Abstract
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 significantly as a lipase; it exhibits no detectable activity on triglycerides, and has 10 5 -fold to 10 6 -fold lower activity than Rhizopus niveus lipase on diglycerides. Conversely, lipases exhibit ∼ 2.5 x 10 6 -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) -α-9-arabinofuranosyl]-(1 → 3)-O-β-3-xylopyranosyl-(1 → 4)-3-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 significant lipase activity, and lipases exhibit no significant ferulic acid esterase activity.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
