TY - JOUR
T1 - Synthesis and Characterization of Cross-Linked Aggregates of Peroxidase from Megathyrsus maximus (Guinea Grass) and Their Application for Indigo Carmine Decolorization
AU - Perez, Angie V.
AU - Gaitan-Oyola, Jorge A.
AU - Vargas-Delgadillo, Diana P.
AU - Castillo, John J.
AU - Barbosa, Oveimar
AU - Fernandez-Lafuente, Roberto
N1 - Publisher Copyright:
© 2024 by the authors.
PY - 2024/6
Y1 - 2024/6
N2 - We present the synthesis of a cross-linking enzyme aggregate (CLEAS) of a peroxidase from Megathyrsus maximus (Guinea Grass) (GGP). The biocatalyst was produced using 50%v/v ethanol and 0.88%w/v glutaraldehyde for 1 h under stirring. The immobilization yield was 93.74% and the specific activity was 36.75 U mg−1. 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 H2O2 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.
AB - We present the synthesis of a cross-linking enzyme aggregate (CLEAS) of a peroxidase from Megathyrsus maximus (Guinea Grass) (GGP). The biocatalyst was produced using 50%v/v ethanol and 0.88%w/v glutaraldehyde for 1 h under stirring. The immobilization yield was 93.74% and the specific activity was 36.75 U mg−1. 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 H2O2 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.
KW - CLEAS
KW - guinea grass peroxidase
KW - indigo carmine
UR - http://www.scopus.com/inward/record.url?scp=85195867348&partnerID=8YFLogxK
U2 - 10.3390/molecules29112696
DO - 10.3390/molecules29112696
M3 - Artículo Científico
AN - SCOPUS:85195867348
SN - 1420-3049
VL - 29
JO - Molecules
JF - Molecules
IS - 11
M1 - 2696
ER -