Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes, Camila de Carvalho; Barbosa, Aulus Estevão Anjos de Deus; Macedo, Leonardo Lima Pepino; Pitanga, J. C.M.; Moura, Fabiano Tavares de; Oliveira, Adeliana S.; Moura, Raniere M.; Queiroz, Alexandre F.S.; Macedo, Francisco P.; Andrade, Lucia B. S.; Vidal, Márcia Soares; Sales, Maurı́cio P.

doi:10.1016/j.plaphy.2005.11.004

Cited by 80 publications

(63 citation statements)

References 59 publications

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“…The relative stability of trypsin inhibitors was possible due to intramolecular disulfide bridges. These bridges can retain the functional stability of trypsin inhibitors in the presence of physical and chemical denaturants such as temperature, pH and reducing agents (Gomes et al 2005). Our results indicated that L. sativus inhibitor has a high intrinsic stability due to the presence of possible disulfide bridges.…”

Section: Discussionmentioning

confidence: 66%

Protease Inhibitor From the Crude Extract of Plant Seeds Affects the Digestive Proteases in Hyphantria Cunea (Lep.: Arctiidae)

Aghaali¹,

Ghadamyari²,

Hosseininaveh³

et al. 2013

Journal of Plant Protection Research

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Proteases are one of the most important digestive enzymes in the midgut of Hyphantria cunea Drury. Proteases are responsible for protein digestion. In the present study, we evaluated the efficiency of some plant inhibitors on proteases in the gut of the H. cunea. Last instar larvae were collected from mulberry trees. The digestive system of the larvae was used as an enzyme source. The total proteolytic and trypsin activity were assessed by the hemoglobin and BApNA, respectively, as the substrate. The evaluation of the total proteolytic and trypsin activities in various pHs showed the highest relative activity at a pH of 11. Also, the inhibitory effect of inhibitors extracted from Alhagi maurorum Medik., Lathyrus sativus L., Vicia faba L., Prosopis farcta (Banks & Sol.) Eig., and Panicum miliaceum L. on the digestive protease of the fall webworm was measured. Protease inhibitors extracted from A. maurorum, P. farcta and P. miliaceum showed negligible inhibition but L. sativus was able to inhibit 34.72% and 100% of the total activity of proteolytic and trypsin, respectively. Also, the total proteolytic and trypsin activities were inhibited by the inhibitor from V. faba, at 22.27% and 100%, respectively. The zymogram pattern of trypsin with nitro-cellulose membranes showed 2 isoforms in the gut of H. cunea. The inhibitor from L. sativus completely inhibited both isoforms. Gel electrophoresis of proteolitytic activity revealed at least 6 isoforms the inhibitor extracted from L. sativus; completely inhibiting some of them. The inhibitor from L. sativus was purified by ammonium sulfate precipitation and gel-filtration. The molecular mass of the inhibitor was determined as 45 kDa. The highest inhibition of trypsin activity by the inhibitor from L. sativus occurred at a pH of 10. The stability of the inhibitor from L. sativus was evaluated at different pHs and temperatures. The results showed that the inhibitor from L. sativus was stable at a pH of 11.0, and showed 45% inhibition on trypsin activity at a pH of 11. Also, this inhibitor revealed stability up to 50°C.

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Section: Discussionmentioning

confidence: 66%

Protease Inhibitor From the Crude Extract of Plant Seeds Affects the Digestive Proteases in Hyphantria Cunea (Lep.: Arctiidae)

Aghaali¹,

Ghadamyari²,

Hosseininaveh³

et al. 2013

Journal of Plant Protection Research

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“…In general, Fabaceae seeds have high levels of protease inhibitors and these molecules have been purifi ed from several legume species (Gomes et al 2005, Migliolo et al 2010, Paula et al 2012, Chevreuil et al 2014. For example, in Pithecelobium dumosum, two trypsin inhibitors were purifi ed (Oliveira et al 2007) and in Poincianella pyramidalis seeds, a Kunitz inhibitor with insecticide effect was isolated (Guimarães et al 2015).…”

Section: Discussionmentioning

confidence: 99%

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Brito

Melo

Alves

et al. 2016

Hoehnea

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-(Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions). The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds. Keywords: antimicrobial, cystatin, Fabaceae, protease RESUMO -(Purificação parcial de um inibidor de tripsina/papaína de sementes de Hymenaea courbaril L. e atividade antibacteriana de suas frações proteicas). O extrato bruto e frações proteicas de sementes de Hymenaea courbaril foram investigados para a presença de inibidores de tripsina e papaína e atividade antimicrobiana contra Vibrio parahaemolyticus, Staphylococcus aureus e Escherichia coli. As frações foram obtidas após precipitação do extrato bruto com sulfato de amônio em três faixas de saturação (0-30%, 30-60% e 60-90%) e denominadas Hc030, Hc3060 e Hc6090, respectivamente. O extrato bruto e as frações apresentaram diferente especificidade em inibir a atividade da tripsina e papaína. A atividade antimicrobiana foi observada nas frações Hc030 e Hc3060 e somente contra V. parahaemolyticus. O inibidor isolado a partir de Hc3060 foi mais eficiente na inibição da tripsina (100% de inibição) do que da papaína (54% de inibição), e mostrou uma massa molecular aparente de 20 kDa. Este estudo mostra que as sementes de H. courbaril possuem inibidores de proteases e proteínas com atividade antibacteriana, indicando que a espécie é uma fonte de compostos bioativos.

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“…Protease inhibitors when incorporated into artificial diets or expressed in transgenic plants increase mortality [174] and reduce the growth and development of larvae from many insect pest species including Coleoptera [175,176], Orthoptera [177] and Lepidoptera [178,179] (Table 2). The mechanisms by which ingested PIs mediate their effects on insect physiology differs between insect species [180].…”

Section: Mechanism Of Action Of Protease Inhibitors On Lepidopteran Imentioning

confidence: 99%

Biotechnological Approaches for the Control of Insect Pests in Crop Plants

Stevens¹,

Dunse²,

Fox³

et al. 2012

Pesticides - Advances in Chemical and Botanical Pesticides

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Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Cited by 80 publications

References 59 publications

Protease Inhibitor From the Crude Extract of Plant Seeds Affects the Digestive Proteases in Hyphantria Cunea (Lep.: Arctiidae)

Protease Inhibitor From the Crude Extract of Plant Seeds Affects the Digestive Proteases in Hyphantria Cunea (Lep.: Arctiidae)

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Biotechnological Approaches for the Control of Insect Pests in Crop Plants

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