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

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.

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Publication Details

Journal
BMC Biotechnology
Published
2026-06-17
DOI
https://doi.org/10.1186/s12896-026-01178-2
Primary Topic
Enzyme-mediated dye degradation
Type
article
Field-Weighted Citation Impact
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article

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

Ozoemena Emmanuel Eje, Okpanachi N. Oyibo, Arinze L. Ezugwu, Rachael C. Chinweuba et al.
BMC Biotechnology
Enzyme-mediated dye degradation
article

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

Ozoemena Emmanuel Eje, Okpanachi N. Oyibo, Arinze L. Ezugwu, Rachael C. Chinweuba, Ferdinand C. Chilaka, Immaculata A. Eze
article en

Abstract

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.

BMC Biotechnology
University of Nigeria (NG)
Zero hunger
Openalex Percentile: Top 9%
Enzyme-mediated dye degradation
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