| Purification and properties of phenolic acid decarboxylase from Candida guilliermondii. | |
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MedLine Citation:
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PMID: 21681484 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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A heat-labile phenolic acid decarboxylase from Candida guilliermondii (an anamorph of Pichia guilliermondii) was purified to homogeneity by simple successive column chromatography within 3 days. The molecular mass was 20 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 36 kDa by gel-filtration chromatography, suggesting that the purified enzyme is a homodimer. The optimal pH and temperature were approximately 6.0 and 25°C. Characteristically, more than 50% of the optimal activity was observed at 0°C, suggesting that this enzyme is cold-adapted. The enzyme converted p-coumaric acid, ferulic acid, and caffeic acid to corresponding products with high specific activities of approximately 600, 530, and 46 U/mg, respectively. The activity was stimulated by Mg(2+) ions, whereas it was completely inhibited by Fe(2+), Ni(2+), Cu(2+), Hg(2+), 4-chloromericuribenzoate, N-bromosuccinimide, and diethyl pyrocarbonate. The enzyme was inducible and expressed inside the cells moderately by ferulic acid and p-coumaric acid and significantly by non-metabolizable 6-hydroxy-2-naphthoic acid. |
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Authors:
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Hui-Kai Huang; Masamichi Tokashiki; Sayaka Maeno; Shoko Onaga; Toki Taira; Susumu Ito |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-6-17 |
Journal Detail:
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Title: Journal of industrial microbiology & biotechnology Volume: - ISSN: 1476-5535 ISO Abbreviation: - Publication Date: 2011 Jun |
Date Detail:
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Created Date: 2011-6-17 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9705544 Medline TA: J Ind Microbiol Biotechnol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima, Kagoshima, 890-8580, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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