Biochemical differences between products of the ADH locus in olive fruit fly (Bactrocera oleae).

Purified alcohol dehydrogenases from olive fruit flies of genotypes SS, II, and SI were biochemically compared. The enzymes were found to differ in the specific activity, in the influence of pH and temperature on activity, and in the affinity with different substrate-alcohols. The probable relationships of these findings with the dramatic changes in allele frequencies observed when natural populations are introduced in the laboratory are discussed.

Purification of alcohol dehydrogenase from four genotypes of the olive fruit fly Bactrocera (Dacus) oleae.

This is the first report describing the purification of alcohol dehydrogenase (ADH) from four genotypes of the olive fruit fly Bactrocera oleae, the most important pest of olives in the Mediterranean region. The purified enzyme shows a single band after SDS-PAGE analysis, corresponding to subunit mass of 26 kDa. The native ADH shows a molecular mass of 48 kDa, after gel filtration HPLC analysis. The purification method incorporated a preliminary ammonium sulphate precipitation step, followed by an anion-exchange DEAE chromatography step, a dye affinity chromatography step on Cibacron blue 3GA, and an anion-exchange DEAE chromatography step employing the same column of the first step. The present method offers good overall recovery (40%) and high enzyme purity, and it is applicable to different genotypes. Furthermore, the method is rapid and economical, as it employs two cheap, widely used, and commercially available chromatography materials.