Kinetic Constants of Recombinant POXA 1B.pdf (18.91 kB)

Kinetic constants complete results.

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posted on 2016-05-03, 03:44 authored by Claudia M. Rivera-HoyosClaudia M. Rivera-Hoyos, Edwin D. Morales-Álvarez, Angela M. Cardozo-Bernal, Diego A. Albarracín-Pardo, Raúl A. Poutou-Piñales, Aura M. Pedroza-Rodríguez, Dennis Díaz, Alexander Rodríguez, Carlos J. Alméciga-Díaz, Refugio Rodríguez-Vázquez, Claudia L. Cuervo-Patiño

Enzyme kinetics of pure recombinant POXA 1B was characterized using ABTS as a substrate. Maximum velocity values (V_max), substrate affinity or Michaelis constant (Km), catalytic constant or turnover number (K_cat), and kinetic efficiency (specificity constant K_cat/Km) also were found.

Funding

This research was funded by Grants 00005575 and 00006337 from Pontificia Universidad Javeriana, and 00006169 (Jóven Investigador Colciencias 2015), Bogotá, D.C. Colombia. Financing entityhad no role in the study design, data collection, or analysis, decis

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Keywords

enzyme kinetics measurements Recombinant Proteins laccase production Media optimization POXA 1 B constitutive expression Biotechnology

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CC BY 4.0

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