A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

Gadge, Prafull P.; Wagh, Sandip K.; Shaikh, Faiyaz K.; Tak, Rajesh D.; Padul, Manohar V.; Kachole, Manvendra S.

doi:10.1016/j.pestbp.2015.06.007

Cited by 22 publications

(10 citation statements)

References 44 publications

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“…In the present study, candidate genes belonging to lectin receptor kinase and chalcone and stilbene synthase family, underlying qUlwv01 are predicted to alter the weight of pod borer larvae feeding on vegetative stage chickpea leaves. Inhibition of cysteine proteinase and α‐amylase have been shown to reduce the performance of insect and virus in barley, rice and Arabidopsis (Carrillo et al., 2011; Gadge et al., 2015; Leplé et al., 1995). Our findings complement previous reports and also suggest that cysteine proteinase inhibitor 12‐like and legumin A‐like genes may inhibit cysteine proteinase and α‐amylase activity, respectively, in the midgut of H. armigera , thereby controlling its weight.…”

Section: Discussionmentioning

confidence: 99%

Development of a dense genetic map and QTL analysis for pod borer Helicoverpa armigera (Hübner) resistance component traits in chickpea (Cicer arietinum L.)

et al. 2020

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Genetic enhancement for resistance against the pod borer, Helicoverpa armigera is crucial for enhancing production and productivity of chickpea. Here we provide some novel insights into the genetic architecture of natural variation in H. armigera resistance in chickpea, an important legume, which plays a major role in food and nutritional security. An interspecific recombinant inbred line (RIL) population developed from a cross between H. armigera susceptible accession ICC 4958 (Cicer arietinum) and resistant accession PI 489777 (Cicer reticulatum) was evaluated for H. armigera resistance component traits using detached leaf assay and under field conditions. A high‐throughput AxiomCicerSNP array was utilized to construct a dense linkage map comprising of 3,873 loci and spanning a distance of 949.27 cM. Comprehensive analyses of extensive genotyping and phenotyping data identified nine main‐effect QTLs and 955 epistatic QTLs explaining up to 42.49% and 38.05% phenotypic variance, respectively, for H. armigera resistance component traits. The main‐effect QTLs identified in this RIL population were linked with previously described genes, known to modulate resistance against lepidopteran insects in crop plants. One QTL cluster harbouring main‐effect QTLs for three H. armigera resistance component traits and explaining up to 42.49% of the phenotypic variance, was identified on CaLG03. This genomic region, after validation, may be useful to improve H. armigera resistance component traits in elite chickpea cultivars.

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Section: Discussionmentioning

confidence: 99%

Development of a dense genetic map and QTL analysis for pod borer Helicoverpa armigera (Hübner) resistance component traits in chickpea (Cicer arietinum L.)

et al. 2020

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“…Because sugars commonly fit the active site of α-amylase and peptides are unlikely to be recognised as a substrate, glycopeptides produced from buckwheat α-AI would be the competitive inhibitors. Some researchers reported glycoproteins that were obtained from plants inhibit α-amylase in a competitive manner [ 33 , 34 , 35 ]. In addition, glycoproteins larger than 29 kDa were detected in undigested buckwheat α-AI ( Figure 6 B).…”

Section: Discussionmentioning

confidence: 99%

Suppressive Effect of the α-Amylase Inhibitor Albumin from Buckwheat (Fagopyrum esculentum Moench) on Postprandial Hyperglycaemia

et al. 2018

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Inhibiting starch hydrolysis into sugar could reduce postprandial blood glucose elevation and contribute to diabetes prevention. Here, both buckwheat and wheat albumin that inhibited mammalian α-amylase in vitro suppressed blood glucose level elevation after starch loading in vivo, but it had no effect after glucose loading. In contrast to the non-competitive inhibition of wheat α-amylase inhibitor, buckwheat albumin acted in a competitive manner. Although buckwheat α-amylase inhibitor was readily hydrolysed by digestive enzymes, the hydrolysate retained inhibitory activity. Together with its thermal stability, this suggests its potential use in functional foods that prevent diabetes.

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“…[22,23] Researchers have also reported the use of two different downstream process methods to purify a bifunctional amylase/trypsin inhibitor . [24,25] Single-step affinity chromatography and two-step chromatography were performed by, first, ion exchange chromatography and then gel chromatography. The purification of amylase and trypsin inhibitor determined by affinity chromatography was 6.59-fold, with a recovery rate of 81.48%, while the purification of amylase and trypsin inhibitor by ion exchange chromatography was 4.28-fold, with a recovery rate of 75.95%.…”

Section: Separation and Purification Of Proteinaceous α-Amylase Inhibitorsmentioning

confidence: 99%

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

Zhou

Zhang

et al. 2021

International Journal of Food Properties

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α-Amylase is abundant in plants and animals. α-Amylase inhibitors can reduce endogenous α-amylase activity, playing an essential role in agricultural pest control, and preventing and treating human disease. In the agricultural field, α-Amylase inhibitors can restrict pest that relies on the starch of crops. Acarbose is an α-amylase inhibitor used to treat diabetes. Some αamylase inhibitors are represented by antinutritional factors, while others are proteinaceous. Depending on their structures and sources, researchers have divided them into seven types: The knottin-like type, the γ-thionin-like type, the cereal type, the Kunitz type, the thaumatin-like type, and the lectin-like type. This paper introduces the methods for separating, purifying, and detecting proteinaceous α-amylase inhibitors while examining the structure and inhibition mechanism of several proteinaceous α-amylase inhibitors. Finally, it explores the potential applications of α-amylase inhibitors.

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A bifunctional α-amylase/trypsin inhibitor from pigeonpea seeds: Purification, biochemical characterization and its bio-efficacy against Helicoverpa armigera

Cited by 22 publications

References 44 publications

Development of a dense genetic map and QTL analysis for pod borer Helicoverpa armigera (Hübner) resistance component traits in chickpea (Cicer arietinum L.)

Development of a dense genetic map and QTL analysis for pod borer Helicoverpa armigera (Hübner) resistance component traits in chickpea (Cicer arietinum L.)

Suppressive Effect of the α-Amylase Inhibitor Albumin from Buckwheat (Fagopyrum esculentum Moench) on Postprandial Hyperglycaemia

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

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