated the binding of LAVE to the bacterial cell surface. Propidium iodide uptake assay and fluorescence microscopy further elucidated that LAVE induces cell lysis by augmenting membrane permeability. [ABSTRACT FROM AUTHOR]

Copyright of Acta Materiae Compositae Sinica is the property of Acta Materiea Compositae Sinica 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 immobilization of enzymes, especially lipases, presents a significant challenge in contemporary biotechnology due to their wide-ranging application in industrial processes. Given the array of available techniques for enzyme immobilization, this study aimed to immobilize Candida antarctica B (CALB) lipase within silica xerogel and sonogel matrices obtained through the sol–gel technique. Polyethylene glycol (PEG) was incorporated as an additive, with tetramethylorthosilicate (TMOS) serving as the silica precursor. This study assessed the operational stability, storage stability, and thermal properties of the resulting supports. Results revealed that both sonogel and xerogel supports, supplemented with PEG, maintained storage stability above 50% throughout a 365-day period. Moreover, operational stability tests demonstrated that the xerogel support could be reused up to 21 times, while the sonogel support exhibited 10 reuses. Thermal analysis further highlighted a reduction in the deactivation constant and an elongation of the half-life time for both supports. These observations suggest that the supports effectively shield the enzyme from thermal inactivation. Overall, these findings underscore the potential utility of PEG-enhanced sonogel and xerogel supports in various industrial enzyme applications, providing valuable insights into their operational, storage, and thermal stability. [ABSTRACT FROM AUTHOR]

Biodiesel generated from oils and fats composed of fatty acid alkyl esters is a potential substitution for fossil fuels, gaining attention as the demand for sustainable energy grows. Enzymatic transesterification has emerged as a promising method for biodiesel production due to the low energy required, easy glycerol recovery and compatibility with various feedstocks. This method also offers high specificity and operates under mild reaction conditions. However, limitations such as enzyme production cost, low product yield, and low stability under harsh conditions, have hindered the progress of biocatalysis. Protein engineering has emerged as an important strategy to overcome these limitations, particularly through rational design. Rational design approaches are advantageous in lipase engineering, due to accessible experimental tools and existing knowledge of lipase structure and function. Site-directed mutagenesis has been applied to improve stability, substrate specificity, methanol tolerance, and catalytic efficiency of lipase by introducing molecular interactions like hydrogen bonds and disulfide bridges as well as improved lid flexibility by mutations at the lid or lid swapping. This targeted approach allows for the precise modification of amino acid residues, optimizing lipase for better performance, which is crucial for efficient biodiesel production. [ABSTRACT FROM AUTHOR]

This work attempts to achieve the enrichment of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in acylglycerols as well as biodiesel production by investigating the performance of various lipases in ethanolysis. The ethanolysis activities of five immobilized lipases in decreasing order were as follows: Lipozyme TL IM, Novozym 40086/Lipozyme RM IM, Novozym 435 and Rhizopus oryzae lipase immobilized on polypropylene (RO PP). EPA could be enriched to a certain content by Lipozyme TL IM, Novozym 40086, Lipozyme RM IM, and RO PP. The enrichment of DHA was achieved well by those four sn‐1,3 regioselective lipases, and DHA contents in acylglycerols were the highest when Lipozyme TL IM and Novozym 40086 were used, reaching 2.87‐fold and 2.81‐fold of the initial content. However, Novozym 435 could not enrich EPA and DHA effectively. Fatty acid ethyl esters produced in this work contained abundant palmitic acid and palmitoleic acid, which could be ideal biodiesel considering their chain length. The competitive factors of five lipases towards DHA were all significantly higher than those towards EPA. When Lipozyme TL IM and Novozym 40086 achieved the maximum DHA contents, their DHA recoveries in acylglycerols reached 91.87% and 89.00%, respectively. The DHA recoveries were all significantly higher than the corresponding EPA recoveries in the reactions catalyzed by five lipases. Moreover, Lipozyme TL IM could be a potential lipase for the separation of EPA and DHA. This study may promote the full use of fish oil and broaden the application of lipases. [ABSTRACT FROM AUTHOR]

Copyright of Wiener Medizinische Wochenschrift is the property of Springer Nature 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 & Fermentation Industries is the property of Food & Fermentation Industries 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.)

