Authors : Sheetal Patil; Neelakanth M Jeedi; Savita S Desai

Volume/Issue : Volume 10 - 2025, Issue 7 - July

Google Scholar : https://tinyurl.com/2u7528mj

DOI : https://doi.org/10.38124/ijisrt/25jul226

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Abstract : Tyrosinase (EC 1.14.18.1), a copper-containing bifunctional enzyme, catalyzes the hydroxylation of monophenols to o-diphenols and their oxi- dation to o-quinones, playing key roles in melanin synthesis, L-DOPA pro- duction, and bioremediation of phenolic compounds. This study aimed to isolate, purify, and characterize tyrosinase-producing microorganisms from freshwater soil and water samples in Ahmednagar, India. Samples were enriched on tyrosine-containing media, and black-brown pigment for- mation was used to screen for tyrosinase activity. Among the isolates, the most promising was identified as Brevundimonas diminuta by 16S rRNA gene sequencing. Tyrosinase was partially purified via ammonium sulfate precipitation and dialysis, and characterized for pH, temperature, metal ion effects, and substrate concentration. The enzyme showed optimal ac- tivity at pH 7.0 and 37°C, with increased activity in the presence of Cu2+. Kinetic analysis revealed Michaelis–Menten constants in line with other bacterial tyrosinases. This work highlights the biotechnological potential of B. diminuta tyrosinase in environmental and pharmaceutical applica- tions.

Keywords : Tyrosinase, Brevundimonas Diminuta, L-DOPA, Bioremedia- Tion, Enzyme Characterization.

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