IMBICE   05372
INSTITUTO MULTIDISCIPLINARIO DE BIOLOGIA CELULAR
Unidad Ejecutora - UE
artículos
Título:
The Proteolytic Activity of Philibertia gilliesii Latex. Purification of Philibertain g II
Autor/es:
SEQUEIROS C; CAFFINI NO; TREJO SA; TORRES, MARÍA JOSÉ; NATALUCCI CL; NIEVAS ML; LÓPEZ LMI
Revista:
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Editorial:
HUMANA PRESS INC
Referencias:
Lugar: Oregon; Año: 2016 vol. 179 p. 332 - 346
ISSN:
0273-2289
Resumen:
Abstract The latex from the patagonic plant Philibertia gilliesii Hook. et Arn.(Apocynaceae) is a milky-white suspension containing a proteolytic system constitutedby several cysteine endopeptidases. A proteolytic preparation (philibertain g) from thelatex of P. gilliesii fruits was obtained and characterized to evaluate its potential use inbioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activityof 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7?10 range, retained 80 % of the original activity after 2 h of incubation at temperaturesranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain gretained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteinsfrom stickwater one, of the main waste effluents generated during fishmeal production.Furthermore, as a contribution to the knowledge of the proteolytic system of P. gilliesii, weare reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecularmass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain gthrough a purification scheme including acetone fractionation, cation exchange, molecularexclusion chromatography, and ultrafiltration.