CERTAIN PROPERTIES OF Β-GLUCOSIDASE FROM YUCCA GLORIOSA FLOWERS

The search for rational synthetic pathways for steroid drugs from accessible plant sources represents an important and relevant objective. Yucca gloriosa presents significant interest as a source of tigogenin-a valuable sapogenin for steroid hormonal drug production. Along with traditionally utilized leaves, the flowers of this plant contain 1.25-1.48% tigogenin and possess several technological advantages: simpler extraction of the target product due to lower lipophilic substance content and softer raw material texture. Endogenous β-glucosidase plays a key role in the tigogenin production process, catalyzing the conversion of oligofurostanoside to oligospirostanoside. This work investigated the properties of β-glucosidase from flowers of Yucca gloriosa cultivated in Georgia. Two enzyme forms differing in substrate specificity were identified. The first form (30% ammonium sulfate saturation fraction) hydrolyzes both natural oligofurostanoside and synthetic substrate 4-nitrophenyl-β-D-glucopyranoside, whereas the second form (80% saturation fraction) cleaves only the synthetic substrate. For the first β-glucosidase form, which has practical significance for tigogenin production, optimal operating conditions were determined: pH6.3 and temperature 47°C. Notably, the temperature optimum for the flower enzyme (47°C) proved higher than for the leaf enzyme (37°C). Heating at 57°C for 10 minutes reduces enzyme activity by 29%, while at 67°C it reduces activity by 79%.