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Purification and Characteristics of Feruloyl Esterase from Aspergillus awamori G‐2 Strain
Author(s) -
Kanauchi M.,
Watanabe S.,
Tsukada T.,
Atta K.,
Kakuta T.,
Koizumi T.
Publication year - 2008
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2008.00839.x
Subject(s) - aspergillus awamori , chemistry , esterase , chromatography , ion chromatography , starch , enzyme , enzyme assay , xylan , biochemistry
For food industry production processes and other uses, a mold that produces high levels of feruloyl esterase was obtained from laboratory mold collections and other sources. It was Aspergillus awamori G‐2 that produces high levels of feruloyl esterase. The feruloyl esterase was purified using ion‐exchange chromatography, size‐exclusion chromatography, and HPLC chromatography. The enzyme was identified as a monomer protein using size‐exclusion chromatography. Its optimum temperature and pH were, respectively, 40 °C and pH 5. Its activity was stable at pH 3 to 5. The enzyme was combined with xylan and starch, but it was absorbed by cellulose. The km of the feruloyl esterase was 0.0019% (0.01 mM). The enzyme showed stable activity at pH 3 and 50 °C, making this enzyme useful for food production.