Studies on a Doubleheaded Protease Inhibitor from Phaseolus mungo

Hajela, N.; Pande, Amit; Sharma, Sujata; Rao, Dandina N.; Hajela, Krishnan

doi:10.1007/bf03263059

Cited by 38 publications

(33 citation statements)

References 13 publications

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“…Therefore, in all the subsequent experiments, 50 mM phosphate buffer (pH 7.6) was used for extraction. Previously, different media have been reported to be suitable for extraction of trypsin inhibitor by various workers (Sessa and Nelsen, 1991;Domoney et al, 1993;Marconi et al, 1993;Hajela et al, 1999;Maggo et al, 1999).…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, Marquez and Alonso (1999) observed completed inactivation of chickpea protease inhibitor on boiling for 300s. In general, protease inhibitors from legumes are quite stable up to 80°C but lose activity above this temperature (Hajela et al, 1999;Maggo et al, 1999;Gupta et al, 2000). The stability of the inhibitor at high temperatures may be attributed to its rigid and compact protein structure stabilized by a number of disulfide linkages as suggested for PI from pea seeds (Sierra et al, 1999).…”

Section: Determination Of Molecular Massmentioning

confidence: 99%

“…Using similar techniques, protease inhibitors were purified to homogeneity from other legumes (Hajela et al, 1999;Maggo et al, 1999;Lawrence and Nielsen, 2001). …”

Section: Purification Of Trypsin Inhibitormentioning

confidence: 99%

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Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera

Kansal

Kumar

Kuhar

et al. 2008

Braz. J. Plant Physiol.

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Protease inhibitors in legumes are one of the most promising weapons that confer resistance against insects by inhibiting proteases present in the gut of insect larvae. In the present study, trypsin inhibitor activity was detected in the seed flour extracts of 10 selected varieties of chickpea. The presence of inhibitor was confirmed by dot blot analysis. All the varieties showed inhibitory activity in vitro against the gut protease of Helicoverpa armigera (HGP). Trypsin inhibitor has been purified to near homogeneity to 60.46 fold and 29.20% recovery from chickpea seeds using heat denaturation, ammonium sulphate fractionation, DEAE-Sephadex A-25 and Sephadex G-75. The purified inhibitor showed a single band on SDS-PAGE corresponding to molecular mass of 30,000 Da. The purified inhibitor was active over a wide pH range whereas it retained maximum activity between pH 6 and 10. The inhibitor protein was stable up to 80°C but retained only 40% of activity when heated at 100°C for 20 min. The inhibitor lost its complete activity at 121°C. The chickpea trypsin inhibitor exhibited inhibitory activity against Helicoverpa armigera both in vitro and in vivo. In insect bioassay, a progressive decline in larval weight, growth and survival as well as temporal extension of larval growth was observed after feeding H. armigera larvae on diet supplemented with increasing concentrations of chickpea trypsin inhibitor. The adult emergence was also adversely affected by the inhibitor. It may be concluded that chickpea trypsin inhibitor has insecticidal potential against H. armigera.

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Section: Resultsmentioning

confidence: 99%

Section: Determination Of Molecular Massmentioning

confidence: 99%

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Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera

Kansal

Kumar

Kuhar

et al. 2008

Braz. J. Plant Physiol.

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“…Trypsin inhibitor activity was determined by the enzyme assay (Hajela et al 1999) by using benzoyl-DL-arginine-p-nitroanilide (BAPNA) as a substrate. One trypsin inhibitor unit (TIU) is expressed as an increase of 0.01 absorbance units per 10 ml of reaction mixture at 410 nm.…”

Section: Analysis Of Antinutritional Compoundsmentioning

confidence: 99%

Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans

et al. 2013

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The study was carried out, to explore the potentiality of extrusion technology for elimination of antinutritional components of cereal brans. Extrusion variables were moisture content (14, 17 and 20 %) and temperatures (115°C, 140°C, 165°C). Phytic acid, polyphenols, oxalates, trypsin inhibitor, bulk density and color of brans after extrusion were analyzed. All four raw bran samples had high concentration of phytic acid, polyphenols, oxalates and trypsin inhibitors. Extrusion cooking was found effective in reduction of these antinutritients. Extrusion processing reduced the phytic acid by 54.51 %, polyphenol by 73.38 %, oxalates by 36.84 %, and trypsin inhibitor by 72.39 %. The heat treatment caused the highest reduction in polyphenols followed by trypsin inhibitors, phytic acid and oxalates. The highest reduction in antinutrients was observed at 140°C and 20 % moisture content. Bulk density increased significantly compared to raw brans and increase in redness and decrease in yellowness of brans was observed after extrusion treatment.

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“…Protease inhibitor was extracted and estimated by the method of Hajela et al (1999). Phytic acid was extracted (Zemel and Shelef 1982) and organic phosphorus was estimated by the method of Rouser et al (1974).…”

Section: Determination Of Condensed Tannins Protease Inhibitor and Pmentioning

confidence: 99%

Appraisal of maize germplasm for identification of nutritionally rich nutraceutical genotypes

Kaur

2016

Cereal Research Communications

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Thirty maize genotypes were characterized for their nutritional, antinutritional and nutraceutical traits for identification of elite germplasm rich in beneficial characteristics. Starch, proteins, lipids, tryptophan, lysine, β-carotene, condensed tannins, protease inhibitor, phytic acid, total phenols, flavonols, o-dihydroxy phenols and DPPH radical scavenging activity were determined in grains of all the genotypes. Correlation coefficient among the various parameters showed that lysine, total phenols, flavonols and o-dihydroxy phenols were negatively correlated with phytic acid content of the genotypes. This showed that the nutritional and the nutraceutical potency of genotypes, rich in lysine and phenolic compounds, is further propounded by a reduction of phytic acid content in them. On the basis of various constituents, the genotypes were divided into three groups. Group-A genotypes had high to moderate levels of both nutritional and nutraceutical traits. Group-B included those genotypes that exhibited high to moderate levels of either nutritional or nutraceutical traits. Group-C was constituted of genotypes that had lower levels of both nutritional and nutraceutical traits. Agglomerative hierarchical clustering showed that the D subcluster of MC-2 was chiefly comprised of genotypes that had high to moderate levels of both nutritional and nutraceutical traits. It may be concluded that CML134, CML266, TOO14601, LM11, CML264, CML321, SE563, LM10, LM18, LM14 and CML32 were nutritionally rich nutraceutical genotypes having low antinutrient potency.

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Studies on a Doubleheaded Protease Inhibitor from Phaseolus mungo

Cited by 38 publications

References 13 publications

Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera

Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera

Effect of extrusion variables (temperature, moisture) on the antinutrient components of cereal brans

Appraisal of maize germplasm for identification of nutritionally rich nutraceutical genotypes

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