Purification and characterization of a feruloylesterase from Aspergillus awamori
A feruloylesterase was purified from the extracellular broth of Aspergillus awamori grown on wheat bran culture. The purified enzyme gave a single band on SDS-polyacrylamide gel electrophoresis and isoelectric focusing, with an apparent Mr of 35,000 and a pI of 3.8, respectively. The substrate speci...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998-10, Vol.62 (10), p.2032-2034 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A feruloylesterase was purified from the extracellular broth of Aspergillus awamori grown on wheat bran culture. The purified enzyme gave a single band on SDS-polyacrylamide gel electrophoresis and isoelectric focusing, with an apparent Mr of 35,000 and a pI of 3.8, respectively. The substrate specificity of the purified enzyme differed obviously from that of acetylesterase of A. awamori. The enzyme bound to microcrystalline cellulose |
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ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.62.2032 |