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KMID : 0380020140290010001
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Korean Journal of Biotechnology and Bioengineering
2014 Volume.29 No. 1 p.1 ~ p.8
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Recent Advances in Tyrosinase Research as An Industrial Enzyme
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Kim Hye-Rin
Kim Hyun-Mi
Choi Yoo-Seong
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Abstract
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Tyrosinases catalyze the hydroxylation of monophenolic compounds and the conversion of o-diphenols to o-quinones. The enzymes are mainly involved in the modification of tyrosine into L-3,4-dihydroxyphenyl-alanine (L-DOPA) and DOPA/DOPAquinone-drived intermolecular cross-linking, which play the key roles of pigmentation to the cells. It is ubiquitously distributed in microorganisms, plants, and animals all around the nature world. They are classified as copper- containing dioxygen activating enzymes; two copper ions are coordinated with six histidine residues in their active sites and they are distinguished as met-, deoxy-, and oxy-form depending on their oxidative states. Natural extraction and recombinant protein approaches have been tried to obtain practical amounts of the enzymes for industrial application. Tyrosinases have been widely applied to industrial and biomedical usages such as detoxification of waste water containing phenolic compounds, L-DOPA as a drug of Parkinson’s disease, biomaterials preparation based on the cross-linking ability and biosensors for the detection of phenolic compounds. Therefore, this review reports the mechanism of tyrosinase, biochemical and structural features and potential applications in industrial field.
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KEYWORD
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Enzyme, Tyrosinase, Monophenolase, Diphenolase
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