02082nas a2200217   4500008004100000022001400041245012000055210006900175260007900244300001200323490000800335520125300343653001601596653002201612653001701634653002001651653002301671100001801694700002501712856012701737       2015                        eng d  a0273-228900aBiophysicochemical characterization of an alkaline protease from beauveria sp. MTCC 5184 with multiple applications0 aBiophysicochemical characterization of an alkaline protease from  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJAN  a589-6020 v1753 a<p>This study illustrates the biophysicochemical properties of an alkaline protease, BAP (Beauveria sp. alkaline protease) from Beauveria sp. MTCC 5184. This protease exhibited maximum activity at 50 degrees C, pH 9.0, and stability in a broad pH range, in the presence of organic solvents, denaturants, as well as detergents. Wash performance studies revealed that BAP was able to remove blood clots/stains from blood-soaked cloth. Peptide mass fingerprinting results demonstrated partial homology of BAP with subtilisin-like proteinase. BAP showed catalytic activity against natural as well as synthetic substrates. Active site characterization of BAP confirmed the involvement of serine, tryptophan, and aspartic acid in catalytic activity. Detailed kinetic and thermodynamic studies of BAP demonstrated that the activation energy (Ea) for casein hydrolysis was 82.55 kJ/M, the specificity constant (Kcat/K-m), and the values of Delta G (change in Gibbs free energy) decreased with increase in temperature, whereas Delta H (change in enthalapy) and Delta S (change in entropy) were constant. The results of the present study indicate that BAP has potential for applications as detergent additive, in peptide synthesis, and in basic research.</p>10aActive site10aAlkaline Protease10aBeauveria sp10aOrganic solvent10aSubstrate kinetics1 aShankar, Shiv1 aLaxman, Ryali, Seeta  uhttps://library.ncl.res.in/content/biophysicochemical-characterization-alkaline-protease-beauveria-sp-mtcc-5184-multiple-0