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Ferulic acid esterase‐III from Aspergillus niger does not exhibit lipase activity
Author(s) -
Aliwan Fraj O,
Kroon Paul A,
Faulds Craig B,
Pickersgill Richard,
Williamson Gary
Publication year - 1999
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(19990301)79:3<457::aid-jsfa283>3.0.co;2-g
Subject(s) - ferulic acid , lipase , esterase , aspergillus niger , rhizopus oryzae , chemistry , triacylglycerol lipase , biochemistry , enzyme , fermentation
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 ∽2.5×10 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‐ L ‐arabinofuranosyl]‐(1→3)–O–β‐ D ‐xylopyranosyl‐(1→4)‐ D ‐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. © 1999 Society of Chemical Industry