Enzymatic hydrolysis of anthocyanin glycosides by Bifidobacterium infantis cell-free enzymes: Stability assessment and bioavailability implications

The bioavailability of anthocyanins is crucial for conveying their health benefits, but they are poorly absorbed in the gastrointestinal tract (GIT). The deglycosylation of anthocyanins is the key step in improving their bioavailability and bioactivity. This study investigated the potential of β-glucosidase and β-galactosidase cell-free enzymes from Bifidobacterium infantis, on glycolytic hydrolysis of essential anthocyanins, including Cyanidin-3-O-β-D-glucoside (C3-Glu), Malvidin-3- O-β-D-glucoside (M3-Glu), Cyanidin-3-O-β-D-galactoside (C3-Gal) and Delphinidin-3-O-β-D-glucoside (D3-Glu). According to our previous work, Bifidobacterium infantis (B. infantis) was chosen for this study due to its high β- glucosidase and β-galactosidase activity. The anthocyanin glycosides' stability was also evaluated to distinguish chemical instability from enzymatic degradation. B. infantis β-glucosidase exerted the highest activity toward C3-Glu, forming high levels of protocatechuic acid as an active compound, with lower hydrolytic rates observed for M3-Glu. Additionally, B. infantis's β-galactosidase activity was efficient against C3-Gal. According to this study, B. infantis prefers cyanidin glucoside and cyanidin galactoside as substrates. Under experimental circumstances, delphinidin exhibited lower chemical stability, but malvidin and cyanidin glycosides exhibited similar stability. In conclusion, chemical instability is the cause of delphinidin's rate of degradation. According to these results, B. infantis may be utilized as a probiotic supplement to improve the health advantages and bioavailability of meals high in anthocyanins, supporting the development of functional foods and medicinal formulations.