Four peroxidases and four laccases were compared as to reaction rates catalysed with six phenolic substrates of relevance to the plant cell wall. When each phenolic substrate was tested at 670 mu M and pH 6.0, in the presence of 670 mu M H2O2 Or similar to 270 mu M O-2 as the electron acceptor, all the peroxidases and laccases had similar substrate preferences: reaction rates were in the order sinapyl > coniferyl > p-coumaryl alcohols, and feruloyl >p-coumaroyl esters. Specific activities were in the order basic peroxidase > acidic peroxidase>>laccase. The data are consistent with the view that peroxidases rather than laccases play a major role in phenolic cross-linking in the cell wall. (C) 1999 Elsevier Science Ltd. All rights reserved.
|Number of pages||5|
|Publication status||Published - Nov 1999|