Production of .beta.-apiosidase by Aspergillus niger: partial purification, properties, and effect on terpenyl apiosylglucosides from grape

Abstract

Various aspects of fungus-originated 0-apiosidase were studied. The production of the enzyme on various carbon sources by fungi appeared to be inducible as it was only produced when apiin, an apiosylglucoside, was present in the culture medium. The influence of apiin concentration, nitrogen source, and surfactants on enzyme production was studied. The enzyme was partially purified by filtration chromatography on Ultrogel AcA44 and ion-exchange chromatography on DEAE-Sepharose CLGB. The molecular weight of this enzyme was 38 OOO; K , and V,, values for p-nitrophenyl O-Dapiofuranoside were, respectively, 16 mM and 0.192 nkat/mg of protein. With regard to activity, the optimum p H and temperature were, respectively, 5.6 and 50 "C. The optimum p H of stability was 7. Na+, Mgz+, MnZ+, Cu+, Cu2+ have an inhibitor effect on 0-apiosidase activity. Conversely, the enzyme was inhibited neither by glucose nor by ethanol. The effect of 0-apiosidase toward apiosylglucosides of terpenols, grape flavor precursors, was tested.

Flavour enhancement through the enzymatic hydrolysis of glycosidic aroma precursors in juices and wine beverages: a review

“…26 Furthermore, glycosidases from fungi are more heatresistant than those from plants and yeasts. While fungal β-glucosidase activity is inhibited by glucose, its exoglycosidase activities [38][39][40] are not significantly inhibited at the concentrations at which this sugar occurs in fruit juices. For this reason, enzymes from fungi could be useful in the final stages of winemaking, whilst some yeast strains would enhance aroma if directly added during fermentation.…”

“…Among the latter, β-glucosidase and α-arabinofuranosidase are usually the most abundant, while α-rhamnosidase and β-apiosidase activities are very low or absent. 39 Among commercial crude enzymes preparations tested, Kelzyme 200 was found to be the richest in β-apiosidase. Commercial enzyme preparations differ largely in glycosidase activities, since they are formulated as a function of their pectinase or cellulase activities.…”

Application of Non-Saccharomyces Yeasts to Wine-Making Process

“…This β-glucosidase is associated with the yeast cell wall is quite glucose independent but is inhibited by ethanol. These results could open new pathways regarding other glycosidase activities in S. cerevisiae; α-rhamnosidase, α-arabinosidase or β-apiosidase activities could be induced in wine yeast by changing the composition of the medium including inductive compounds, as well as in filamentous fungi [74].…”

Free and Bound Volatile Secondary Metabolites of Vitis Vhifera Grape cv. Sauvignon Blanc

“…2). This would be the case if the fungal enzyme systems used were deficient in apiosidase activity (Dupin et al, 1992).…”