Purification and properties of phenolic acid decarboxylase from Candida guilliermondii.
作者： Hui-Kai Huang , Masamichi Tokashiki , Sayaka Maeno , Shoko Onaga , Toki Taira
DOI: 10.1007/S10295-011-0998-4
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摘要: 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 20 kDa sodium dodecyl sulfate–polyacrylamide gel electrophoresis and 36 kDa gel-filtration chromatography, suggesting that the enzyme is a homodimer. optimal pH temperature were approximately 6.0 25°C. Characteristically, more than 50% activity observed at 0°C, this cold-adapted. converted p-coumaric acid, ferulic caffeic corresponding products with high specific activities 600, 530, 46 U/mg, respectively. stimulated Mg2+ ions, whereas it completely inhibited Fe2+, Ni2+, Cu2+, Hg2+, 4-chloromericuribenzoate, N-bromosuccinimide, diethyl pyrocarbonate. inducible expressed inside cells moderately significantly non-metabolizable 6-hydroxy-2-naphthoic acid.
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