Purificación y caracterización parcial de una proteasa del polen de Acacia caven

CRISTINA BARCIA, PEDRO CURTO, RUI CRUZ, ANA LEAL, RAQUELVINHAS, SONIA BARBERIS Y PAULA VERÍSSIMO.

Montevideo

Encuentro; IV Encuentro Regional de Biocatálisis y Biotransformaciones (IV EnReBB).; 2010

Red Latinoamericana de Biocatálisis y Biotransformaciones (IV EnReBB).

Acacia caven (Mol.) Molina belongs to the Fabaceae family and its respective pollen is used perfumery, as a dietary supplement, or as a drug. The purpose of this work was to purify and characterize the proteases released by hydration of the pollen of Acacia caven. The protocol to extract proteins from pollen grains was optimized. The pigments presents in the soluble extract were separated through exclusion chromatography. Were determined by SDS-PAGE two proteins with a molecular mass of 50 and 75 kDa. The protein with a mass molecular close to 75 kDa showed proteolytic activity (zymography) and degraded characteristic substrates for aminopeptidases. Further studies must be conducted for the best characterization of this protease.