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β-Glycosidase Activity toward Different Glycosidic Forms of Isoflavones

2005; American Chemical Society; Volume: 53; Issue: 12 Linguagem: Inglês

10.1021/jf0404694

1520-5118

Baraem Ismail, K.D. Hayes,

Natural Antidiabetic Agents Studies

Isoflavones, a group of soybean components that significantly contribute to human health and disease prevention, exist in various chemical forms. The enzyme activity can be very sensitive to molecular structure; thus, the profile of the isoflavones can affect their rate of hydrolysis. The objective of this work was to study the β-glycosidase activities toward isoflavone β-glycosides and their conjugated forms. Hydrolysis experiments were conducted where β-glycosides and their conjugates were treated with β-glycosidase. Results confirmed that β-glycosidase can hydrolyze nonconjugated β-glycosides into aglycones. However, when the enzyme amount and/or activity were limited, significant differences in enzyme activity toward the β-glycosides were observed. On the other hand, β-glycosidase was not effective in hydrolyzing the conjugated glycosides to their respective aglycones, even with increased levels of the enzyme and with prolonged incubation. The transformation of conjugated glycosides into their respective β-glycosides will most likely result in increased hydrolysis rates and better absorption. Keywords: Isoflavones; β-glycosides; aglycones; malonylglycosides; acetylglycosides; β-glycosidase activity; hydrolysis