Biochemical Aspects of a Serine Protease from<i>Caesalpinia echinata</i>Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

Praxedes-Garcia, Priscila; Cruz-Silva, Ilana; Gozzo, Andrezza Justino; Nunes, Viviane Abreu; Torquato, Ricardo J.S.; Tanaka, Aparecida S.; Figueiredo-Ribeiro, Rita de Cássia L.; González, Yoel Martínez; Araújo, Mariana da Silva

doi:10.1100/2012/562715

Cited by 8 publications

(4 citation statements)

References 36 publications

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“…For example, gel spots 8, 15, and 26; are all GME273_g isoforms. The presence of three lower molecular weight isoforms (< 9 kDa) of GME273_g (spots 13, 28, and 38) suggests the plausible degradation of GME273_g by the relatively large quantity of serine proteases in the initiation of the storage proteins mobilization 30 , 31 .…”

Section: Discussionmentioning

confidence: 99%

Genome-based Proteomic Analysis of Lignosus rhinocerotis (Cooke) Ryvarden Sclerotium

Yap¹,

Fung²,

Ng³

et al. 2015

Int. J. Med. Sci.

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Lignosus rhinocerotis (Cooke) Ryvarden (Polyporales, Basidiomycota), also known as the tiger milk mushroom, has received much interest in recent years owing to its wide-range ethnobotanical uses and the recent success in its domestication. The sclerotium is the part with medicinal value. Using two-dimensional gel electrophoresis coupled with mass spectrometry analysis, a total of 16 non-redundant, major proteins were identified with high confidence level in L. rhinocerotis sclerotium based on its genome as custom mapping database. Some of these proteins, such as the putative lectins, immunomodulatory proteins, superoxide dismutase, and aegerolysin may have pharmaceutical potential; while others are involved in nutrient mobilization and the protective antioxidant mechanism in the sclerotium. The findings from this study provide a molecular basis for future research on potential pharmacologically active proteins of L. rhinocerotis.

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Section: Discussionmentioning

confidence: 99%

Genome-based Proteomic Analysis of Lignosus rhinocerotis (Cooke) Ryvarden Sclerotium

Yap¹,

Fung²,

Ng³

et al. 2015

Int. J. Med. Sci.

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“…Furthemore, those molecules as a source of sulfur amino acids, and/or have been associated with defense against insect and pathogen attack (Klomklao et al 2011, Martínez et al 2012, Praxedes-Garcia 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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“…Secondary peaks between 5.0 and 6.5 were also noticed in these extracts, supporting the idea that the principal peptidase activity is due to serine or metalloproteases, but with some other types of proteases also present. Serine protease activities are the most abundant proteases in all living organisms, including plants as in species of the Leguminosae family [ 12 , 23 , 27 – 29 ].…”

Section: Resultsmentioning

confidence: 99%

Proteases fromCanavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

Gonçalves

Barbosa

Silva-López

2016

Biotechnology Research International

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Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. ensiformis proteases exhibited molecular masses of about 200–57, 40–37, and 20–15 kDa by SDS-PAGE analysis. These enzymes cleaved hemoglobin, bovine serum albumin, casein, and gelatin at different levels. Serine and metalloproteases are the major proteases in C. ensiformis extracts, modulated by divalent cations, stable at 1% of surfactant Triton X-100 and at different concentrations of the reducing agent β-mercaptoethanol. Thus, C. ensiformis expresses a particular set of proteases in distinctive organs with high activity and stability, making this legume an important source of proteases with biotechnological potential.

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Biochemical Aspects of a Serine Protease fromCaesalpinia echinataLam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

Cited by 8 publications

References 36 publications

Genome-based Proteomic Analysis of Lignosus rhinocerotis (Cooke) Ryvarden Sclerotium

Genome-based Proteomic Analysis of Lignosus rhinocerotis (Cooke) Ryvarden Sclerotium

Partial purification of trypsin inhibitors from Parkia seeds (Fabaceae)

Proteases fromCanavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

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