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

Aida Shala; Toskë Kryeziu; Mimoza Basholli Salihu

Makale detayları

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

Yazarlar:

Aida Shala | Toskë Kryeziu | Mimoza Basholli Salihu

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.29 Issue 2, pp.486-496

Belge Tipi:

Makale

Yayın Tarihi:

8/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001341699

pISSN:

2630-6344

Anahtar kelimeler:

Özet:

 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. infantiss 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 delphinidins 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.

 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. infantiss 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 delphinidins 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.

 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. infantiss 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 delphinidins 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.

 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. infantiss 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 delphinidins 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.

Makale detayları

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

Yazarlar:

Aida Shala | Toskë Kryeziu | Mimoza Basholli Salihu

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.29 Issue 2, pp.486-496

Belge Tipi:

Makale

Yayın Tarihi:

8/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001341699

pISSN:

2630-6344

Anthocyanins

Bioavailability

Deglycosilation

Bifidobacterium infantis

β-Glucosidase

β-Galactosidase

Enzymatic hydrolysis

Cell-free Enzyme Stability

Sayı

Makale detayları

Yazarlar: Aida Shala | Toskë Kryeziu | Mimoza Basholli Salihu

Yayıncı: Marmara University

Ana Başlıklar: Pharmaceutical Sciences

Dergi: Journal of Research in Pharmacy Vol.29 Issue 2, pp.486-496

Belge Tipi: Makale

Yayın Tarihi: 8/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001341699

pISSN: 2630-6344

Sayı

Yazarlar:

Aida Shala | Toskë Kryeziu | Mimoza Basholli Salihu

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Sciences

Dergi:

Journal of Research in Pharmacy Vol.29 Issue 2, pp.486-496

Belge Tipi:

Makale

Yayın Tarihi:

8/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001341699

pISSN:

2630-6344