Title : Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase - Faulds_1993_Biotechnol.Appl.Biochem_17_349 |
Author(s) : Faulds CB , Williamson G |
Ref : Biotechnol Appl Biochem , 17 :349 , 1993 |
Abstract :
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. |
PubMedSearch : Faulds_1993_Biotechnol.Appl.Biochem_17_349 |
PubMedID: 8338641 |
Faulds CB, Williamson G (1993)
Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase
Biotechnol Appl Biochem
17 :349
Faulds CB, Williamson G (1993)
Biotechnol Appl Biochem
17 :349