Purification and Characteristics of Feruloyl Esterase from Aspergillus awamori G-2 Strain |
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Authors: | M Kanauchi S Watanabe T Tsukada K Atta T Kakuta T Koizumi |
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Affiliation: | Author Kanauchi is with Dept. of Food Management, Miyagi Univ. 2-2-1 Hatatate, Taihaku-ku, Sendai, Miyagi, Japan 982-0215. Authors Watanabe, Tsukada, Kakuta, and Koizumi are with Dept. of Fermentation, Tokyo Univ. of Agriculture 1-1-1 Sakuragaoka, Setagaya, Tokyo, Japan 156-8502. Author Atta is with Chuko Distillers Corp., 132 Nakachi, Tomigusuku City, Okinawa, Japan. Direct inquiries to author Kanauchi (E-mail: ). |
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Abstract: | ABSTRACT: 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. |
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Keywords: | Aspergillus awamori ferulic acid feruloyl esterase purification |
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