Title : ( Structural characterization of exopolysaccharide from Leuconostoc mesenteroides P35 and its binding interaction with bovine serum albumin using surface plasmon resonance biosensor )
Authors: Mojtaba Azari Anpar , Kambiz Jahanbin , Pascal Degraeve , Farideh Tabatabaei yazdi , Isabelle Adt , Nadia Oulahal , Didier Le Cerf ,Access to full-text not allowed by authors
Abstract
This paper describes the structural elucidation of Leuconostoc mesenteroides P35 exopolysaccharide (EPS-LM). Ln. mesenteroides P35 strain was isolated from a French goat cheese for its capacity to produce EPS increasing the viscosity of a whey-based fermentation medium. The chemical structure of EPS-LM analysis was elucidated by determination of optical rotation degree, macromolecular characterization, sugar units and methylation analyses, FT-IR, 1D NMR spectroscopy (1H and 13C NMR), 2D NMR spectroscopy (1Hsingle bond1H COSY, HSQC and HMBC). EPS-LM was a high molecular weight (ranging from 6.7 × 106 Da to 9.9 × 106 Da) dextran that is composed of only d-glucose units containing α (1 → 6) linkages and paltry α (1 → 3) branches. Since polysaccharide-protein interactions can be exploited to control and design food matrices, EPS-LM interactions with bovine serum albumin (the main constituent of bovine plasma) were investigated by surface plasmon resonance (SPR). Kinetic properties of EPS-LM binding with immobilized BSA via showed an increase of EPS-LM affinity (equilibrium constant (Kd)) for BSA from (2.50 ± 0.01) × 10−5 M−1 at 298 K to (9.21 ± 0.05) × 10−6 M−1 at to 310 K. The thermodynamic parameters revealed that van der Waals and hydrogen binding forces play a major role in the interaction of EPS-LM with BSA. However, EPS-LM-BSA interaction was non-spontaneous, entropy driven and an EPS-LM - BSA binding process was endothermic (ΔG > 0). The structural findings suggested that Ln. mesenteroides P35 α-D-glucan might find widespread technological applications in the biopolymer, medical and food industries.
Keywords
Ln. mesentroides dextran NMR Interaction Surface plasmon resonance Bovine serum albumin@article{paperid:1095036,
author = {Azari Anpar, Mojtaba and Kambiz Jahanbin and Pascal Degraeve and Tabatabaei Yazdi, Farideh and Isabelle Adt and Nadia Oulahal and Didier Le Cerf},
title = {Structural characterization of exopolysaccharide from Leuconostoc mesenteroides P35 and its binding interaction with bovine serum albumin using surface plasmon resonance biosensor},
journal = {International Journal of Biological Macromolecules},
year = {2023},
volume = {246},
number = {125599},
month = {August},
issn = {0141-8130},
pages = {125599--125612},
numpages = {13},
keywords = {Ln. mesentroides dextran
NMR
Interaction
Surface plasmon resonance
Bovine serum albumin},
}
%0 Journal Article
%T Structural characterization of exopolysaccharide from Leuconostoc mesenteroides P35 and its binding interaction with bovine serum albumin using surface plasmon resonance biosensor
%A Azari Anpar, Mojtaba
%A Kambiz Jahanbin
%A Pascal Degraeve
%A Tabatabaei Yazdi, Farideh
%A Isabelle Adt
%A Nadia Oulahal
%A Didier Le Cerf
%J International Journal of Biological Macromolecules
%@ 0141-8130
%D 2023