Self-assembly of beta-lactoglobulin and the soluble fraction of gum tragacanth in aqueous medium

Mahtab Hasandokht Firooz, Mohammad Amin Mohammadifar, Parivash Haratian

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Spectrophotometric and light scattering measurements, along with optical microscopy, were used to follow the complexation and coacervation process that occur when beta-lactoglobulin (BLG)/tragacanthin (T) mixed dispersions (0.3 wt.% total concentration: BLG:T ratio of 2:1) were brought from pH 6 to pH 2. In addition, the coupling of slow in situ acidification of the mixture and rheometry was utilised to gain deeper insights into pH-induced structural transitions during the assembly process. The results obtained by this multi-methodological approach allowed the associative phase separation process to be parameterised in terms of a set of characteristic pH values (similar to 5.3, similar to 4.8, similar to 4.5, similar to 4.15, similar to 4, similar to 3.8, similar to 2.5) at which critical structural changes took place. Investigation of the absorbance profiles of complexed/coacervated systems as a function of time revealed that several transitions could occur at different time scales. Morphological changes in the assemblies and the subsequent formation of some flocculant substances during the late stage of process were clearly visualised using microscopy. (C) 2012 Elsevier B.V. All rights reserved.
Original languageEnglish
JournalInternational Journal of Biological Macromolecules
Volume50
Issue number4
Pages (from-to)925-931
Number of pages7
ISSN0141-8130
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • β-Lactoglobulin
  • Complex coacervation
  • Gum tragacanth
  • Rheology
  • Self-assembly
  • beta lactoglobulin
  • gum tragacanth
  • acidification
  • analytical parameters
  • aqueous solution
  • article
  • carbohydrate analysis
  • coacervation
  • concentration (parameters)
  • flow measurement
  • microscopy
  • pH
  • protein assembly
  • protein carbohydrate interaction
  • protein structure
  • separation technique
  • Animals
  • Cattle
  • Hydrogen-Ion Concentration
  • Lactoglobulins
  • Particle Size
  • Protein Binding
  • Solubility
  • Tragacanth
  • Water
  • BIOCHEMISTRY
  • COMPLEX COACERVATION
  • ACACIA GUM
  • ASTRAGALUS-GOSSYPINUS
  • LIGHT-SCATTERING
  • PHASE-SEPARATION
  • WHEY PROTEINS
  • TITRATION
  • VISCOSITY
  • WEIGHT
  • PART
  • beta-Lactoglobulin
  • MOLECULAR self-assembly
  • coacervation process
  • in situ acidification reaction
  • morphological change
  • pH-induced structural transition
  • phase separation process
  • aqueous medium
  • beta-lactoglobulin BLG
  • gum tragacanth 9000-65-1
  • tragacanthin
  • 10060, Biochemistry studies - General
  • 10064, Biochemistry studies - Proteins, peptides and amino acids
  • 10068, Biochemistry studies - Carbohydrates
  • light scattering spectroscopy laboratory techniques, spectrum analysis techniques
  • multi-methodological approach laboratory techniques
  • optical microscopy laboratory techniques, imaging and microscopy techniques
  • rheometry mathematical and computer techniques
  • spectrophotometry laboratory techniques, spectrum analysis techniques
  • Biochemistry and Molecular Biophysics
  • Methods and Techniques
  • ACIDIFICATION
  • BINDING
  • GUM TRAGACANTH
  • GUMS
  • LACTOGLOBULINS
  • PH
  • STRUCTURE
  • β-LACTOGLOBULIN
  • Chemistry and biochemistry
  • Food sciences

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