Production, purification and characterization of a novel antithrombotic and anticoagulant serine protease from food grade microorganism .

A novel thrombolytic enzyme was produced by food grade microorganism using agro-industrial by-products as substrates. Process parameters were optimized using Plackett-Berman and Box-Benhken design. Under the optimized fermentation conditions, high fibrinolytic activity of 403.

Gene cloning, expression and homology modeling of first fibrinolytic enzyme from mushroom (Cordyceps militaris).

Fibrinolytic enzymes are important thrombolytic agents for blood-clotting disorders like cardiovascular diseases. Availability of novel recombinant fibrinolytic enzymes can overcome the shortcomings of current thrombolytic drugs. With the objective of facilitating their cost-effective production for therapeutic applications and for gaining deeper insight into their structure-function, we have cloned and expressed the first fibrinolytic protease gene from Cordyceps militaris.

Enhanced elimination of non-digestible oligosaccharides from soy milk by immobilized α-galactosidase: A comparative analysis.

This study compared two immobilization matrices like calcium-alginate and chitosan for immobilization of α-galactosidase and evaluated their potential for the removal of non-digestible raffinose family oligosaccharides from soy milk which cause abdominal discomfort. The pH optima of the free and immobilized enzymes were found to be similar at pH 4.0.

Enhanced Properties and Lactose Hydrolysis Efficiencies of Food-Grade β-Galactosidases Immobilized on Various Supports: a Comparative Approach.

In this study, a fungal and two yeast β-galactosidases were immobilized using alginate and chitosan. The biochemical parameters and lactose hydrolysis abilities of immobilized enzymes were analyzed. The pH optima of immobilized fungal β-galactosidases shifted to more acidic pH compared to free enzyme.

A dual-function chymotrypsin-like serine protease with plasminogen activation and fibrinolytic activities from the GRAS fungus, Neurospora sitophila.

In this study, we have isolated and characterized a fibrinolytic enzyme from the GRAS (Generally Recognized as Safe) fungus, Neurospora sitophila. The enzyme was purified by fractional ammonium sulfate precipitation, hydrophobic interaction, ion exchange and gel filtration chromatography to 45.2 fold with a specific activity of 415.

Preparation of glycosylated zein and retarding effect on lipid oxidation of ground pork.

The focus of the present work was to investigate the glycosylation of zein, partial properties of the glycosylated zein (GZ) and its retarding effect on lipid oxidation of ground pork. Zein was glycosylated with chitosan (MW 1500Da) by microbial transglutaminase, the reaction was verified by FT-IR. Under the optimized conditions, 97.

Biochemical characterization of a novel fibrinolytic enzyme from Cordyceps militaris.

A fibrinolytic enzyme was produced by the medicinal mushroom, Cordyceps militaris using submerged fermentation. The enzyme was purified from culture supernatant by hydrophobic interaction, ion exchange and gel filtration chromatographies. It was purified by 36 fold, with a specific activity of 1,467.

Purification and biochemical characterization of a novel fibrinolytic enzyme from culture supernatant of Cordyceps militaris.

A novel fibrinolytic enzyme from Cordyceps militaris was produced by submerged culture fermentation, purified, and biochemically characterized. The enzyme was purified to homogeneity, with an overall yield of 4.0% and a specific activity of 1682 U/mg.

Purification and characterization of a novel fibrinolytic enzyme from culture supernatant of Pleurotus ostreatus.

A fibrinolytic enzyme was produced by an edible mushroom of Pleurotus ostreatus using submerged culture fermentation. The enzyme was purified from the culture supernatant by applying a combination of freeze-thaw treatment, ammonium sulfate precipitation, hydrophobic interaction, and gel filtration chromatographies. The enzyme was purified by a 147-fold, with a yield of 7.

Purification and characterisation of a novel chitinase from persimmon (Diospyros kaki) with antifungal activity.

A novel chitinase from the persimmon fruit was isolated, purified and characterised in this report. The Diospyros kaki chitinase (DKC) was found to be a monomer with a molecular mass of 29 kDa. It exhibited optimal activity at pH 4.

Purification and characterization of a novel chitinase gene from Paecilomyces thermophila expressed in Escherichia coli.

A novel chitinase gene (PtChiA) from the thermophilic fungus Paecilomyces thermophila was cloned and expressed in Escherichia coli as an intracellular soluble protein. The gene sequence alignment indicates that PtChiA belongs to glycoside hydrolase (GH) family 18 and has an open reading frame comprising of 1473 bp nucleotide sequences with five introns. PtChiA encodes 400 amino acids without any predicted signal peptide.