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SHR Neuro Krebs Kardio Lipid

Biundo, A; Braunschmid, V; Pretzler, M; Kampatsikas, I; Darnhofer, B; Birner-Gruenberger, R; Rompel, A; Ribitsch, D; Guebitz, GM.
Polyphenol oxidases exhibit promiscuous proteolytic activity
COMMUN CHEM. 2020; 3(1): 62
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Autor/innen der Med Uni Graz:
Birner-Grünberger Ruth
Darnhofer Barbara

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Tyrosinases are an industrially significant class of polyphenol oxidase. Here, two tyrosinases are shown to cleave a specific peptide bond in a carboxylesterase, yielding a truncated product with higher catalytic activity than the full-length enzyme. Tyrosinases catalyse both the cresolase and catecholase reactions for the formation of reactive compounds which are very important for industrial applications. In this study, we describe a proteolytic activity of tyrosinases. Two different tyrosinases originating from mushroom and apple are able to cleave the carboxylesterase EstA. The cleavage reaction correlates with the integrity of the active site of tyrosinase and is independent of other possible influencing factors, which could be present in the reaction. Therefore, the cleavage of EstA represents a novel functionality of tyrosinases. EstA was previously reported to degrade synthetic polyesters, albeit slowly. However, the EstA truncated by tyrosinase shows higher degradation activity on the non-biodegradable polyester polyethylene terephthalate (PET), which is a well-established environmental threat.

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