Exploring the protease mediated conformational stability in a trypsin inhibitor from Archidendron ellipticum seeds

Bhattacharyya, Arindam; Babu, C. R.

doi:10.1016/j.plaphy.2006.10.008

Cited by 6 publications

(5 citation statements)

References 30 publications

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“…PIs can inhibit specifically trypsin, for example, the Caesalpinia echinata trypsin inhibitor (CeKI); 36 can also inhibit only chymotrypsin 37 or both enzymes. 38 Based on stoichiometric studies, we demonstrated that PeTI is a single-headed Kunitz inhibitor with higher activity against trypsin than chymotrypsin. This difference in affinity is due to the reactive site composition, as observed in soybean inhibitors.…”

Section: ■ Discussionmentioning

confidence: 94%

“…PIs exhibit considerable stability to temperature, pH, denaturing agents, and proteolysis. 26,29,38,43 These stabilities may be attributed to the presence of disulfide bonds and other noncovalent interactions. 44 PeTI also showed these properties, being active and stable after incubation up to 70 °C and over a range of pH, as seen for other PIs from other species of legumes, including Moringa oleifeira 29 and Piptadenia moniliformis.…”

Section: ■ Discussionmentioning

confidence: 99%

“…From this analysis, we observed that the equimolar amount of PeTI necessary to inhibit 100% of trypsin activity inhibited only 30% of chymotrypsin activity. PIs can inhibit specifically trypsin, for example, the Caesalpinia echinata trypsin inhibitor (CeKI); can also inhibit only chymotrypsin or both enzymes . Based on stoichiometric studies, we demonstrated that PeTI is a single-headed Kunitz inhibitor with higher activity against trypsin than chymotrypsin.…”

Section: Discussionmentioning

confidence: 99%

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Novel Peptidase Kunitz Inhibitor from Platypodium elegans Seeds Is Active against Spodoptera frugiperda Larvae

Ramalho¹,

Bezerra²,

Oliveira³

et al. 2018

J. Agric. Food Chem.

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A novel Kunitz-type inhibitor from Platypodium elegans seeds (PeTI) was purified and characterized. The mass spectrometry analyses of PeTI indicated an intact mass of 19 701 Da and a partial sequence homologous to Kunitz inhibitors. PeTI was purified by ion exchange and affinity chromatographies. A complex with a 1:1 ratio was obtained only for bovine trypsin, showing a K = 0.16 nM. Stability studies showed that PeTI was stable over a wide range of temperature (37-80 °C) and pH (2-10). The inhibitory activity of PeTI was affected by dithiothreitol (DTT). Bioassays of PeTI on Spodoptera frugiperda showed negative effects on larval development and weight gain, besides extending the insect life cycle. The activities of digestive enzymes, trypsin and chymotrypsin, were reduced by feeding larvae with 0.2% PeTI in an artificial diet. In summary, we describe a novel Kunitz inhibitor with promising biotechnological potential for pest control.

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Section: ■ Discussionmentioning

confidence: 94%

Section: ■ Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Novel Peptidase Kunitz Inhibitor from Platypodium elegans Seeds Is Active against Spodoptera frugiperda Larvae

Ramalho¹,

Bezerra²,

Oliveira³

et al. 2018

J. Agric. Food Chem.

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“…Kabau peas belong to the Fabaceae family, mostly found in tropical regions such as Indonesia, Thailand, Malaysia, and the Philippines [ 1 ]. Kabau is categorized as an indigenous Indonesian plant and is commonly found in Sumatra and Kalimantan.…”

Section: Introductionmentioning

confidence: 99%

“…However, it is also stated that Kabau contains a significant amount of antinutritional components. These antinutritional components include trypsin inhibitors [ 1 , 5 , 6 ], tannin, and hemagglutinin [ 5 ]. Tannin, trypsin inhibitor, and hemagglutinin of Kabau are 0.46 g/100 g wet weight, 12.5 TIU/ml, and 1280 HU/g wet weight, respectively [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Conventional Processing Affects Nutritional and Antinutritional Components and In Vitro Protein Digestibility in Kabau (Archidendron bubalinum)

Fitriani

Santoso

Supriyadi

2021

International Journal of Food Science

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Kabau, an unexplored crop, was analyzed to determine its nutrition and antinutrition components and in vitro protein digestibility (IVPD). Some conventional processes, such as steaming, frying, and boiling, were carried out to study their effect. The results indicated that all of the techniques reduced carbohydrate content. Frying significantly increased the fat content of Kabau and reduced other nutritional components. In general, all the methods significantly reduced phytic acid, tannin, and trypsin inhibitors, as much as 94.95–96.26%, 20–35%, and 89.22–92.88%, respectively. The reduction of antinutritional components resulted in higher IVPD on boiled and steamed Kabau, 69.47% and 61.48%, respectively.

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A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

et al. 2010

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Kunitz-type trypsin inhibitors from legume seeds have been characterized structurally. The presence of Cys-Cys in single or double chains shows a new pattern of proteins structurally not so closely related to STI. Therefore, briefly, with regard to cysteine content, plant Kunitz proteinase inhibitors may be classified into four groups: no Cys-Cys at all, one, two and more than two Cys residues. Functional properties and diversity of these proteins are also briefly discussed.

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Exploring the protease mediated conformational stability in a trypsin inhibitor from Archidendron ellipticum seeds

Cited by 6 publications

References 30 publications

Novel Peptidase Kunitz Inhibitor from Platypodium elegans Seeds Is Active against Spodoptera frugiperda Larvae

Novel Peptidase Kunitz Inhibitor from Platypodium elegans Seeds Is Active against Spodoptera frugiperda Larvae

Conventional Processing Affects Nutritional and Antinutritional Components and In Vitro Protein Digestibility in Kabau (Archidendron bubalinum)

A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

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