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Production of a Novel Laccase from Ceratorhiza Hydrophila and Assessing Its Potential in Natural Dye Fixation and Cytotoxicity Against Tumor Cells

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Specialty Biotechnology
Date 2023 Feb 9
PMID 36757585
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Abstract

Background: Flavonoid natural dyes have gained attention because they are nontoxic and eco-friendly. However, they do not work effectively with artificial fibers and require the use of mordants, which are considered as hazardous chemicals. Laccase enzyme catalyzes the oxidation of phenols, forming phenoxyl radicals that undergo a further polymerization process. So, laccase can oxidize flavonoid dyes, and it can be used instead of harmful mordants in flavonoid dye fixation on cotton fabrics. Laccases also are involved in a variety of metabolic processes, and they have anti-proliferative effects toward HepG2 and MCF-7 tumor cells.

Results: Among fifteen fungal isolates, the fungus Ceratorhiza hydrophila isolated from the submerged plant Myriophyllum spicatum was selected as the most potent laccase producer. Optimization of the production medium resulted in a 9.9-fold increase in laccase productivity. The partially purified Ceratorhiza hydrophila laccase could successfully improve the affinity of cotton fabrics toward quercetin (flavonoid) dye with excellent color fastness properties. The partially purified laccase also showed anti-proliferative activity against HepG2 and MCF-7 tumor cells. However, high laccase concentration is required to estimate IC50.

Conclusions: Ceratorhiza hydrophila MK387081 is an excellent laccase producer. The partially purified laccase from Ceratorhiza hydrophila can be used in textile dyeing and printing processes as a safer alternative to the conventional hazardous mordants. Also, it can be used in preparation of cancer treatment drugs. However, further studies are needed to investigate IC50 for both cell types at higher laccase concentrations.

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PMID: 40085415 DOI: 10.1007/s11033-025-10416-3.

References
1.
Muthukumarasamy N, Jackson B, Raj A, Sevanan M . Production of Extracellular Laccase from Bacillus subtilis MTCC 2414 Using Agroresidues as a Potential Substrate. Biochem Res Int. 2015; 2015:765190. PMC: 4584229. DOI: 10.1155/2015/765190. View

2.
da Cunha M, Barbosa A, Giese E, Dekker R . The effect of carbohydrate carbon sources on the production of constitutive and inducible laccases by Botryosphaeria sp. J Basic Microbiol. 2003; 43(5):385-92. DOI: 10.1002/jobm.200310250. View

3.
Lam S, Han Q, Ng T . Isolation and characterization of a lectin with potentially exploitable activities from caper (Capparis spinosa) seeds. Biosci Rep. 2008; 29(5):293-9. DOI: 10.1042/BSR20080110. View

4.
Bourbonnais R, Paice M . Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett. 1990; 267(1):99-102. DOI: 10.1016/0014-5793(90)80298-w. View

5.
Wang H, Ng T . Purification of a novel low-molecular-mass laccase with HIV-1 reverse transcriptase inhibitory activity from the mushroom Tricholoma giganteum. Biochem Biophys Res Commun. 2004; 315(2):450-4. DOI: 10.1016/j.bbrc.2004.01.064. View