In this study, we report an environment‐friendly protocol by integrating the nonnatural catalytic activity of lipase with electrocatalysis for synthesizing C‐3 alkylated oxindoles, which are part of many natural and pharmaceuticals products. Gratifyingly, Candida antarctica lipase B (CALB) is found to be highly active and regioselective for catalyzing the nonnatural C‐3 alkylation reaction at indole when combined with an electrochemical C‐2 oxidation process in the same vessels. Further, the generality and feasibility of the developed protocol are shown by employing several functional groups on the indole moiety and obtaining the desired products in moderate to good yield. Besides, the control experiments are set up along with the molecular docking studies to substantiate the role of the active site of Candida antarctica lipase B (CALB) in carrying out the regioselective C‐3 alkylation reaction. In addition, control experiments and cyclic voltammetry are performed to get insight into the electrochemical C‐2 oxidation process and as a result, a plausible mechanism for the integrated process is presented. [ABSTRACT FROM AUTHOR]

[Display omitted] Understanding the digestion of lipid-based pharmaceutical formulations and food systems is necessary for optimising drug and nutrient delivery and has been extensively studied in bulk emulsion systems using the pH-stat method [1]. However, this approach is not suitable for investigation of individual lipid droplets, in particular the interface where the lipase acts. Microfluidic approaches to study digestion at lipid-water interfaces using droplet trapping have been proposed, however the aqueous phase in that case washes over the interface presenting uncertainty over the stoichiometry of interactions [2]. The internal interface of a Janus-like droplet, containing distinct aqueous and lipid compartments, mimics the interface of a lipid droplet in aqueous solution with controlled stoichiometry [3]. Hence, it was hypothesised that the internal interface of Janus droplets can offer a precise way to study the enzymatic digestion of lipids formulations. Using microfluidic methods, Janus-like droplets were formed by coalescing emulsion droplets containing lipid formulation and pancreatic lipase. Polarised light microscopy (PLM) and in-situ small-angle X-ray scattering (SAXS) were used to investigate the droplets. PLM revealed the growth of an aligned inverse hexagonal phase (H 2), and with SAXS showed that this phase transformation and alignment resulted from enzymatic digestion. A subsequent partial transformation from H 2 to inverse bicontinuous cubic phase occurred when simulated intestinal fluid was used instead of Tris buffer. Suggesting that phospholipids and bile salts could diffuse across the internal interface to locally affect their surroundings. [ABSTRACT FROM AUTHOR]

The current study focuses on evaluating the enzyme inhibition (acetylcholinesterase, α-amylase, α-glucosidase, pancreatin lipase), antioxidant, and antimicrobial activities of the "Modesto" apricot, "Stanley" plum, and their hybrid the "Stendesto" plum–apricot. The "Stendesto" is the only successful plum–apricot hybrid in Bulgaria. A spectrophotometric approach was used to evaluate the antioxidant activity following four complementary assays (DPPH, ABTS, FRAP, and CUPRAC). The "Stendesto" plum–apricot revealed its enhanced antioxidant potential compared to its parental lines. Apart from the free phenolics extraction, two other techniques (alkaline and acid hydrolysis) were applied to reveal the biological potential of the studied fruit. Not only free but also bound phenolic extracts were able to inhibit α-glucosidase and acetylcholinesterase, while none of the extracts inhibited lipase or α-amylase. None of the apricot extracts had antimicrobial activity, while the other fruit had limited antimicrobial activity. The proposed results undoubtedly reveal that hybrid fruits possess enhanced biological activity compared to their parents. This is a first comprehensive evaluation of hybrid fruits with reference to parental lines. This makes them an interesting research topic that should be better explored. [ABSTRACT FROM AUTHOR]

