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Research Article Open access CC BY 3.0

Conformation and Structure of Bio Polymer Nano Particle Formed by β-Lactoglobulin-Pectin in the Presence of Sorbitol

Zahra Pishgahi, Hamid Ezzatpanah

Current Journal of Applied Science and Technology · pp. 1144–1161 · Published 25 Jul 2013

10.9734/BJAST/2013/2261

Abstract

Aims: This research investigates the influences of low methoxyl pectin (LMP) and sorbitol on the morphology and secondary structure of beta-lactoglobulin (BLG). Methodology: The effects of pH and temperature on the structure of the nano-complexes containing BLG, BLG-LMP and BLG-LMP in the presence of co-solvent (sorbitol) were studied by means of a far-UV Circular Dichroism spectroscopy (CD) and the size and morphology of nano-complexes measured by particle size analyzers, Scanning Electron Microscope (SEM) and Transmission Electron Microscopy (TEM). Results: CD results at different pH levels (4, 4.5, 5.3 and 6.3) indicated that the structural changes of BLG were more pronounced relative to BLG-LMP and BLG-LMP in presence of sorbitol. However, less destruction faced the protein structure at pH 5.3 compared to pH 4.5 and 4, therefore pH 5.3 was selected. BLG-LMP in presence of sorbitol had more protective effects on the secondary structure and indicated a high thermal stability when heated up to 75ºC for 10 minutes. Particle size measurement revealed that the size of BLG aggregate was as much as 250 nm while the BLG-LMP size in presence of sorbitol nano-complex was around 100 nm. SEM and TEM observations indicated uniform and spherical nano-complexes. Conclusion: The treated bio polymer particles have suitable properties and great potential as carriers for encapsulation and delivery of bio-active materials as well as a substitution for lipid droplets.

Beta lactoglobulin pectin sorbitol nano-complex SEM TEM

References (31)

  1. 1 Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function [DOI]
  2. 2 Polysaccharide protein interactions [DOI]
  3. 3 Protein–polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects [DOI]
  4. 4 Effect of extraction conditions on the yield, purity and surface properties of sugar beet pulp pectin extracts [DOI]
  5. 5 Complexation between milk proteins and polysaccharides via electrostatic interaction: principles and applications – a review [DOI]
  6. 6 Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein–polysaccharide complexes [DOI]
  7. 7 Effect of temperature on the secondary structure of β -lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis [DOI]
  8. 8 Protein-Polysaccharide Interactions for Stabilization of Food Emulsions [DOI]
  9. 9 Structural Changes Accompanying pH-Induced Dissociation of the β-Lactoglobulin Dimer , [DOI]
  10. 10 Effects of the proteinaceous moiety on the emulsifying properties of sugar beet pectin [DOI]
  11. 11 Versatile and Efficient Formation of Colloids of Biopolymer-Based Polyelectrolyte Complexes [DOI]
  12. 12 Interbiopolymer complexing between β-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration [DOI]
  13. 13 Role of Protein and Ferulic Acid in the Emulsification Properties of Sugar Beet Pectin [DOI]
  14. 14 Formation of biopolymer particles by thermal treatment of β-lactoglobulin–pectin complexes [DOI]
  15. 15 Thermal analysis of β-lactoglobulin complexes with pectins or carrageenan for production of stable biopolymer particles [DOI]
  16. 16 Influence of the overall charge and local charge density of pectin on the complex formation between pectin and β-lactoglobulin [DOI]
  17. 17 Thermodynamic Parameters of β-Lactoglobulin−Pectin Complexes Assessed by Isothermal Titration Calorimetry [DOI]
  18. 18 Thermodynamic Aspects of Biopolymer Functionality in Biological Systems, Foods, and Beverages [DOI]
  19. 19 pH-Induced Structural Transitions during Complexation and Coacervation of β-Lactoglobulin and Acacia Gum [DOI]
  20. 20 Effect of hydrocolloids on the thermal denaturation of proteins [DOI]
  21. 21 Food protein interactions in sugar solutions [DOI]
  22. 22 Sugar Beet Pectin–Protein Complexes [DOI]
  23. 23 Influence of Binding of Sodium Dodecyl Sulfate, All-trans-retinol, Palmitate, and 8-Anilino-1-naphthalenesulfonate on the Heat-Induced Unfolding and Aggregation of β-Lactoglobulin B [DOI]
  24. 24 Impact of cosolvents on formation and properties of biopolymer nanoparticles formed by heat treatment of β-lactoglobulin–Pectin complexes [DOI]
  25. 25 Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels [DOI]
  26. 26 Microstructures of β-lactoglobulin/amylopectin gels on different length scales and their significance for rheological properties [DOI]
  27. 27 Comparative analysis of refolding of chemically denatured β-lactoglobulin types A and B using the dilution additive mode [DOI]
  28. 28 trans-Parinaric acid as a versatile spectroscopic label to study ligand binding properties of bovine β-lactoglobulin [DOI]
  29. 29 Physicochemical basis for cosolvent modulation of β-lactoglobulin functionality: Interfacial tension study [DOI]
  30. 30 Thermodynamic parameters for beta-lactoglobulin dissociation over a broad temperature range at pH 2.6 and 7.0 [DOI]
  31. 31 Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies 1 1Edited by C. R. Matthews [DOI]

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