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.
Authors
- Ozoemena Emmanuel Eje (ORCID: https://orcid.org/0000-0001-8680-6117)
- Okpanachi N. Oyibo
- Arinze L. Ezugwu
- Rachael C. Chinweuba
- Ferdinand C. Chilaka
- Immaculata A. Eze
Institutions
- University of Nigeria (NG)
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
- 0.00