Protective activity of beta-1, 3-glucan binding protein against AAPH induced oxidative stress in Saccharomyces cerevisiae.

Abstract

The present work aimed to evaluate the antioxidant efficacy of beta-1,3-glucan binding/recognition protein against oxidative stress-induced Saccharomyces cerevisiae. Beta-1,3-glucan binding/recognition protein was attained from the Paratelphusa hydrodromus (Phβ-GBP) using laminarin coupled Sepharose CL-6B column. The structural characteristics of Phβ-GBP were analyzed through circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR) and proton nuclear magnetic resonance spectroscopy (1H NMR) analysis. CD spectrum showed the occurrence of α-helix (4.5%), β-sheets (23.6%), β-turn (17.2%) and random coils (54.8%). FTIR confirms the occurrence of amide and aromatic compounds whereas 1H NMR predicts the secondary structures and presence of amino acids in the Phβ-GBP. In vitro radical scavenging analysis disclose that Phβ-GBP has the potential to scavenge DPPH (73%), peroxyl radicals (81%) and hydrogen peroxide (56%) at 100\u202fμg/ml concentration. Reactive oxygen species production, lipid peroxidation, cell death, and DNA damage were decreased in the Phβ-GBP pretreated S. cerevisiae. In silico protein-protein interaction was performed between the β-GBP-glutathione reductase and β-GBP-catalase A. The interaction study reveals that glutathione reductase and catalase A interacts with β-GBP to reduce the oxidized glutathione and remove free radicals. This finding demonstrates that Phβ-GBP may act as a good antioxidant which protects from human pathologies linked with oxidative stress.