Purification and properties of tyrosinases from Vibrio tyrosinaticus1
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Biochemical characterization of a tyrosinase from Bacillus aryabhattai and its application
2021, International Journal of Biological MacromoleculesCitation Excerpt :The purified rTYR indicated a relatively 1.76-fold higher substrate affinity for l-tyrosine than l-DOPA. And the Km value of rTYR for l-tyrosine as substrate was generally very similar to tyrosinases from bacteria such as R. etil CFN42 (0.19 mM) [5], and P. putida F6 (0.23 mM) [12], lower than that of Vibrio tyrosinaticus tyrosinase (3.1 mM) [34], B. thuringiensis tyrosinase (0.563 mM) [23], and Candidatus Nitrosopumilus koreensis tyrosinase (9.2 mM) [35], and higher than that of B. megaterium tyrosinase (0.075 mM) [14]. Meanwhile, the Km value of rTYR for l-DOPA was lower than the value reported for tyrosinases from B. thuringiensis (0.768 mM) [23], C. Nitrosopumilus koreensis (2.6 mM) [35], S. castaneoglobisporus (8.1 mM) [36], and P. putida F6 (0.33 mM) [12].
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2014, Journal of BiotechnologyCitation Excerpt :For staining of PAG for tyrosinase activity, a reaction mixture of 2 mM 3-(3,4-dihydroxyphenyl)-l-alanine (l-DOPA; Serva, Germany) and 50 mM Tris–HCl (pH 7.5) was used. Brown bands corresponding to tyrosinase developed within 10 min (Pomerantz and Murthy, 1974). The molecular masses of the proteins were determined as described by Weber and Osborn (1969).
Biochemical characterisation of the coexisting tyrosinase and laccase in the soil bacterium Pseudomonas putida F6
2007, Enzyme and Microbial TechnologyIsolation and biochemical characterization of laccase and tyrosinase activities in a novel melanogenic soil bacterium
2006, Enzyme and Microbial TechnologyExpression of the melA gene from Rhizobium etli CFN42 in Escherichia coli and characterization of the encoded tyrosinase
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This research was supported by Research Grant CA-07093 from the National Cancer Institute, National Institutes of Health. A portion of this work is derived from a Dissertation presented by V. V. Murthy to the Graduate School of the University of Maryland in 1968 in partial fulfillment of the Ph.D. degree.