Detect and partially purify trypsin inhibitor from Aesculus hippocastanum (Indian chestnut) seeds

Farias M.F.A.M.S1; Patriota L.L.S2; Procópio T.F2; Paiva P.M.G3; Santos N.D.L4; Napoleão T.H3

1Estudante do Curso de Biomedicina – UFPE,2Doutoranda em Bioquímica e Fisiologia; 3Docente do Departamento de Bioquímica da UFPE. 4Pesquisadora do Departamento de Bioquímica da UFPE.

Introduction: Plants have several mechanisms of defense against phytopathogens, being one of them formation of defense proteins, such as protease inhibitors. Objectives: The objective of this work was to detect and partially purify trypsin inhibitor from Aesculus hippocastanum (Indian chestnut) seeds. Methodology: The A. hippocastanum seed powder was submitted to saline extraction in 0.15 M NaCl (10% w/v). The extract was evaluated for trypsin inhibitor activity and protein concentration and to chromatography on DEAE-Sephadex column equilibrated with 0.1 M Tris-HCl pH 8.0 and eluted with the same buffer containing 1.0 M NaCl. The obtained peaks were dialyzed and evaluated for trypsin inhibitory activity. Results and Discussion: Saline extract (4 mg/mL of protein) showed a specific trypsin inhibitory activity (STIA) of 149.57 U/mg. The pool of proteins adsorbed on DEAE-Sephadex matrix showed high STIA (1280.31 U/mg), corresponding to a purification factor of 8.5. Conclusion: Seeds of A. hippocastanum possess a trypsin inhibitor that was partially purified by ion exchange chromatography.

Keywords:  Indian chestnut; trypsin inhibitor; protein purification.

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How to cite this article:
Farias M.F.A.M.S; Patriota L.L.S; Procópio T.F; Paiva P.M.G; Santos N.D.L; Napoleão T.H.Detect and partially purify trypsin inhibitor from Aesculus hippocastanum (Indian chestnut) seeds.American Journal of Ophthalmic Research and Reviews, 2018, 1:3. DOI:10.28933/ajoorr-2018-06-1803

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