Unveiling the therapeutic potential: anti-inflammatory and antioxidant properties of selective medicinal plants.

This study highlights the potential of plant extracts as sustainable and cost-effective alternatives to traditional anti-inflammatory drugs, owing to their rich bioactive compounds. The chemical composition and biological activities of ethanolic extracts from Artemisia campestris, Haloxylon articulatum, and Retama raetam were investigated. Extraction yields ranged from 2.

A Proteinaceous Alpha-Amylase Inhibitor from Moringa Oleifera Leaf Extract: Purification, Characterization, and Insecticide Effects against Insect Larvae.

The main objective of the current study was the extraction, purification, and enzymatic characterization of a potent proteinaceous amylase inhibitor from Moringa oleifera. The antimicrobial potential and insecticide effects against C. maculates insect larvae were also studied.

Biochemical, Kinetic and Biological Properties of Group V Phospholipase A2 from Dromedary.

Secretory group V phospholipase A2 (PLA-V) is known to be involved in inflammatory processes in cellular studies, nevertheless, the biochemical and the enzymatic characteristics of this important enzyme have been unclear yet. We reported, as a first step towards understanding the biochemical properties, catalytic characteristics, antimicrobial and cytotoxic effects of this PLA, the production of PLA-V from dromedary. The obtained DrPLA-V has an absolute requirement for Ca and NaTDC for enzymatic activity with an optimum pH of 9 and temperature of 45 °C with phosphatidylethanolamine as a substrate.

Efficient heterologous expression in Pichia pastoris, immobilization and functional characterization of a scorpion venom secreted phospholipase A.

Industrial processes have expanded with the ability to clone and express recombinant immobilized enzymes in microorganisms such as Pichia pastoris that have commercially attractive amounts of the appropriate genes. This report describes the overexpression in Pichia pastoris, immobilization, and functional characterization of a secreted phospholipase A from scorpion venom Scorpio maurus: rPLA(-5). After 48 h of culture, the recombinant rPLA(-5) was secreted into the culture medium and expressed at about 9 mg/L.

Production and structure prediction of amylases from Chlorella vulgaris.

Amylases are enzymes required for starch degradation and are naturally produced by many microorganisms. These enzymes are used in several fields such as food processing, beverage, and medicine as well as in the formulation of enzymatic detergents proving their significance in modern biotechnology. In this study, a three-stage growth mode was applied to enhance starch production and amylase detection from Chlorella vulgaris.

A Novel Thermostable and Alkaline Protease Produced from Isolated from Olive Oil Mill Sols Suitable to Industrial Biotechnology.

This study was conducted to identify a new alkaline and thermophilic protease (Ba.St.Pr) produced from isolated from olive oil mill sols and to evaluate its culture conditions, including temperature, pH, carbon and nitrogen sources, and incubation time.

Molecular and Structural Characterizations of Lipases from by Functional Genomics.

Microalgae have been poorly investigated for new-lipolytic enzymes of biotechnological interest. In silico study combining analysis of sequences homologies and bioinformatic tools allowed the identification and preliminary characterization of 14 putative lipases expressed by . These proteins have different molecular weights, subcellular localizations, low instability index range and at least 40% of sequence identity with other microalgal lipases.

Purification and Biochemical Characterization of a New Protease Inhibitor from with Antimicrobial, Antifungal and Cytotoxic Effects.

The main objective of the current study was the extraction, purification, and biochemical characterization of a protein protease inhibitor from . Antimicrobial potential and cytotoxic effects were also examined. The protease inhibitor was extracted in 0.

Spirulina platensis, Punica granatum peel, and moringa leaves extracts in cosmetic formulations: an integrated approach of in vitro biological activities and acceptability studies.

The selection of suitable natural raw materials in the cosmetic research and development is a key point, in order not only to obtain the expected results but also to avoid undesirable side effects. In this study, spirulina platensis, pomegranate (Punica granatum) peel, and moringa leaves alone were evaluated for anti-oxidant and antimicrobial properties. The chemical composition (moisture, dry matter, protein, lipid, and ash) and total polyphenols, flavonoids, and carotenoids content were evaluated in the three extracts.

