Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus

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Abstract
Fumarate hydratase (EC 4.2.1.2) from the extremely thermophilic archaeobacterium Solfolobus solfataricus has been purified to homogeneity by a rapid purification procedure using affinity chromatography and high-performance size-exclusion chromatography, and the enzyme''s physicl and biochemical properties have been determined. The native enzyme has a molecular mass of 170 kDa and is composed of identical subunits with a moleuclar mass of 45 kDa, thus indicating a tetrameric structure similar to fumarases isolated from other organisms. The enzyme as active at temperatures ranging from 40.degree. C to 90.degree. C, with a maximum activity at 85.degree. C. The pH optimum for generation of fumarate was found to be pH 8.0. The enzyme showed high stability to denaturation by heat ad organic solvents.