Lipases are enzymes whose activity often positively contributes to the development of the characteristic aroma during cheese ripening. They may originate from microorganisms present in milk or from starter cultures. This study attempted to identify four extracellular lipases of Lactiplantibacillus plantarum (formerly Lactobacillus plantarum), which were previously partially purified and characterised by a different research group two decades ago, providing the Nterminal protein sequences. The genome of Lb. plantarum DSM 12028 was sequenced in the current work and the protein matches for the sequenced fragments were searched for. The matches were correctly located at proteins' Ntermini, if the removal of the preprotein domain was considered, to simulate the protein maturation by Signal peptidase I. However, the identified proteins are peptidoglycan hydrolases rather than lipases. The lipase activity observed in the previous study might have been caused by different proteins coeluted with the peptidoglycan hydrolases, but substrate specificity should be experimentally verified for definitive conclusion. The genome was searched for other extracellular hydrolase genes, possibly lipases or esterase, resulting in 17 candidates. Additionally, the genomic sequence of the strain will be valuable for research teams investigating its potential as a probiotic strain. [ABSTRACT FROM AUTHOR]

Musa balbisiana Colla plant belongs to the Musaceae family, which is well‐known for its nutritional and pharmacological properties. This study aimed to evaluate the anti‐xanthine oxidase, anti‐lipase, and anti‐tyrosinase activities of samples of corm, pseudostem, inflorescence, fruit, peel, and seed of M. balbisiana. The results show that seed performed the highest capacity in the inhibition of three investigated enzymes, with IC50 values of 290.25 μg/mL (anti‐tyrosinase), 141.51 μg/mL (anti‐xanthine oxidase), and 25.66 μg/mL (anti‐lipase). In addition, while fruit showed better performance in anti‐lipase inhibition (IC50: 32.72 μg/mL), corm pointed out higher capability on anti‐xanthine oxidase (IC50: 160.67 μg/mL) and anti‐tyrosinase (IC50: 334.43 μg/mL). The data show the high potential of the application of M. balbisiana parts in medical aesthetics, dietary supplements, or medicine. This is the first report to systematically present the biological activities of all parts of M. balbisiana grown in Vietnam. [ABSTRACT FROM AUTHOR]

This study describes the production of solketal esters from used soybean cooking oil (USCO) via enzymatic hydroesterification. This process consists of the complete hydrolysis of USCO into free fatty acids (FFAs) catalyzed by crude lipase extract from Candida rugosa (CRL). The resulting FFAs were recovered and utilized as the raw material for an esterification reaction with solketal, which was achieved via an open reaction. For this purpose, lipase Eversa® Transform 2.0 (ET2.0) was immobilized via physical adsorption on treated epicarp particles from Acrocomia aculeata (macauba), a lignocellulosic residue. A protein loading of 25.2 ± 1.3 mg g−1 with a support and immobilization yield of 64.8 ± 2.5% was achieved using an initial protein loading of 40 mg g−1 of support. The influence of certain parameters on the esterification reaction was evaluated using a central composite rotatable design (CCRD). Under optimal conditions, a FFAs conversion of 72.5 ± 0.8% was obtained after 150 min of reaction at 46 °C using a biocatalyst concentration of 20% wt. and a FFAs–solketal molar ratio of 1:1.6. The biocatalyst retained 70% of its original activity after ten esterification batches. This paper shows the conversion of two agro-industrial waste into valuable materials (enzyme immobilization support and solketal esters). [ABSTRACT FROM AUTHOR]

