Purification and properties of an extracellular protease from Myxococcus virescens

PURIFICATION AND PROPERTIES OF AN EXTRACELLULAR PROTEASE PRODUCED BY PENICIUIUM EXPANSUM

Penicilliurn expamum grown in a medium with rice husk as a carbon source produced an extracellular protease. The protease enzyme was isolated from culture broth by fractionation with acetone and column chromatography on Sephadex G- 100 and DEAE A-50. The protease enzyme was purified about 17.47 fold, with a recovery of 14%. The purified protease was homogenous on SDS polyacrylarnide disc ge...

Purification and properties of an extracellular protease of Staphylococcus aureus.

extraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties

آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...

Purification and Properties of an Extracellular Protease Produced by the Entomopathogenic Fungus Beauveria bassiana.

Beauveria bassiana GK2016 grown in a medium with gelatin as the sole carbon and nitrogen source produced an extracellular protease. The protease production was highest when the fungus was grown on a semiliquid medium and was purified about 18-fold, with a recovery of 21%. The protease molecular weight was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be about 35,000....

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...