1887

Abstract

Fumarate hydratase (EC 4.2.1.2) from the extremely thermophilic archaeobacterium has been purified to homogeneity by a rapid purification procedure using affinity chromatography and high-performance size-exclusion chromatography, and the enzyme’s physical and biochemical properties have been determined. The native enzyme has a molecular mass of 170 kDa and is composed of identical subunits with a molecular mass of 45 kDa, thus indicating a tetrameric structure similar to fumarases isolated from other organisms. The enzyme was active at temperatures ranging from 40 °C to 90 °C, with a maximum activity at 85 °C. The pH optimum for generation of fumarate was found to be pH 8·0. The enzyme showed high stability to denaturation by heat and organic solvents.

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/content/journal/micro/10.1099/00221287-136-8-1537
1990-08-01
2021-05-18
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