Kinetic modeling of the enzymatic hydrolysis of proteins of visceras from red tilapia (Oreochromis sp): effect if substrate and enzyme concentration / Modelado de la cinética de la hidrolisis enzimática de proteínas de vísceras de tilapia roja (Oreochromis sp): efecto de la concentración de enzima y de sustrato

Background: the growth of world aquaculture has generated important environmental impacts as discard residues that are important sources of protein, which has been used to manufacture low-value products, such as animal food, fish flour and fertilizers. Objectives: to evaluate the effect of enzyme and substrate concentration on the degree of hydrolysis (DH) of proteins in the red tilapia (Oreochromis sp.) viscera (RTV). Methods: the commercial alcalase 2.4 L enzyme was used at different concentrations to hydrolyse the proteins in RTV at 53.5°C and a pH of 9.5 in a 1 L magnetically stirred, jacketed, glass batch reactor connected to an automatic titrator. Each experiment was conducted over 6 h in which every consumed volume of base was recorded every 5 min to determine the corresponding DH at each point. Results: the results indicated that increasing the enzyme concentration produced an increase in the DH and in the reaction rate, while increasing the substrate concentration produced a decrease in both parameters. For this reason, a mathematical model was adjusted for the inhibition of substrate from the exponential kinetic equation d(DH)/dt = a* EXP[-b* (DH)] to explain the behavior of the DH as a function of substrate concentration in this hydrolytic process. The parameters a and b were estimated from a nonlinear regression. Based on these results, the reaction constants were determined as Ks = 456.75 g L-1, K2 = 1.2191 min-1, Kd = 0.2224 min-1, KM = 1.8963 and K3 = 0.1173 L g-1 min-1, which allowed the generation of a good correlation between the predicted and experimental values at the different evaluated operating conditions. This correlation was supported by a low average relative error (ARE) of 3.26%. Conclusion: under evaluated experimental conditions, the kinetics of the hydrolysis reaction followed a substrate inhibition mechanism without product inhibition, which was adjusted through a typical exponential Equation that involves two parameters (a and b) associated with the kinetic constants (Ks, K2, and Kd).

Antecedentes: el crecimiento de la acuicultura en el mundo ha provocado importantes impactos ambientales como el descarte de residuos que son importantes fuentes de proteína, los cuales han sido usados para manufacturar productos de bajo valor tales como: alimento para animales, harina de pescado y fertilizantes. Objetivo: evaluar el efecto de la concentración de enzima y de sustrato sobre el grado de hidrolisis (GH) de las proteínas presentes en las vísceras de tilapia roja (Oreochromis sp.) (VTR). Métodos: se empleó la enzima commercial alcalasa 2.4 L a diferentes concentraciones para hidrolizar las proteínas presentes en la VTR a 53°C y a un pH de 9.5 en un reactor de vidrio de 1 L con chaqueta, magnéticamente agitado y conectado a un titulador automático. Cada experimento se llevó cabo por 6 h registrando cada 5 min el volumen de base cosumido para determinar el grado de hidrolisis correspondiente a cada punto. Resultados: los resultados indicaron que un incremento en la concentración de enzima producía un incremento en el GH y en la velocidad de reacción, mientras que un aumento en la concentración de sustrato provocaba una disminución en ambos parámetros. Por esta razón, se ajustó un modelo matemático para la inhibición de sustrato a partir de la ecuación de cinética exponencial d(GH)/dt = a*EXP[-b*(GH)] para explicar el comportamiento del GH como una función de la concentración de sustrato en este proceso hidrolítico. Los parámetros a y b fueron evaluados mediante una regresión no lineal. Con base en estos resultados, las constantes de reacción fueron determinadas como Ks = 456.75 g L-1, K2 = 1.2191 min-1, Kd = 0.2224 min-1, KM = 1.8963 and K3 = 0.1173 L g-1 min-1, los cuales permitieron obtener una buena correlación entre los valores experimentales y los predichos a las diferentes condiciones de operación. Esta correlación fue soportada por un bajo error medio relativo del 3.26%. Conclusión: bajo las condiciones experimentales evaluadas, la cinética de la reacción de hidrólisis siguió un mecanismo de inhibición por sustrato sin inhibición por producto, el cual fue ajustado mediante una ecuación típica exponencial que involucra dos parámetros (a and b) asociados a las constantes cinéticas Ks, K2, and Kd.

Biodegradation kinetics of o-cresol by Pseudomonas putida DSM 548 (pJP4) and o-cresol removal in a batch-recirculation bioreactor system

The biodegradation kinetics of o-cresol was examined by acclimatized P. putida DSM 548 (pJP4) in batch experiments at varying initial o-cresol concentrations (from 50 to 500 mg/L). The kinetic parameters of o-cresol aerobic biodegradation were estimated by using the Haldane substrate inhibition equation. The biodegradation kinetics of o-cresol was investigated. In batch culture reactors, the Maximum specific growth rate (μmax), Monod constant (Ks) and the inhibition constant (Ki) were established as 0.519 h-1, 223.84 mg/L and 130.883 mg/L, respectively. o-cresol biodegradation in a batch-recirculation bioreactor system by immobilized P. putida was also studied. The recycled packed bed reactor system, which was composed of Ca-alginate beads and pumice on which cells immobilized, has been performed to determine possible stability for further developments.

Catechol biodegradation kinetics using Candida parapsilopsis

This study evaluated the biodegradation of catechol by a yeast strain of Candida parapsilopsis in standard medium in Erlenmeyer flasks. Results shown that the highest concentration of catechol caused the longer lag period, demonstrating that acclimatized cultures could completely degrade an initial catechol concentration of 910 mg/L within 48 h. Haldane's model validated the experimental data adequately for growth kinetics over the studied catechol concentration ranges of 36 to 910 mg/L. The constants obtained for this model were µmax = 0.246 h-1, Ks = 16.95 mg/L and Ki = 604.85 mg/L.

Neste trabalho foi estudada a biodegradação de catecol em frascos de Erlenmeyers em água residuária sintética pela levedura Candida parapsilopsis. As respostas dos ensaios cinéticos mostraram que altas concentrações de catecol ocasionaram uma fase lag longa para a levedura. Portanto, a aclimatização da cultura de levedura empregada para biodegradação de catecol é de fundamental importância, sendo possível reduzir toda a concentração inicial de catecol da água residuária sintética de 910 mg/L em 48 horas. Os dados experimentais da cinética de biodegradação do catecol foram ajustados pelo modelo de Haldane adequadamente, sobre a faixa de concentração de catecol investigada de 36 a 910 mg/L. Os parâmetros cinéticos obtidos do modelo de Haldane foram: µmax = 0,246 h-1, Ks = 16,95 mg/L e Ki = 604,85 mg/L.