Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase

CB Faulds, G. Williamson

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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) 29,000), 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. 1993 The Swiss Political Science Review

Original languageEnglish
Pages (from-to)349-359
Number of pages11
JournalBiotechnology and Applied Biochemistry
Issue number3
Publication statusPublished - 1 Jan 1993
Externally publishedYes

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