Covalent immobilization of an alkaline protease from Bacillus licheniformis

Immobilization of Alkaline Protease produced from Bacillus Licheniformis PTCC1331 on Calcium Alginate (Its effect on enzymatic activity)

Alkaline Protease enzyme produced from Bacillus Licheniformis PTCC1331 in optimum Condition(Temperature 37 ?C, 150 rpm, PH=10), is immobilized in different concentrations of Sodium Alginate using entrapment method, to increase its thermal resistance in detergents, and its activity is measured thereafter. Maximum enzymatic activity of 46 was obtained in 2%w/v Sodium alginate solution. Investiga...

Stabilization of Bacillus Licheniformis ATCC 21415 Alkaline Protease by Immobilization and Modification

Alkaline protease from Bacillus licheniformis ATCC21415 was partially purified by fractional precipitation at 70% ethanol which showed 6.2-fold purification. Immobilization of the enzyme by physical adsorption on loofa (as a new carrier) had the highest immobilization yield (70.5%).Chemical modification of the enzyme by covalent coupling with sodium -periodate activated amylopectin retained (78...

immobilization of alkaline protease produced from bacillus licheniformis ptcc1331 on calcium alginate (its effect on enzymatic activity)

alkaline protease enzyme produced from bacillus licheniformis ptcc1331 in optimum condition(temperature 37 ?c, 150 rpm, ph=10), is immobilized in different concentrations of sodium alginate using entrapment method, to increase its thermal resistance in detergents, and its activity is measured thereafter. maximum enzymatic activity of 46 was obtained in 2%w/v sodium alginate solution. investigat...

Isolation and Identification of an Alkaline Protease Producing Bacillus from Soil

Cloning and Enhanced Expression of an Extracellular Alkaline Protease from a Soil Isolate of Bacillus clausii in Bacillus subtilis

in the detergent industry. In this study, the extracellular alkaline serine protease gene, aprE, from Bacillusclausii was amplified by PCR and further cloned and expressed in B. subtilis WB600 using the pWB980 expression vector. Protease activity of the recombinant B. subtilis WB600 harboring the plasmid pWB980/aprEreached up to 1020 U/ml, approximately 3-folds higher than the nativ...