@article { ISI:000230613600002,
	title = {Unraveling biochemical properties of cockroach (Periplaneta americana) proteinases with a gel X-ray film contact print method},
	journal = {Comparative Biochemistry and Physiology B-Biochemistry \& Molecular Biology},
	volume = {141},
	number = {3},
	year = {2005},
	month = {JUL},
	pages = {261-266},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Eleven proteinase activity bands were detected in American cockroach (Periplaneta americana) gut. These were partially purified and characterized using a gel X-ray film contact print method. Cockroach gut proteinases (CGPs) show activity over a broad range of pH with maximum activity between pH 6 and 10, and optimal activity at 50-70 degrees C. CGPs were partially purified by preparative gel electrophoresis and analyzed using synthetic substrates and inhibitors. Four of the proteases exhibited chymotrypsin-like (C1 to C4) activity and seven trypsin-like (T I to T7) activity. Accuracy of the gel X-ray film contact print method is confirmed by including bovine chymotrypsin in CGP analysis. Inhibition of CGPs with different plant proteinaceous proteinase inhibitors allowed identification of potential CGP inhibitors. Our results imply that presence of several CGP activity bands, and their stability and activity over a broad pH and temperature range might contribute to adaptation of P americana to extreme environmental conditions and the polyphagous nature of the species. (c) 2005 Elsevier Inc. All rights reserved.</p>},
	keywords = {activity visualization, cockroach, gut enzymes, Periplaneta americana, plant proteinase inhibitors, Proteinases},
	issn = {1096-4959},
	doi = {10.1016/cbpc.2005.02.015},
	author = {Hivrale, Vandana K. and Chougule, Nanasaheb P. and Chhabda, Pavan J. and Giri, Ashok P. and Kachole, M. S.}
}
@article { ISI:000328395400001,
	title = {Characterization of a chemostable serine alkaline protease from Periplaneta americana},
	journal = {BMC Biochemistry},
	volume = {14},
	year = {2013},
	month = {NOV},
	pages = {32},
	publisher = {BIOMED CENTRAL LTD},
	address = {236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND},
	abstract = {<p>Background: Proteases are important enzymes involved in numerous essential physiological processes and hold a strong potential for industrial applications. The proteolytic activity of insects{\textquoteright} gut is endowed by many isoforms with diverse properties and specificities. Thus, insect proteases can act as a tool in industrial processes. Results: In the present study, purification and properties of a serine alkaline protease from Periplaneta americana and its potential application as an additive in various bio-formulations are reported. The enzyme was purified near to homogeneity by using acetone precipitation and Sephadex G-100 gel filtration chromatography. Enzyme activity was increased up to 4.2 fold after gel filtration chromatography. The purified enzyme appeared as single protein-band with a molecular mass of similar to 27.8 kDa in SDS-PAGE. The optimum pH and temperature for the proteolytic activity for purified protein were found around pH 8.0 and 60 degrees C respectively. Complete inhibition of the purified enzyme by phenylmethylsulfonyl fluoride confirmed that the protease was of serine-type. The purified enzyme revealed high stability and compatibility towards detergents, oxidizing, reducing, and bleaching agents. In addition, enzyme also showed stability towards organic solvents and commercial detergents. Conclusion: Several important properties of a serine protease from P. Americana were revealed. Moreover, insects can serve as excellent and alternative source of industrially important proteases with unique properties, which can be utilized as additives in detergents, stain removers and other bio-formulations. Properties of the P. americana protease accounted in the present investigation can be exploited further in various industrial processes. As an industrial prospective, identification of enzymes with varying essential properties from different insect species might be good approach and bioresource.</p>},
	keywords = {Chemostability, Industrial catalyst, Insect proteases, Periplaneta americana, Serine alkaline protease},
	issn = {1471-2091},
	doi = {10.1186/1471-2091-14-32},
	author = {Sanatan, Prashant T. and Lomate, Purushottam R. and Giri, Ashok P. and Hivrale, Vandana K.}
}
