Changes in enzymes involved in suberisation in elicitor-treated french bean cells

Abstract

Transfer of ferulic acid from feruloyl-CoA onto polymeric material can be readily demonstrated by microsomal membranes from suspension-cultured cells of French bean. Transfer onto endogenous components present in the microsomal preparations can be supplemented by addition of polysaccharide or lipid components. However, addition of catalase to reaction mixtures suppresses transfer onto polysaccharide components, indicating that this is peroxidative. In contrast, suppression of microsomal peroxidase activities leads to increased transfer onto hydroxy-hexadecanoic acid showing that any transferase is possibly specific for lipid and therefore involved in suberisation. This transferase was transiently induced by elicitation of the cells. The time course of induction was similar to that for the cytochrome P450, laurate ω-hydroxylase required for the hydroxylation of fatty acids. Solubilisation and partial purification of the transferase was accomplished and indicated an enzyme with a tendency to aggregate but with a probable minimum subunit M r of 40 000. © 1997 Elsevier Science Ltd. All rights reserved