@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.}
}
@article {UGC-New Delhi},
	title = {Developmental and digestive flexibilities in the midgut of a polyphagous pest, the cotton bollworm, helicoverpa armigera},
	journal = {Journal of Insect Science},
	volume = {12},
	number = {3-4},
	year = {2012},
	month = {MAR},
	pages = {42},
	publisher = {UNIV ARIZONA},
	address = {LIBRARY C327, TUCSON, AZ 85721 USA},
	abstract = {<p>Developmental patterns and survival of the cotton bollworm, Helicoverpa armigera Hubner (Lepidoptera: Noctuidae), a polyphagous insect pest, have been studied with reference to the effect of diet on major gut digestive enzymes (amylases, proteases, and lipases). Significant correlations between nutritional quality of the diet and larval and pupal mass were observed when H. armigera larvae were fed on various host plants viz. legumes (chickpea and pigeonpea), vegetables (tomato and okra), flowers (rose and marigold), and cereals (sorghum and maize). Larvae fed on diets rich in proteins and/or carbohydrates (pigeonpea, chickpea, maize, and sorghum) showed higher larval mass and developed more rapidly than larvae fed on diets with low protein and carbohydrate content (rose, marigold, okra, and tomato). Low calorific value diets like rose and marigold resulted in higher mortality (25-35\%) of H. armigera. Even with highly varying development efficiency and larval/pupal survival rates, H. armigera populations feeding on different diets completed their life cycles. Digestive enzymes of H. armigera displayed variable expression levels and were found to be regulated on the basis of macromolecular composition of the diet. Post-ingestive adaptations operating at the gut level, in the form of controlled release of digestive enzymes, might be a key factor contributing to the physiological plasticity in H. armigera.</p>},
	keywords = {amylases, larval performance, Lipases, Proteases},
	issn = {1536-2442},
	doi = {10.1016/j.tetasy.2012.02.004},
	author = {Sarate, P. J. and Tamhane, V. A. and Kotkar, H. M. and Ratnakaran, N. and Susan, N. and Gupta, Vidya S. and Giri, Ashok P.}
}
