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Purification and characterization of hydroxycinnamate decarboxylase from Brettanomyces anomalus

Edlin, DA, Narbad, A, Gasson, MJ, Dickinson, JR and Lloyd, D 1998. Purification and characterization of hydroxycinnamate decarboxylase from Brettanomyces anomalus. Enzyme and Microbial Technology 22 (4) , 232--239. 10.1016/S0141-0229(97)00169-5

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Abstract

The yeast, Brettanomyces anomalus, produces a hydroxycinnamic acid decarboxylase which is active toward ferulic acid, p-coumaric acid, and caffeic acid. The enzyme transforms these hydroxycinnamic acids to hydroxystyrenes by the removal of the carboxyl group from the C3 side chain. We have purified this enzyme 235-fold from B. anomalus NCYC 615 using Mono ion exchange, Phenyl Superose, and Superose 12 column chromatography. Enzyme activity was found to be optimal at 40°C and pH 6.0 and was enhanced by EDTA, Mg2+, and Cr3+. Fe3+, Ag+, and SDS completely inhibited the activity. Kinetic studies indicated a Km of 1.15 mm and a Vmax of 13,494 nmol min−1 mg−1 for ferulic acid and a Km of 1.55 mM and a Vmax of 22,256 nmol min−1 mg−1 for p-coumaric acid. Using gel filtration, an apparent molecular mass of 39.8 kDa was estimated. The decarboxylase was inactive toward both o- and m-coumaric acid and toward cinnamic acid, indicating that the para-hydroxy group is essential for activity.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Elsevier
ISSN: 0141-0229
Date of Acceptance: 5 August 1997
Last Modified: 05 Mar 2020 16:00
URI: http://orca.cf.ac.uk/id/eprint/127777

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