However the quercetin standard showed a higher percentage of oxidation inhibition, possibly due to its more hydrophobic nature. The XO inhibitory capacity of hydrolyzed rutin (after 4, 8 and 12 h of hydrolysis with hesperidinase) was not statistically different from rutin, which could be considered a weak inhibitor of XO. Quercetin, on the other hand, exhibited the strongest inhibitory activity, as shown in Table 1. The antiproliferative properties of the samples before and after bioconversion were assessed using nine human cancer cell lines, and the chemotherapeutic drug, doxorubicin, as a positive control (Fig. 4 and Table 2). A horizontal line at 0% was traced to visualize
Total Growth Inhibition (TGI) that represents the concentration required to completely inhibit cell growth (total Enzalutamide molecular weight cytostatic effect) (Table 2). For all cell lines tested, rutin hydrolyzed by hesperidinase displayed a moderate Selleckchem ATM inhibitor antiproliferative activity with selectivity for OVCAR-3 (ovarian, TGI = 1.5 μg/mL), MCF-7 (breast, TGI = 2.3 μg/mL) and U251 (glioma, TGI = 3.6 μg/mL) while quercetin presented a weak activity with selectivity for U251 (glioma, TGI = 31.4 μg/mL), MCF-7 (breast, TGI = 31.9 μg/mL), 786–0 (renal, TGI = 42.7 μg/mL) and NCI-ADR/RES (ovarian expressing
multidrug resistance, TGI = 44.0 μg/mL). Rutin did not inhibit cell proliferation of any of the cancer cell lines tested. Flavonoid glycosides production of by removing rhamnose from rutinosides can be performed through controlled enzymatic catalysis. In the present study, we were able to define a good condition of β-d-glucosidase inactivation for hesperidinase and naringinase, while keeping a high level of α-l-rhamnosidase activity. After 4 h of enzymatic reaction catalyzed by hesperidinase, previously heated at 70 °C for 30 min, significant amounts of quercetin-3-glucoside (approximately
70%) were obtained. Hesperidinase hydrolyzed rutin more efficiently than naringinase. Hydrolyzed rutin produced by bioconversion using hesperidinase was subsequently selected for further Erythromycin investigation. Vila-Real, Alfaia, Bronze, Calado, and Ribeiro (2011) performed a similar procedure to produce flavonoid monoglycosides, including quercetin-3-glucoside, from rutinosides, using naringinase from Penicillium decumbens as biocatalyst. The authors reported that a selective inactivation of β-d-glucosidase activity of naringinase was achieved at 81.5 °C and pH 3.9, keeping a very high residual activity of α-l-rhamnosidase (78%). Similarly, You et al. (2010) reported that β-d-glucosidase activity of crude enzyme extract of Aspergillus niger was completely inactivated by treatment for 30 min at 70 °C while the α-l-rhamnosidase activity was decreased by only 50%. The difference in the Rha/Glu activity ratio between hesperidinase and naringinase (Fig.