@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:000306146400006,
	title = {Purification and biochemical characterization of endoglucanase from Penicillium pinophilum MS 20},
	journal = {Indian Journal of Biochemistry \& Biophysics},
	volume = {49},
	number = {3},
	year = {2012},
	month = {JUN},
	pages = {189-194},
	publisher = {NATL INST SCIENCE COMMUNICATION-NISCAIR},
	address = {DR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIA},
	abstract = {<p>Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate of Penicillium pinophilum MS 20 was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. The purified endoglucanase (specific activity 69 U/mg) was a monomeric protein with molecular mass of 42 kDa, as determined by SDS-PAGE. The endoglucanase was active over a broad range of pH (4-7) with maximum activity at pH 5 and showed optimum temperature of 50 degrees C. It retained 100\% activity at 50 degrees C for 6 h and half- lives of 4 h and 3 h at 60 degrees C and 70 degrees C, respectively. The kinetic constants for the endoglucanase determined with carboxymethyl cellulose as substrate were V-max of 72.5 U/mg and apparent K-m of 4.8 mg/ml. The enzyme also showed moderate activity towards H3PO4 swollen cellulose and p-nitrophenyl beta-D-glucoside, but no activity towards filter paper, Avicel and oat spelt xylan. The activity was positively modulated by 47, 32 and 25\% in the presence of Co2+, Zn2+ and Mg2+, respectively to the reaction mixture. The wide pH stability (4-7) and temperature stability up to 50 degrees C of endoglucanase makes the enzyme suitable for use in cellulose saccharification at moderate temperature and pH.</p>},
	keywords = {Biochemical properties, Carboxymethyl cellulose, Endoglucanase, Penicillium pinophilum MS 20, Purification},
	issn = {0301-1208},
	author = {Pol, Dipali and Laxman, Ryali Seeta and Rao, Mala}
}
