Fibrinolytic enzyme from Arthrospira platensis and its effects on breast cancer cells: Exploring its potential as an innovative therapy.

Fibrinolytic enzymes are promising in treating cardiovascular diseases due to their capacity to dissolve blood clots. The fibrinolytic enzyme from Arthrospira platensis (FEAP) was purified by ion exchange chromatography to investigate its ability to activate plasminogen, as well as its thrombolytic and fibrinogenolytic potential. Subsequently, two different cytotoxic assays (MTT and NR) and hemolysis test were performed to evaluate FEAP's safety.

Viability of microencapsulated species of Trichoderma as a strategy to optimize use in biological control.

The increasing use of chemical fungicides without effective control of phytopathogens has led to the development of resistance in microorganisms. As a promising alternative, products formulated with Trichoderma have emerged for their sustainable and effective potential in integrated disease management. However, the predominant formulations do not offer the necessary protection against abiotic factors.

Purification and characterization of a protease produced by submerged fermentation: Ultrasound-enhanced collagenolytic protease from Streptomyces parvulus.

Proteases are a large group of enzymes in high demand due to their wide and different biotechnological applications mainly in the biomedical field. Ultrasound (US) has been used successfully in several Bioprocesses in biotechnology, such as in the upregulation of enzymatic hydrolysis (biocatalysis). The objective of this work was to purify an enzyme from Streptomyces parvulus and to characterize it through physic-chemical applications including ultrasound effect.

Toxicological assays in the evaluation of safety assessment of fibrinolytic enzymes.

Cardiovascular diseases (CVDs) cause 30% of deaths each year, and in 2030, around 23.6 million people will die due to CVDs. The major challenge is to obtain molecules with minimal adverse reactions that can prevent and dissolve blood clots.

Extracellular collagenase isolated from UFPEDA 3421: purification and biochemical characterization.

Collagenases are proteases able to degrade native and denatured collagen, with broad applications such as leather, food, and pharmaceutical industries. The aim of this research was to purify and characterize a collagenase from . In the present work, the coffee ground substrate provided conditions to obtaining high collagenase activity (377.

A novel β-fructofuranosidase produced by URM 4459: purification and biochemical features.

Fructooligosaccharides (FOS) are prebiotics of interest to the food industry. These compounds can be produced through the transfructosylation reaction by the enzyme fructofuranosidase. This enzyme is widely produced by fungi in a medium rich in sugar.

Purification, biochemical characterization and fibrinolytic potential of proteases produced by bacteria of the genus Bacillus: a systematic literature review.

Thrombosis is a hematological disorder characterized by the formation of intravascular thrombi, which contributes to the development of cardiovascular diseases. Fibrinolytic enzymes are proteases that promote the hydrolysis of fibrin, promoting the dissolution of thrombi, contributing to the maintenance of adequate blood flow. The characterization of new effective, safe and low-cost fibrinolytic agents is an important strategy for the prevention and treatment of thrombosis.

Immobilization of fibrinolytic protease from Mucor subtilissimus UCP 1262 in magnetic nanoparticles.

This work reports the immobilization of a fibrinolytic protease (FP) from Mucor subtilissimus UCP 1262 on FeO magnetic nanoparticles (MNPs) produced by precipitation of FeCl·6HO and FeCl·4HO, coated with polyaniline and activated with glutaraldehyde. The FP was obtained by solid state fermentation, precipitated with 40-60% ammonium sulfate, and purified by DEAE-Sephadex A50 ion exchange chromatography. The FP immobilization procedure allowed for an enzyme retention of 52.

Evaluation of the influence of temperature on the protein-tannic acid complex.

Precipitation of blood products from plasma fractionation has played a fundamental role in the industrial purification of important therapeutic products. Only a few studies have been reported by using tannins as proteins precipitant agent from whole plasma while, several conditions have been analyzed. Here, we decided to verify the effect of the temperature on the precipitation process of plasma proteins using tannic acid (TA).

Fibrinolytic enzyme from Arthrospira platensis cultivated in medium culture supplemented with corn steep liquor.

Artrhospira (Spirulina) platensis produced fibrinolytic enzyme under mixotrophic conditions using corn steep liquor (CSL). The enzyme was extracted, purified by combination of two chromatographic techniques and biochemically characterized. Maximum fibrinolytic production (268.

Lovastatin producing by wild strain of isolated from Brazil.

Lovastatin is a drug in the statin class which acts as a natural inhibitor of 3-hydroxy-3-methylglutaryl, a coenzyme reductase reported as being a potential therapeutic agent for several diseases: Alzheimer's, multiple sclerosis, osteoporosis and due to its anti-cancer properties. is known for producing a cholesterol reducing drug. This study sets out to evaluate the production of lovastatin by Brazilian wild strains of isolated from a biological sample and natural sources.

Purification of a lectin from crude extract seed by a single step PEG/phosphate aqueous two-phase system.

The partitioning and purification of lectins from the crude extract of seeds (Cramoll 1,4) was investigated in aqueous two-phase systems (ATPS). A factorial design model (2) was used to evaluate the influence of polyethylene glycol (PEG) molar mass (1500-8000 g/mol), PEG concentration (12.5-17.

Effect of acute exposure in swiss mice (Mus musculus) to a fibrinolytic protease produced by Mucor subtilissimus UCP 1262: An histomorphometric, genotoxic and cytological approach.

The fibrinolytic enzyme produced by Mucor subtilissimus UCP 1262 was obtained by solid fermentation and purified by ion exchange chromatography using DEAE-Sephadex A50. The enzyme toxicity was evaluated using mammalian cell lineages: HEK-293, J774.A1, Sarcoma-180 and PBMCs which appeared to be viable at a level of 80%.

Purification, biochemical, and structural characterization of a novel fibrinolytic enzyme from Mucor subtilissimus UCP 1262.

Fibrinolytic proteases are enzymes that degrade fibrin. They provide a promising alternative to existing drugs for thrombolytic therapy. A protease isolated from the filamentous fungus Mucor subtilissimus UCP 1262 was purified in three steps by ammonium sulfate fractionation, ion exchange, and molecular exclusion chromatographies, and characterized biochemically and structurally.

Purification of a fibrinolytic protease from Mucor subtilissimus UCP 1262 by aqueous two-phase systems (PEG/sulfate).

A fibrinolytic protease from M. subtilissimus UCP 1262 was recovered and partially purified by polyethylene glycol (PEG)/sodium sulfate aqueous two-phase systems (ATPS). The simultaneous influence of PEG molar mass, PEG concentration and sulfate concentration on the enzyme recovery was first investigated using a 2(3) full factorial design, and the Response Surface Methodology used to identify the optimum conditions for enzyme extraction by ATPS.