Introduction: Acute Pancreatitis is a medical disorder characterized by a sudden and intense inflammation of the pancreas. Patients presenting with severe acute upper abdomen discomfort should be considered for acute pancreatitis. However, to confirm the diagnosis, either biochemical or radiologic documentation is necessary. Aims and Objectives: The purpose of this study is to determine the role of biochemical marker in predicting acute pancreatitis. Methods The present research is a retrospective investigation carried out at the Department of General surgery, SCB MCH, Cuttack during the period of May 2023 to November 2023. Demographic information obtained from the medical records included age, sex, serum amylase levels, and lipase amylase lipase ratio.. Results: Out of the total of 90 patients, 73.3% (n=66) were male and 26.7% (n=24) were female. Mean age and standard deviation of patients in this research group were 38.5±2.2.5 years. The mean and standard deviation of Amylase, Lipase, and Amylase Lipase Ratio measured 870.3±754.23, 235.8±124.5, and 3.87±2.45, respectively. Amylase and Lipase exhibited sensitivity and specificity of 83.33% and 84.88% respectively, when tested three times over the normal range. The positive predictive statistic is 85.23% and the negative predictive statistic is 82.95%.Point accuracy: 84.09%. Conclusion: The ACG practice recommendations accept elevated levels of lipase and/or amylase over 3 times the upper limit of normal (ULN) as diagnostic for individuals experiencing stomach discomfort consistent with Acute Pancreatitis. Compared to amylase, lipase is somewhat more specific to Acute Pancreatitis. Elevates sooner and remains higher than serum amylase in individuals with acute pancreatitis. Diagnostic accuracy of serum lipase surpassed that of serum amylase. [ABSTRACT FROM AUTHOR]

This study aimed to optimize the kinetic resolution of building blocks for the synthesis of β-blockers using Candida rugosa lipases, which could be potentially used to synthesize enantiomerically pure β-blockers further. Reaction mixtures were incubated in a thermostated shaker. Qualitative and quantitative analyses of the reaction mixtures were performed using chiral stationary phases and the UPLC-IT-TOF system. Of the 24 catalytic systems prepared, a system containing lipase from Candida rugosa MY, [EMIM][BF4] and toluene as a two-phase reaction medium and isopropenyl acetate as an acetylating agent was optimal. This resulted in a product with high enantiomeric purity produced via biotransformation, whose enantioselectivity was E = 67.5. Using lipases from Candida rugosa enables the enantioselective biotransformation of the β-blockers building block. The biocatalyst used, the reaction environment, and the acetylating agent significantly influence the efficiency of performer kinetic resolutions. The studies made it possible to select an optimum system, a prerequisite for obtaining a product of high enantiomeric purity. As a result of the performed biotransformation, the (S)-enantiomer of the β-blocker derivative was obtained, which can be used to further synthesize enantiomerically pure β-blockers. [ABSTRACT FROM AUTHOR]

Copyright of Modern Food Science & Technology is the property of Editorial Office of Modern Food Science & Technology 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 China Condiment is the property of China Condiment 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 Cotton Textile Technology is the property of Cotton Textile Technology Editorial Office 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.)

In order to assessing the heterogeneity of Bacillus sp. isolates spoilage potential, six Bacillus sp. isolates isolated from spoiled low-temperature sausages were used to investigate the heterogeneity of their spoilage properties at 20 °C (room temperature) and 37 °C (optimum growth temperature). The growth curve, acid production capacity, gas production capacity, protease activity, lipase activity, and amylase activity of six strains of Bacillus sp. were measured in the experiment. The results revealed that Bacillus cereus (C) had the greatest capacity for producing acid and that after 48 hours at 37 °C, the pH in the culture medium dropped by 0.71 relative to the blank control group. Following a 5-day culture at 37 °C, Bacillus amyloliquefaciens (G) displayed the greatest protease and amylase activities, with a maximum protease activity of 7.17 U/mL and a decomposition circle area of starch agar of 16.53 cm². Bacillus cereus (C) exhibited the least comprehensive spoiling ability, as evidenced by its protease activity of 2.63 U/mL and the decomposition circle area of starch agar of 7.55 cm2 after 5 days of culture at 37 °C. Furthermore, it was discovered that the growth temperature significantly impacted the spoilage potential of the strains. In summary, there was great heterogeneity in the spoilage characteristics of Bacillus sp.. When examining its spoilage traits, it is important to consider this heterogeneity. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]