Abstract
Tyrosinase is a copper-containing metalloprotein that catalyzes the oxidation of tyrosine, in particular, L-DOPA to L-Dopaquinone, which are precursors of brown pigments in some wounded eukaryotic tissues. The present study focused on screening, production and characterization of tyrosinase from multi-enzyme producing Fusarium solani B1 and Fumago sp. A total of 25 strains were isolated from rotting wood samples and screened for hydrolytic and oxidative multi-enzyme potentials using different polymeric substrates. The two most consistent strains: Fusarium solani B1 and Fumago sp. B13 were further evaluated for tyrosinase production. Some media cultural parameters and physiological conditions were optimized in order to maximize tyrosinase production. Incubation of Fumago sp. B13 and Fusarium solani B1 for 96 and 144 h in medium containing 2 % and 0.2 % ratios of Glucose and NaNO3 with pH 6 and 7, respectively, was most suitable for tyrosinase production. Characterization of the partially purified tyrosinase from Fumago sp. B13 and Fusarium solani B1 exhibited optimal activities at pH 6-7, 30 °C, and 1 mM Cu2+, respectively, thereby suggesting their potentials for novel biotechnological applications.
Highlights
With the advent of biotechnology, there has been a growing interest and demand for enzymes with novel properties
A total of 25 fungi were isolated from rotting wood samples, where five (B1, B9, B13, B18, and B23) demonstrated consistent multi-enzyme characteristics by producing different zones of hydrolysis or oxidation on the screening substrates: starch, cellulose, tannic acid, pectin, casein, gum acacia, and tyrosine (Table 1)
Among these five isolates, the most consistent multi-enzyme activity was observed with isolates B1 and
Summary
With the advent of biotechnology, there has been a growing interest and demand for enzymes with novel properties. Considerable efforts are being directed towards the selection of microorganisms producing enzymes with enhanced catalytic properties and tolerance to extreme conditions charactersitic of industrial processes, such as temperature, salts, pH and many others. The potentials of using fungi as biotechnological sources of industrially relevant enzymes have stimulated interest in the exploration of their extracellular enzyme activity. Multienzymes could be produced through their induction on exposure to certain cultural conditions [1], through engineered microbes with multi-functions [2], through mixed culture of microbes [3], or through directed evolution of enzymes [4]. Notwithstanding, pure enzyme extracts might still contain trivial amounts of a variety of accessory enzymes, which may be responsible for their multicatalytic potentials
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