@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:000291879600008,
	title = {Biochemical characterisation of alpha-amylase inhibitors from achyranthes aspera and their interactions with digestive amylases of coleopteran and lepidopteran insects},
	journal = {Journal of the Science of Food and Agriculture},
	volume = {91},
	number = {10},
	year = {2011},
	month = {AUG},
	pages = {1773-1780},
	publisher = {WILEY-BLACKWELL},
	address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
	abstract = {<p>BACKGROUND: Starchy seeds are an important food and a source of dietary ingredients in many countries. However, they suffer from extensive predation by bruchids (weevils) and other pests. alpha-Amylase inhibitors are attractive candidates for the control of seed weevils, as these insects are highly dependent on starch as an energy source. RESULTS: A proteinaceous alpha-amylase inhibitor from the seeds of Achyranthes aspera was identified, purified and characterised. In electrophoretic analysis, two prominent amylase inhibitor activity bands (AI1 and AI2) were detected. The inhibitor was purified 9.99-fold with 1206.95 total amylase inhibitor units mg(-1) protein. The molecular weight of the purified inhibitor was around 6 kDa. The isolated alpha-amylase inhibitor was found to be resistant to heat and proteolysis. Feeding analysis of Callosobruchus maculatus larvae on a diet containing seed powder of A. aspera revealed that survival of the larvae was severely affected, with the highest mortality rate occurring on the fifth day of feeding. The isolated inhibitor inhibited the majority of amylase isoforms of C. maculatus, Tribolium confusum and Helicoverpa armigera in electrophoretic analysis and solution assays. CONCLUSION: The information obtained in the present investigation could be useful for a genetic engineering approach that would make seeds resistant to storage pest infestations. (C) 2011 Society of Chemical Industry</p>},
	keywords = {Achyranthes aspera, Amylase inhibitors, amylases, Callosobruchus maculatus, Tribolium confusum},
	issn = {0022-5142},
	doi = {10.1002/jsfa.4380},
	author = {Hivrale, Vandana K. and Chougule, Nanasaheb P. and Giri, Ashok P. and Chhabda, Pavan J. and Kachole, Andmanvendra S.}
}
