Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase
Faulds, C.B.; Williamson, G.
Biotechnology and Applied Biochemistry 17(3): 349-359
1993
ISSN/ISBN: 0885-4513 PMID: 8338641 Document Number: 408791
Two forms of ferulic acid esterase from Aspergillus niger have been isolated from a commercial source of pectinase. One, designated I, has a M-r of 132,000, is probably dimeric, and has a pI of 3.0. The second, designated II, was partially purified and is monomeric (M-r 29,0 000), with a pI of 3.6. Both enzymes were free of pectinase and xylanase activity and released ferulic acid from methyl ferulate. In association with a xylanase, they also released ferulic acid from destarched wheat bran. Ferulic acid esterase II released a small amount of ferulic acid (0.09 unit/mg of protein) in the absence of xylanase. The enzymes had different specificities for a range of methyl ester derivatives of cinnamoyl and benzoyl acids, acetylated xylan and p-nitrophenyl acetate.