Isolation and Characterization of an Insulin‐Like Protein From Moringa Oleifera and Estimation of Its Antidiabetic Potential DOI Open Access
Sumera Zaib, Imtiaz Khan,

Laiba Babar

et al.

ChemistrySelect, Journal Year: 2025, Volume and Issue: 10(6)

Published: Feb. 1, 2025

Abstract Moringa oleifera is used all over the world as an herbal cure for a myriad of diseases. The current research focuses on extraction proteins from leaves, estimating their total protein content, detecting insulin‐like protein, and evaluating its hypoglycemic effect. With help Tris‐HCl buffer solution, leaf extract obtained through solvent extraction, which subjected afterward to filtration, centrifugation, dialysis provide purified supernatant pellet. A content 8.0 ± 0.25 g/dL in both fractions revealed by serum albumin assay. visible precipitation with ZnCl 2 confirms presence protein. Alpha‐amylase alpha‐glucosidase enzyme assays are performed test properties. Notably, displays strong inhibition against α ‐amylase, having percentage values 75.48 82.93% relevant IC 50 0.6 17.6 µM pellet, respectively. However, ‐glucosidase modest, 11.1 14.1% These findings suggest that within can contribute This study paves way further exploration this protein's potential, possibly leading novel drug development managing diabetes mellitus.

Language: Английский

Isolation and Characterization of an Insulin‐Like Protein From Moringa Oleifera and Estimation of Its Antidiabetic Potential DOI Open Access
Sumera Zaib, Imtiaz Khan,

Laiba Babar

et al.

ChemistrySelect, Journal Year: 2025, Volume and Issue: 10(6)

Published: Feb. 1, 2025

Abstract Moringa oleifera is used all over the world as an herbal cure for a myriad of diseases. The current research focuses on extraction proteins from leaves, estimating their total protein content, detecting insulin‐like protein, and evaluating its hypoglycemic effect. With help Tris‐HCl buffer solution, leaf extract obtained through solvent extraction, which subjected afterward to filtration, centrifugation, dialysis provide purified supernatant pellet. A content 8.0 ± 0.25 g/dL in both fractions revealed by serum albumin assay. visible precipitation with ZnCl 2 confirms presence protein. Alpha‐amylase alpha‐glucosidase enzyme assays are performed test properties. Notably, displays strong inhibition against α ‐amylase, having percentage values 75.48 82.93% relevant IC 50 0.6 17.6 µM pellet, respectively. However, ‐glucosidase modest, 11.1 14.1% These findings suggest that within can contribute This study paves way further exploration this protein's potential, possibly leading novel drug development managing diabetes mellitus.

Language: Английский

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