01854nas a2200217   4500008004100000022001400041245009400055210006900149260009900218300001200317490000700329520104200336653002201378653002401400653001701424653002201441100001801463700001401481700002501495856011601520       2011                        eng d  a1359-511300aPurification and characterization of an alkaline protease by a new strain of Beauveria sp0 aPurification and characterization of an alkaline protease by a n  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB  a579-5850 v463 a<p>A fungal culture isolated from animal dung was identified as a new strain of Beauveria sp MTCC 5184 based on 18S rDNA and ITS nucleotide sequence homology. The fungal isolate secretes alkaline protease active at pH 9 and 50 degrees C. The alkaline protease from Beauveria sp (BAP) was purified to homogeneity with 10.2-folds increase in specific activity and 38.6% recovery. The molecular mass and isoelectric point of the protease were found to be 29 kDa and 9.3, respectively. The N-terminal sequence of the BAP showed only partial homology with subtilisin like proteases from other fungi. The enzyme was stable up to 40 degrees C and pH 3-11. The protease was inhibited by Cd(2+), Hg(2+) and Mn(2+). The activity was totally lost in the presence of 1 mM PMSF suggesting it to be a serine protease. The protease showed maximum activity with casein followed by haemoglobin and BSA. The purified protease is able to separate the endothelial cells and can be used in animal cell culture. (C) 2010 Elsevier Ltd. All rights reserved.</p>10aAlkaline Protease10aAnimal cell culture10aBeauveria sp10aSequence homology1 aShankar, Shiv1 aRao, Mala1 aLaxman, Ryali, Seeta  uhttp://library.ncl.res.in/content/purification-and-characterization-alkaline-protease-new-strain-beauveria-sp-002081nas a2200217   4500008004100000022001400041245012000055210006900175260007900244300001200323490000800335520125300343653001601596653002201612653001701634653002001651653002301671100001801694700002501712856012601737       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  uhttp://library.ncl.res.in/content/biophysicochemical-characterization-alkaline-protease-beauveria-sp-mtcc-5184-multiple-0