@article { ISI:000287274000022,
	title = {Purification and characterization of an alkaline protease by a new strain of Beauveria sp},
	journal = {Process Biochemistry},
	volume = {46},
	number = {2},
	year = {2011},
	month = {FEB},
	pages = {579-585},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<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>},
	keywords = {Alkaline Protease, Animal cell culture, Beauveria sp, Sequence homology},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2010.10.013},
	author = {Shankar, Shiv and Rao, Mala and Laxman, Ryali Seeta}
}
@article { ISI:000348102900047,
	title = {Biophysicochemical characterization of an alkaline protease from beauveria sp. MTCC 5184 with multiple applications},
	journal = {Applied Biochemistry and Biotechnology},
	volume = {175},
	number = {1},
	year = {2015},
	month = {JAN},
	pages = {589-602},
	publisher = {HUMANA PRESS INC},
	address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA},
	abstract = {<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>},
	keywords = {Active site, Alkaline Protease, Beauveria sp, Organic solvent, Substrate kinetics},
	issn = {0273-2289},
	doi = {10.1007/s12010-014-1314-3},
	author = {Shankar, Shiv and Laxman, Ryali Seeta}
}