Enhancement of Aeribacillus pallidus strain VP3 lipase catalytic activity through optimization of medium composition using Box-Behnken design and its application in detergent formulations.

Lipases are hydrolytic enzymes owing much importance in industrial applications. These enzyme-based detergents are ecofriendly and produce a wastewater with low level of COD (chemical oxygen demand). In the present work, a novel halophilous, thermoalkaline, and detergent-tolerant lipase produced by a newly isolated Aeribacillus pallidus strain VP3 was studied.

Hydrolysis of three different head groups phospholipids by chicken group V phospholipase A2 using the monomolecular film technique.

The kinetic aspects of lipolysis by pulmonary phospholipase A2 (ChPLA2-V), chicken intestinal phospholipase A2 (ChPLA2-IIA) and chicken pancreatic phospholipase A2 (ChPLA2-IB), from chicken have been compared using the monomolecular films technique, on short-chain phospholipids (with three different head groups) and on long-chain phospholipids. The main conclusions from our experimental data indicate that the maximum catalytic activities of ChPLA2-V on 1,2 phosphatidylcholine and 1,2 phosphatidylethanolamine reached 15.26 and 36.

Purification, biochemical and molecular study of lipase producing from a newly thermoalkaliphilic Aeribacillus pallidus for oily wastewater treatment.

Treatment of oily wastewater is constantly a challenge; biological wastewater treatment is an effective, cheap and eco-friendly technology. A newly thermostable, haloalkaline, solvent tolerant and non-induced lipase from Aeribacillus pallidus designated as GPL was purified and characterized of biochemical and molecular study for apply in wastewater treatment. The GPL showed a maximum activity at 65°C and pH 10 after 22 h of incubation, with preference to TC4 substrates.

A novel bactericidal homodimeric PLA group-I from Walterinnesia aegyptia venom.

A novel non-toxic phospholipase A was purified to homogeneity in a single chromatography step from the venom of Walterinnesia aegyptia, a monotypic elapid snake caught in Saudi Arabia, and its antimicrobial and hemolytic properties were evaluated as well. This enzyme, namely WaPLA, is a homodimer with an estimated molecular mass of 30 kDa, and its NH-terminal sequence exhibits a significant degree of similarity with PLA group-I. At optimal pH (8.

Maneb disturbs expression of superoxide dismutase and glutathione peroxidase, increases reactive oxygen species production, and induces genotoxicity in liver of adult mice.

Maneb (MB), a fungicide largely used in agriculture throughout the world including Tunisia, protects many vegetables, fruits and field crops against a wide spectrum of fungal diseases. However there is a lack of informations regarding the risks arising from MB exposure on non target organisms, especially mammals. The aim of this study was to investigate the morphological, biochemical and molecular aspects of liver injury after exposure of mice to MB.

Renaturation and one step purification of the chicken GIIA secreted phospholipase A2 from inclusion bodies.

The cDNA coding for a mature protein of 123 amino acids, containing all of the structural features of catalytically active group IIA sPLA2, has been amplified from chicken intestine. The gene has been cloned into the bacterial expression vector pET-21a(+), which allows protein over-expression as inclusion bodies and enables about 3mg/l of pure refolded fully active enzyme to be obtained. Recombinant expression of chicken intestinal sPLA2-IIA (ChPLA2-IIA) in Escherichia coli shows that the enzyme is Ca(2+) dependent, maximally active at pH 8-9, and hydrolyses phosphatidylglycerol versus phosphatidylcholine with a 10-fold preference.

Dimethoate induces kidney dysfunction, disrupts membrane-bound ATPases and confers cytotoxicity through DNA damage. Protective effects of vitamin E and selenium.

Dimethoate (DM) is an organophosphate insecticide widely used in agriculture and industry and has toxic effects on non-target organisms especially mammalian. However, we still know little about DM-induced kidney injury and its alleviation by natural antioxidants. In the present study, selenium (Se), vitamin E, DM, Se+DM, vitamin E+DM, Se+vitamin E+DM were given to adult rats for 4 weeks.

