Caracterização físico-química da isoforma γ-tripsina bovina

• Ano de defesa: 2014
• Autor(a) principal: Lacerda, Caroline Dutra
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal do Espírito Santo; BR; Mestrado em Bioquímica e Farmacologia; Centro de Ciências da Saúde; UFES; Programa de Pós-Graduação em Bioquímica e Farmacologia
• Palavras-chave em Português: Isoformas de proteínas; Ativação enzimática; Físico-química; Tripsina; Farmacologia Bioquímica e Molecular; 61
• Link de acesso: http://repositorio.ufes.br/handle/10/1976

A novel bovine trypsin isoform was purified from commercial sample by ion exchange chromatography by Sephadex SP C50®. New isoform contain in addition of loss of N- terminus hexapeptide (as found in parent molecule β-trypsin) an intra-chain split between Lys-155 and Ser-156. The novel enzyme denominate gamma-trypsin showed similar properties with α-trypsin isoform in: polypeptide number chain (two chain), molecular masses (23,312 Da), secondary structure, hydrodynamic radius and others. In spite of enzymatic and structural similarities of both isoforms, -trypsin preferably has a lower rate formation from β-trypsin, a lower surface charge, but the gamma-trypsin has a higher thermal stability than α-trypsin. Due to obtaining facility of purification of bovine trypsin isoforms from commercial font, and properties described above, become this enzyme an interesting alternative for the food industry, detergent and biocatalysis research.