Produção Nacional
Revisado por pares
Gamma trypsin: Purification and physicochemical characterization of a novel bovine trypsin isoform
2014; Elsevier BV; Volume: 70; Linguagem: Inglês
10.1016/j.ijbiomac.2014.06.050
ISSN1879-0003
AutoresCaroline Dutra Lacerda, Antônio Ernani. Teixeira, Jamil S. Oliveira, Silvana Fontoura Silva, Antônio Victor Baioco Vasconcelos, Débora Gonçalves Gouveia, Cleiseano Emanuel da Silva Paniagua, Marcelo M. Santoro, Marcos Mares-Guia, Alexandre Martins Costa Santos,
Tópico(s)Enzyme-mediated dye degradation
ResumoA novel bovine trypsin isoform was purified from commercial sample by ion exchange chromatography by Sephadex SP C50®. New isoform contains 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 γ-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, γ-trypsin preferably has a lower rate formation from β-trypsin, a lower surface charge, but the γ-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, this enzyme becomes an interesting alternative for the food industry, detergent and biocatalysis research.
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