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Bacterial tyrosinases: old enzymes with new relevance to biotechnology

Paper ID Volume ID Publish Year Pages File Format Full-Text
33435 44978 2012 9 PDF Available
Title
Bacterial tyrosinases: old enzymes with new relevance to biotechnology
Abstract

Tyrosinases are copper-containing dioxygen activating enzymes found in many species of bacteria and are usually associated with melanin production. These proteins have a strong preference for phenolic and diphenolic substrates and are somewhat limited in their reaction scope, always producing an activated quinone as product. Despite this fact they have potential in several biotechnological applications, including the production of novel mixed melanins, protein cross-linking, phenolic biosensors, production of l-DOPA, phenol and dye removal and biocatalysis. Although most studies have used Streptomyces sp. enzymes, there are several other examples of these proteins that are also of potential interest. For instance a solvent tolerant enzyme has been described, as well as an enzyme with both tyrosinase and laccase activities, enzymes with altered substrate preferences, an enzyme produced as an inactive zymogen as well as examples which do not require auxiliary proteins for copper insertion (unlike the Streptomyces sp. enzymes which do require such a protein). This article will summarise the reports on the biotechnological applications of bacterial tyrosinases as well as the current information available on the different types of this enzyme.

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Bacterial tyrosinases: old enzymes with new relevance to biotechnology
Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 29, Issue 2, 15 January 2012, Pages 183–191
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering