A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

Oliva, Maria Luiza Vilela; Silva, Mariana C.C.; Sallai, Roberto Carlos; Brito, Marlon Vilela de; Sampaio, Misako U.

doi:10.1016/j.biochi.2010.03.021

Cited by 103 publications

(88 citation statements)

References 105 publications

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“…I. laurina extracts have shown antioxidant [13] and antiplasmodial activities [14]. Additionally, a proteolytic inhibitor was found in their seeds and exhibited inhibitory activity of the trypsin enzyme [12,15], thus acting in this way as a pest control against Homalinotus coriaceus, Diatraea saccharalis and Heliothis virescens [16,17]. Species of the Inga genus are practically unexplored regarding the characterization of its essential oils and their biological activities.…”

Section: Introductionmentioning

confidence: 99%

Seasonal Variation of the Chemical Composition and Antimicrobial and Cytotoxic Activities of the Essential Oils from Inga laurina (Sw.) Willd.

et al. 2014

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Abstract:The seasonal chemical composition of essential oils from Inga laurina was determined by GC/MS. In the stem bark's essential oil extracted during the dry season, the presence of terpenoids (30.05%) stood out, and phytol (9.76%) was the major compound identified. For the stem bark oil obtained during the rainy season, in addition to terpenoids (26.63%), a large amount of fatty acids (46.84%) were identified, in particular palmitic acid (25.40%). Regarding the leaves' essential oil obtained in the dry season, esters (42.35%) were the main components. The main ester present was (Z)-hex-3-enyl benzoate (10.15%) and the major compound of this oil was (Z)-hex-3-en-1-ol (14.23%). Terpenoids for aerobic bacteria, and high selectivity against bacteria was observed. The large amount of fatty acids in rainy season oils may be related to the better inhibitory effects observed.

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Section: Introductionmentioning

confidence: 99%

Seasonal Variation of the Chemical Composition and Antimicrobial and Cytotoxic Activities of the Essential Oils from Inga laurina (Sw.) Willd.

et al. 2014

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“…Conversely, members of the Kunitz family have a molecular mass ranging from 18 to 26 kDa, with one or two polypeptide chains cross-linked by one to three disulfide bonds. These protease inhibitors usually have one reactive site, but recently a secondary reactive site has been observed (Oliva et al 2010, Oliveira et al 2012.…”

Section: Introductionmentioning

confidence: 99%

Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Chevreuil

Gonçalves

Calderon³

et al. 2014

Hoehnea

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-(Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)). Leguminous seeds (Fabaceae) have a high content of inhibitors of which serine protease inhibitors are the most widely studied. However, there are only a few studies related to the investigation of these proteins in tree species belonging to the Amazon flora. The protein content presented in seeds of four Amazonian Leguminosae species, Parkia pendula, P. discolor, P. multijuga and P. Nitida, was extracted by using NaCl 0.15 mol L -1 and then partially fractionated by using affinity chromatography performed on a trypsinSepharose 4B. These inhibitors presented different affinities between trypsin and chymotrypsin serine proteases, showing a higher inhibition to trypsin compared to chymotrypsin, except for P. nitida, which showed high inhibition against both enzymes. The SDS-PAGE analysis showed that the species from Parkia genus have a main band corresponding to partially purified trypsin inhibitors. The apparent molecular mass inhibitors (approximately 13-18 kDa) and the high specificity for trypsin suggest the occurrence of Bowman-Birk and Kunitz type inhibitors. Keywords: Amazonia, Bowman-Birk inhibitor, Kunitz inhibitor, leguminous seeds, serine protease RESUMO -(Purificação parcial de inibidores de tripsina de sementes de Parkia (Fabaceae)). Sementes de leguminosas (Fabaceae) apresentam alto conteúdo de inibidores, incluindo os inibidores de serinoproteinases que têm sido extensivamente estudados. Todavia, poucos estudos foram realizados quanto à investigação dessas proteínas em espécies arbóreas pertencentes à flora amazônica. As proteínas presentes nas sementes de quatro espécies de leguminosas da Amazônia, Parkia pendula, P. discolor, P. multijuga e P. nitida, foram obtidas pela extração usando NaCl 0.15 mol L -1 e, parcialmente purificadas usando a cromatografia de afinidade em tripsina-Sepharose 4B. Os inibidores exibiram afinidades diferentes entre a tripsina e a quimotripsina, exceto para P. nitida, a qual apresentou alta inibição contra as duas enzimas. A análise em SDS-PAGE mostrou que as espécies do gênero Parkia contém uma banda principal correspondendo aos inibidores de tripsina parcialmente purificados. As massas moleculares aparentes determinadas para os inibidores (aproximadamente, 13 a 18 kDa) e a alta especificidade pela tripsina sugerem a ocorrência de inibidores do tipo Bowman-Birk e Kunitz. Palavras-chave: Amazônia, Inibidor Bowman-Birk, Inibidor Kunitz, sementes de leguminosas, serinoproteinase 1.

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“…courbaril crude seed extracts have been investigated for the presence of trypsin inhibitors and have been found to possess strong inhibitory activity (Caramori et al 2004) but, to our knowledge, this is the fi rst report of a trypsin/papain inhibitor isolated from jatobá seeds. The molecular mass found in ITHc of approximately 20 kDa is similar to the trypsin inhibitors of the Kunitz family, which generally have a molecular mass between 18 and 24 kDa (Oliva et al 2010, Guimarães et al 2015.…”

Section: Discussionmentioning

confidence: 75%

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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A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

Cited by 103 publications

References 105 publications

Seasonal Variation of the Chemical Composition and Antimicrobial and Cytotoxic Activities of the Essential Oils from Inga laurina (Sw.) Willd.

Seasonal Variation of the Chemical Composition and Antimicrobial and Cytotoxic Activities of the Essential Oils from Inga laurina (Sw.) Willd.

Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

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

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