Ecology, Environment and Conservation Paper


Vol.30, August Suppl. Issue, 2024

Page Number: S411-S416

ISOLATION, IDENTIFICATION AND OPTIMIZATION OF TYROSINASE ENZYME FROM NEWLY IDENTIFIED FUSARIUM SPECIES

Chethan M.P., Bhavana D., Shivarudraswamy D.2, Soundarya Shree K.R., Kumar J.R., Guru Kumar D. and Nagalambika Prasad

Abstract

Tyrosinases (monophenol, di-phenol oxygen oxidoreductase, EC (1.14.18.1) are the copper- containing enzymes which catalyze the o-hydroxylation of monophenols and even subsequent oxidation of di-phenols to quinones. These enzymes are involved in pigmentation and are the important factors in wound mending and primary immune response. Tyrosinases are found in eukaryotic and prokaryotic microorganisms, in invertebrates, mammals and plants. Fusarium are included in the Nectriaceae family and represents one among the most important genus of the Hypocreales order ascribable to its impactful number of species and their practical part. In fungi, tyrosinases are basically associated with the formation and stability of spores, in defense and acridity mechanisms, and in browning and saturation. First characterized from the comestible mushroom Agaricus bisporus because of undesirable enzymatic browning problems during postharvest storage, tyrosinases were introduced, more recently, in several other fungi with relative insights into molecular and inheritable characteristics and into reaction mechanisms, pointing their veritably promising properties for biotechnological operations.