: The nine closest matches of the deduced primary sequence of ferulic acid esterase (FAE-III/ FAEA) from Aspergillus niger to any other proteins in a redundant database were with fungal lipases (32-26% identity). In this paper we show that FAE-III does not function signiücantly as a lipase ; it exhibits no detectable activity on triglycerides, and has 105-fold to 106-fold lower activity than Rhizopus niveus lipase on diglycerides. Conversely, lipases exhibit ¿ 2.5 Â 106-fold lower ferulic acid esterase activity on methyl ferulate compared to FAE-III. Further, lipases possess no detectable activity on O- [ 5-O-(trans-feruloyl)-a--arabinofuranosyl ] -(1 Ç 3)-O-b-‰-xylopyranosyl-(1 Ç 4)-‰-xylopyranose (FAXX), which is the substrate with the highest catalytic efficiency so far reported for FAE-III. These results show that FAE-III exhibits no signiücant lipase activity, and lipases exhibit no signiücant ferulic acid esterase activity.
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