Duniesky Martínez

Learn More
Enzymes for use in the sugar industry are preferred to be thermotolerant. In this study, a synthetic codon-optimized gene encoding a highly thermostable β-fructosidase (BfrA, EC from the bacterium Thermotoga maritima was expressed in the yeast Pichia pastoris. The gradual increase of the transgene dosage from one to four copies under the control(More)
Thermotoga maritima exo-β-fructosidase (BfrA) secreted by a recombinant Pichia pastoris strain was optimally immobilised on Glyoxyl-Sepharose CL 4B using the Rational Design of Immobilised Derivatives (RDID) strategy. Covalent attachment of the N-glycosylated BfrA onto the activated support at pH 10 allowed total recovery of the loaded enzyme and its(More)
BACKGROUND An ideal immobilized biocatalyst for the industrial-scale production of invert sugar should stably operate at elevated temperatures (60-70°C) and high sucrose concentrations (above 60%, w/v). Commercial invertase from the yeast Saccharomyces cerevisiae is thermolabile and suffers from substrate inhibition. Thermotoga maritima β-fructosidase(More)
Culture supernatants from the rice pathogenic fungus Pyricularia grisea were characterized by general proteolytic assays. Protease activity, as measured by azocasein hydrolysis, peaked over a pH range of 7.0 9.0 with an optimum at pH 8.0. This, together with the results from zymograms of gelatin-containing SDS-PAGE gels combine with specific protease(More)
  • 1