What question did this study set out to answer?

This research aims to evaluate the kinetics, stability, and dye degradation abilities of peroxidase derived from Carica papaya fruit peel.

June 20, 2026Open Access

A novel Carica papaya fruit peel peroxidase: kinetics, stability, and dye degradation

Puntos clave

This research aims to evaluate the kinetics, stability, and dye degradation abilities of peroxidase derived from Carica papaya fruit peel.
Assessed peroxidase activity under different conditions, including pH and temperature.
Measured the enzyme's stability after heat treatment and its dye decolorization efficacy.
Utilized various dyes including malachite green, eriochrome black T, and methyl orange for evaluation.
Peroxidase retained 98.2% activity at pH 7 and 40 °C for 30 min, reducing to 49.8% after 90 min.
Achieved up to 88.09% decolorization of malachite green.
Demonstrated good stability and significant dye-decolorizing ability, indicating its potential for cost-effective biotechnological uses.

Resumen

activated the enzyme. The enzyme retained 98.2% of its original activity after incubation at pH 7 and 40 °C for 30 min, while 49.8% was retained after 90 min. Peroxidase decolorized malachite green (up to 88.09%), eriochrome black T, local, methyl orange, methylene blue, and geni dyes. Hence, Carica papaya fruit peel peroxidase exhibited good stability after heat treatment. Meanwhile, the pronounced dye-decolorizing ability and the sustainable source of this peroxidase make it robust and cost-effective for biotechnological applications.

Preguntar a la IA

Me gusta

Guardar

Ver artículo completo