N-terminal domain of turkey pancreatic lipase is active on long chain triacylglycerols and stabilized by colipase.

The gene encoding the TPL N-terminal domain (N-TPL), fused with a His6-tag, was cloned and expressed in Pichia pastoris, under the control of the glyceraldehyde-3-phosphate dehydrogenase (GAP) constitutive promoter. The recombinant protein was successfully expressed and secreted with an expression level of 5 mg/l of culture medium after 2 days of culture. The N-TPL was purified through a one-step Ni-NTA affinity column with a purification factor of approximately 23-fold.

Renaturation and one step purification of the chicken GIIA secreted phospholipase A2 from inclusion bodies.

The cDNA coding for a mature protein of 123 amino acids, containing all of the structural features of catalytically active group II sPLA2, has been amplified. The gene has been cloned into the bacterial expression vector pET-21a(+), which allows protein over-expression as inclusion bodies and enables about 3 mg per litre of pure refolded fully active enzyme to be obtained. Recombinant expression of chPLA2-IIA in Escherichia coli shows that the enzyme is Ca(2+) dependent, maximally active at pH 8-9, and hydrolyses phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference.

Phospholipase A2 purification and characterization: a case study.

We compared here the purification procedures, the pH, the calcium, the bile salts, and the temperature dependencies as well as the catalytic activities on phosphatidylcholine (PC) and phosphatidylethanolamine (PE) of two purified secreted PLA2 from chicken pancreatic (ChPLA2-IB) and chicken intestinal (ChPLA2-IIA) origins. Interestingly, ChPLA2-IB hydrolyzes efficiently both purified PC and PE, whereas ChPLA2-IIA hydrolyzes only PE and not PC, even after a long incubation period. These analytical results clearly indicate that the catalytic activity of ChPLA2-IIA, measured with the pH-stat and using egg yolk as substrate, is mainly due to the hydrolysis of the PE fraction present in egg yolk.

Drastic changes in the tissue-specific expression of secreted phospholipases A2 in chicken pulmonary disease.

Infectious bronchitis is one of the most important diseases in poultry and it causes major economic losses. Infectious bronchitis is an acute, highly contagious, viral disease of chickens, characterized by rales, coughing, and sneezing. Because secreted phospholipases A2 (sPLA2) are involved in inflammatory processes, the gene expressions of sPLA2s were investigated in both healthy chickens and chickens with infectious bronchitis and lung inflammation.

Kinetic properties of pancreatic and intestinal sPLA2 from chicken and mammals using the monomolecular film technique.

The interfacial kinetic and binding data for the pancreatic and intestinal sPLA2 from bird and mammals show that these enzymes have dramatically different ability to bind and hydrolyse phospholipids. The main conclusions from our experimental data indicate that phosphatidylcholine monolayers (PC), in contrast to phosphatidylethanolamine (PE) and phosphatidylglycerol (PG), were resistant to the hydrolysis by human intestinal sPLA2. Conversely, chicken intestinal sPLA2 was found to be able to hydrolyse all the phospholipids tested, including PC.

Immunohistochemical localization of hepatopancreatic phospholipase A2 in Hexaplex trunculus digestive cells.

Background: Mammalian sPLA2-IB localization cell are well characterized. In contrast, much less is known about aquatic primitive ones. The aquatic world contains a wide variety of living species and, hence represents a great potential for discovering new lipolytic enzymes and the mode of digestion of lipid food.

Biochemical properties of pancreatic colipase from the common stingray Dasyatis pastinaca.

Background: Pancreatic colipase is a required co-factor for pancreatic lipase, being necessary for its activity during hydrolysis of dietary triglycerides in the presence of bile salts. In the intestine, colipase is cleaved from a precursor molecule, procolipase, through the action of trypsin. This cleavage yields a peptide called enterostatin knoswn, being produced in equimolar proportions to colipase.

Purification and biochemical characterization of pancreatic phospholipase A2 from the common stingray Dasyatis pastinaca.

Background: Mammalian sPLA2-IB are well characterized. In contrast, much less is known about aquatic ones. The aquatic world contains a wide variety of living species and, hence represents a great potential for discovering new lipolytic enzymes.