Synthesis and Characterization of Cross-Linked Aggregates of Peroxidase from (Guinea Grass) and Their Application for Indigo Carmine Decolorization

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2024 Jun 19

PMID 38893568

Authors

Angie V Perez

Jorge A Gaitan-Oyola

Diana P Vargas-Delgadillo

John J Castillo

Oveimar Barbosa

Roberto Fernandez-Lafuente

Affiliations

Soon will be listed here.

Abstract

We present the synthesis of a cross-linking enzyme aggregate (CLEAS) of a peroxidase from (Guinea Grass) (GGP). The biocatalyst was produced using 50%/ ethanol and 0.88%/ glutaraldehyde for 1 h under stirring. The immobilization yield was 93.74% and the specific activity was 36.75 U mg. The biocatalyst surpassed by 61% the free enzyme activity at the optimal pH value (pH 6 for both preparations), becoming this increase in activity almost 10-fold at pH 9. GGP-CLEAS exhibited a higher thermal stability (2-4 folds) and was more stable towards hydrogen peroxide than the free enzyme (2-3 folds). GGP-CLEAS removes over 80% of 0.05 mM indigo carmine at pH 5, in the presence of 0.55 mM HO after 60 min of reaction, a much higher value than when using the free enzyme. The operational stability showed a decrease of enzyme activity (over 60% in 4 cycles), very likely related to suicide inhibition.

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