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Structural Characterization of Exopolysaccharide from Leuconostoc Mesenteroides P35 and Its Binding Interaction with Bovine Serum Albumin Using Surface Plasmon Resonance Biosensor

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES(2023)

Univ Lyon | Shahrood Univ Technol | Ferdowsi Univ Mashhad | Normandie Univ

Cited 3|Views16
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 (1H-1H COSY, HSQC and HMBC). EPS-LM was a high molecular weight (ranging from 6.7 x 106 Da to 9.9 x 106 Da) dextran that is composed of only D-glucose units containing & alpha; (1 & RARR; 6) linkages and paltry & alpha; (1 & RARR; 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 & PLUSMN; 0.01) x 10- 5 M-1 at 298 K to (9.21 & PLUSMN; 0.05) x 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 (& UDelta;G > 0). The structural findings suggested that Ln. mesenteroides P35 & alpha;-D-glucan might find widespread technological applications in the biopolymer, medical and food industries.
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Key words
Ln. mesentroides dextran,NMR,Interaction,Surface plasmon resonance,Bovine serum albumin
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