Abstract
The enzymatic reactivation process enables the recovery of catalytic activity for inactive biocatalysts. However, its effect on the specific productivity of the processes has not been studied. The main objective of this work was to evaluate the specific productivity of the processes with and without reactivation using the program Spyder Python (3.7). Using fixed values for all of the parameters, the global specific productivity was 8 mM/h·gbiocat for the process without reactivation, and 4 mM/h·gbiocat for the process with reactivation. Random numbers were generated to use as different values for parameters, and the results yielded a global specific productivity of 3.79 mM/h·gbiocat for the process with reactivation and 3.68 mM/h·gbiocat for the process without reactivation. ANOVA tests showed that there were significant differences between the specific global productivities of the two processes. Reactivation has great potential for use when the biocatalyst is of high cost.
Highlights
Enzymes are biological catalysts that offer advantages over conventional chemical catalysts due to their high specificity, high activity under moderate reaction conditions, high rotation number and biodegradability [1]
Obtained through using data work reported in the field. These works simulations were chosen because therefrom are few investigations in which kinetic parameters have been were determined in the enzymatic reactivation processes
The parameters and starting data arein the chosen because there are few investigations in which kinetic parameters have been determined summarized in enzymatic reactivation processes
Summary
Enzymes are biological catalysts that offer advantages over conventional chemical catalysts due to their high specificity, high activity under moderate reaction conditions, high rotation number and biodegradability [1]. The global enzyme market is projected to grow from USD 5.01 billion in 2016 to USD 6.32 billion in 2021 [1,3] Due to their biological nature, the enzymes used are labile and their activity and stability is affected in the presence of aggressive conditions of pH, temperature [4] and organic solvents [5]. In aqueous media, polar amino acids at the surface are exposed to interactions with the solvent, while the non-polar amino acids are located internally, interacting more with each other Due to this form of folding, it is proposed that one of the main factors that determines protein stability is the hydrophobic interaction of the internal three-dimensional structure [10], which counteracts the surface forces that tend to alter the Processes 2020, 8, 1419; doi:10.3390/pr8111419 www.mdpi.com/journal/processes
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