Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase.
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.
Faulds
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Department of Food Molecular Biochemistry, AFRC Institute of Food Research, Norwich Laboratory, U.K.
Williamson
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D001234:Aspergillus niger / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002853:Chromatography, Liquid / Q000379:methods; D007525:Isoelectric Focusing; D008970:Molecular Weight; D011096:Polygalacturonase / Q000737:chemistry*; D013379:Substrate Specificity
D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase; D011096:Polygalacturonase