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Journal ArticleDOI

Inhibitor potential of protease and α-amylase inhibitors of sweet potato and taro on the digestive enzymes of root crop storage pests

TLDR
The selective inhibitory potential of the isoinhibitors of sweet potato and taro on the digestive enzymes of root crop pests could be exploited for making transgenic plants with improved resistance against major pests.
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This article is published in Journal of Stored Products Research.The article was published on 2004-01-01. It has received 15 citations till now.

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Book ChapterDOI

Uses and Nutritional Data of Sweetpotato

TL;DR: The root is either long and tapered, ovoid or round with a skin colour ranging from white, brown, purple or red and the flesh colour ranging between white, pale cream, orange or purple as discussed by the authors.
Journal ArticleDOI

Purification, characterization, and cDNA cloning of a Bowman-Birk type trypsin inhibitor from Apios americana Medikus tubers.

TL;DR: Comparison of the amino acid sequence with those of the trypsin inhibitors from plants suggests that AATI belongs to the Bowman-Birk family and that it contains two possible reactive sites toward tryPSin at Lys62 and Arg88.
Journal ArticleDOI

α-Amylase inhibitor in local Himalyan collections of Colocasia: Isolation, purification, characterization and selectivity towards α-amylases from various sources

TL;DR: The ability of the inhibitor to inhibit insect amylases highlights its possible role in pest resistance and post harvest decay of crop plants and could suggest its potential in treatment of diabetes and cure of nutritional problems, which result in obesity.
Journal ArticleDOI

Inhibitory effects of plant extracts on growth, development and α-amylase activity in the red flour beetle Tribolium castaneum (Coleoptera: Tenebrionidae)

TL;DR: The results indicate that the bioinsecticidal effects of the leaf extracts are mediated by inhibiting the gene expression and activity of enzymes involved in sugar metabolism.
Journal ArticleDOI

Inhibitory action of Cerrado plants against mammalian and insect α-amylases

TL;DR: The results suggest that the application of plant extracts against insect α-amylases represent a promising biotechnological tool for development of new insect pest control strategies, with noticeable affinity and specificity of action against different target enzymes.
References
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Journal ArticleDOI

Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

TL;DR: The inducible chemicals, which can also occur constitutively, include such complex sub­ stances as antibiotics, alkaloids, and terpenes, as well as proteins such as enzymes, enzyme inhibitors, and lectins, which have provided interesting systems for studying inducibles plant defense.
Journal ArticleDOI

Biochemical basis of insect resistance in Vigna unguiculata

TL;DR: This example of insect resistance in the cowpea is due to an elevated level of trypsin inhibitor, confirmed by insect feeding trials in which various protein fractions were added to a basic meal and the effect on larval survival noted.
Journal ArticleDOI

Assessment of the antimetabolic effects of trypsin inhibitors from cowpea (Vigna unguiculata) and other legumes on development of the bruchid beetle Callosobruchus maculatus

TL;DR: It is concluded that CPTI is an effective antimetabolite of C. maculatus and that this type of mechanism may be widespread, however, it relies upon a finely controlled balance within the host plant which has to make available sufficient nutrients for itself but insufficient to maintain predation.
Journal ArticleDOI

A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor

TL;DR: A maize protein is described which is a potent in vitro inhibitor of bovine trypsin and the α-amylase from Tribolium castaneum beetles and which is highly similar to the intensely sweet protein thaumatin, suggesting a possible function for these proteins.
Journal ArticleDOI

A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 å resolution

TL;DR: The binding of RBI to TMA constitutes a new inhibition mechanism for α -amylases and should be general for all α-amylase inhibitors of the cereal inhibitor superfamily.
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