Experimental Design Optimization and Decolorization of an Azo Dye by Cross-Linked Peroxidase Aggregates

Year 2021, Volume: 31 Issue: 1, 34 - 42, 31.03.2021

Fatma Ayhan , Oguz Akpolat

https://doi.org/10.32710/tekstilvekonfeksiyon.498774

Cited By: 1

Abstract

The immobilization of
horseradish peroxidase in the form of cross-linked enzyme aggregates
(HRP–CLEAs) was optimized by three parameters full factorial experimental
design at two levels and the degradation of an azo dye was tested. The optimal
immobilization conditions were estimated as 0.06 mg enzyme/mL (0.96 U), 3 % (v/v,
Glutaraldehyde)) cross-linker ratio, and 6 mg /mL Bovine Serume Albumine amount,
respectively. The effects of variables were analysed by responce surface plots
and the enzyme concentration effect was insignificant for the tested levels. The
maximum CLEAs activity was 0.2188 U and the kinetic parameters (K_m
and V_max) were 0.0314 mM and 0.1044 mM/min while the calculated
values for soluble enzyme were 0.06 mM and 0.468 mM/min, respectively. Hydrogen
peroxide has inhibitory effect on enzyme aggregate activities at higher amounts
than 0.012 mM. Under optimal conditions, a textile azo dye, Reactive Blue 160
was completely oxidized within 90 h and higher temperatures also showed promising
results in dye degradation.  

Keywords

Cross-Linked Enzyme Aggregates (CLEAs), Horseradish Peroxidase, Full Factorial Design, Decolorization

References

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