Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins
Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatograp...
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1100/2012/562715 |
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| author | Priscila Praxedes-Garcia Ilana Cruz-Silva Andrezza Justino Gozzo Viviane Abreu Nunes Ricardo José Torquato Aparecida Sadae Tanaka Rita de Cássia Figueiredo-Ribeiro Yamile Gonzalez Gonzalez Mariana da Silva Araújo |
| author_facet | Priscila Praxedes-Garcia Ilana Cruz-Silva Andrezza Justino Gozzo Viviane Abreu Nunes Ricardo José Torquato Aparecida Sadae Tanaka Rita de Cássia Figueiredo-Ribeiro Yamile Gonzalez Gonzalez Mariana da Silva Araújo |
| author_sort | Priscila Praxedes-Garcia |
| collection | DOAJ |
| description | Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (Km 55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until 50∘C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−, SO4 2−, and CH3COO−) or chaotropic cations (K+ and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins. |
| format | Article |
| id | doaj-art-2f71b5706dfe40a2904c161f97f7bc5e |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-2f71b5706dfe40a2904c161f97f7bc5e2025-02-03T01:33:07ZengWileyThe Scientific World Journal1537-744X2012-01-01201210.1100/2012/562715562715Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage ProteinsPriscila Praxedes-Garcia0Ilana Cruz-Silva1Andrezza Justino Gozzo2Viviane Abreu Nunes3Ricardo José Torquato4Aparecida Sadae Tanaka5Rita de Cássia Figueiredo-Ribeiro6Yamile Gonzalez Gonzalez7Mariana da Silva Araújo8Department of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilDepartment of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilDepartment of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilSchool of Arts, Sciences, and Humanities, Universidade de São Paulo, 03828-000 São Paulo, SP, BrazilDepartment of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilDepartment of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilSection of Plant Physiology and Biochemistry, Instituto de Botânica de São Paulo, 04045-972 São Paulo, SP, BrazilCenter of Protein Study, Facultad de Biología, Universidad de la Habana, 10400 Havana, CubaDepartment of Biochemistry, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, BrazilSeveral proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (Km 55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until 50∘C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−, SO4 2−, and CH3COO−) or chaotropic cations (K+ and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins.http://dx.doi.org/10.1100/2012/562715 |
| spellingShingle | Priscila Praxedes-Garcia Ilana Cruz-Silva Andrezza Justino Gozzo Viviane Abreu Nunes Ricardo José Torquato Aparecida Sadae Tanaka Rita de Cássia Figueiredo-Ribeiro Yamile Gonzalez Gonzalez Mariana da Silva Araújo Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins The Scientific World Journal |
| title | Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins |
| title_full | Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins |
| title_fullStr | Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins |
| title_full_unstemmed | Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins |
| title_short | Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins |
| title_sort | biochemical aspects of a serine protease from caesalpinia echinata lam brazilwood seeds a potential tool to access the mobilization of seed storage proteins |
| url | http://dx.doi.org/10.1100/2012/562715 |
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