@article{mbs:/content/journal/micro/10.1099/00221287-140-4-779, author = "Faulds, Craig B. and Williamson, Gary", title = "Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose", journal= "Microbiology", year = "1994", volume = "140", number = "4", pages = "779-787", doi = "https://doi.org/10.1099/00221287-140-4-779", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-140-4-779", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "Aspergillus niger", keywords = "Streptomyces olivochromogenes", keywords = "xylanase", keywords = "ferulic acid esterase", abstract = "An inducible ferulic acid esterase (FAE-III) has been isolated, purified and partially characterized from Aspergillus niger after growth on oat spelt xylan. The purification procedure utilized ammonium sulphate precipitation, hydrophobic interaction and anion-exchange chromatography. The purified enzyme appeared almost pure by SDS-PAGE, with an apparent M r of 36000. A single band, corresponding to a pl of 3·3 was observed on isoelectric focusing. With methyl ferulate as substrate, the enzyme had a specific activity of 67 IU (mg protein)−1, pH and temperature optima of 5 and 55–60 °C, respectively, and a Km of 2·08 mM and a V max of 175 μmol min−1 (mg protein)−1. The enzyme was also active upon methyl sinapinate, methyl-3,4-dimethoxy cinnamate and methyl p-coumarate, but not benzoic acid methyl esters or methyl caffeate. Similarly, Streptomyces olivochromogenes FAE showed activity against methyl ferulate, methyl sinapinate and methyl p-coumarate, but at a level 420-fold less (on methyl ferulate) than the A. niger esterase. No activity was detected against the benzoate methyl esters. For both enzymes, this shows the necessity for C-3 on the phenol ring to be methoxylated and the aliphatic region of the substrate to be unsaturated. The specific activity of FAE-III on destarched wheat bran was 31 U (mg protein)−1 in the presence of Trichoderma viride xylanase and 3 U (mg protein)−1 in the absence. Apparent pH dependent binding of A. niger FAE-III to microcrystalline cellulose was also demonstrated.", }