Pure-grade oleuropein, a bitter, hypotensive, phenolic glucoside, was obtained from organic extracts of olive plant leaves by two chromatographic steps. The purified compound was characterized by spectroscopic NMR and FAB-MS methods. The glucoside underwent chemical and enzymatic hydrolysis. Aglycone was characterized by spectroscopic methods (H-1-NMR and FAB-MS). Glucose was measured by enzymatic methods. The enzymatic hydrolysis of oleuropein was carried out by a soluble beta-glucosidase. The reaction was characterized in terms of kinetic parameters, optimal pH value, activation energy, inhibition constant by glucose, and thermal stability. Preliminary experiments were also performed in a continuous-flow ultrafiltration membrane reactor. The cut-off of the membrane was lower than the molecular-weight of the enzyme, thus determining beta-glucosidase confinement within the reactor. Under these conditions, beta-glucosidase had a good long-term stability. This is an encouraging results in view of possible industrial applications.

Production of glucose and bioactive aglycone by chemical and enzymatic hydrolysis of purified oleuropein from Olea europea / Capasso, R.; Evidente, A.; Visca, C.; Gianfreda, L.; Maremonti, M.; Greco, G.. - In: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY. - ISSN 0273-2289. - 61:(1996), pp. 365-377.

Production of glucose and bioactive aglycone by chemical and enzymatic hydrolysis of purified oleuropein from Olea europea

A. Evidente;
1996

Abstract

Pure-grade oleuropein, a bitter, hypotensive, phenolic glucoside, was obtained from organic extracts of olive plant leaves by two chromatographic steps. The purified compound was characterized by spectroscopic NMR and FAB-MS methods. The glucoside underwent chemical and enzymatic hydrolysis. Aglycone was characterized by spectroscopic methods (H-1-NMR and FAB-MS). Glucose was measured by enzymatic methods. The enzymatic hydrolysis of oleuropein was carried out by a soluble beta-glucosidase. The reaction was characterized in terms of kinetic parameters, optimal pH value, activation energy, inhibition constant by glucose, and thermal stability. Preliminary experiments were also performed in a continuous-flow ultrafiltration membrane reactor. The cut-off of the membrane was lower than the molecular-weight of the enzyme, thus determining beta-glucosidase confinement within the reactor. Under these conditions, beta-glucosidase had a good long-term stability. This is an encouraging results in view of possible industrial applications.
1996
Production of glucose and bioactive aglycone by chemical and enzymatic hydrolysis of purified oleuropein from Olea europea / Capasso, R.; Evidente, A.; Visca, C.; Gianfreda, L.; Maremonti, M.; Greco, G.. - In: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY. - ISSN 0273-2289. - 61:(1996), pp. 365-377.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/469375
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