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

Mahtab Hasandokht Firooz; Mohammad Amin Mohammadifar; Parivash Haratian

doi:10.1016/j.ijbiomac.2012.02.020

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

Mahtab Hasandokht Firooz, Mohammad Amin Mohammadifar, Parivash Haratian

Shahid Beheshti University of Medical Sciences

Research output: Contribution to journal › Journal article › Research › peer-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 language	English
Journal	International Journal of Biological Macromolecules
Volume	50
Issue number	4
Pages (from-to)	925-931
Number of pages	7
ISSN	0141-8130
DOIs	https://doi.org/10.1016/j.ijbiomac.2012.02.020
Publication status	Published - 2012
Externally published	Yes

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

Access to Document

10.1016/j.ijbiomac.2012.02.020

OpenUrl availability

Full text

Cite this

@article{6d736770c8a24588a2423f8310d267e2,

title = "Self-assembly of beta-lactoglobulin and the soluble fraction of gum tragacanth in aqueous medium",

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.",

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",

author = "Firooz, {Mahtab Hasandokht} and Mohammadifar, {Mohammad Amin} and Parivash Haratian",

year = "2012",

doi = "10.1016/j.ijbiomac.2012.02.020",

language = "English",

volume = "50",

pages = "925--931",

journal = "International Journal of Biological Macromolecules",

issn = "0141-8130",

publisher = "Elsevier",

number = "4",

}

TY - JOUR

T1 - Self-assembly of beta-lactoglobulin and the soluble fraction of gum tragacanth in aqueous medium

AU - Firooz, Mahtab Hasandokht

AU - Mohammadifar, Mohammad Amin

AU - Haratian, Parivash

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - Biochemistry

KW - Molecular Biology

KW - Structural Biology

KW - β-Lactoglobulin

KW - Complex coacervation

KW - Gum tragacanth

KW - Rheology

KW - Self-assembly

KW - beta lactoglobulin

KW - gum tragacanth

KW - acidification

KW - analytical parameters

KW - aqueous solution

KW - article

KW - carbohydrate analysis

KW - coacervation

KW - concentration (parameters)

KW - flow measurement

KW - microscopy

KW - pH

KW - protein assembly

KW - protein carbohydrate interaction

KW - protein structure

KW - separation technique

KW - Animals

KW - Cattle

KW - Hydrogen-Ion Concentration

KW - Lactoglobulins

KW - Particle Size

KW - Protein Binding

KW - Solubility

KW - Tragacanth

KW - Water

KW - BIOCHEMISTRY

KW - COMPLEX COACERVATION

KW - ACACIA GUM

KW - ASTRAGALUS-GOSSYPINUS

KW - LIGHT-SCATTERING

KW - PHASE-SEPARATION

KW - WHEY PROTEINS

KW - TITRATION

KW - VISCOSITY

KW - WEIGHT

KW - PART

KW - beta-Lactoglobulin

KW - MOLECULAR self-assembly

KW - coacervation process

KW - in situ acidification reaction

KW - morphological change

KW - pH-induced structural transition

KW - phase separation process

KW - aqueous medium

KW - beta-lactoglobulin BLG

KW - gum tragacanth 9000-65-1

KW - tragacanthin

KW - 10060, Biochemistry studies - General

KW - 10064, Biochemistry studies - Proteins, peptides and amino acids

KW - 10068, Biochemistry studies - Carbohydrates

KW - light scattering spectroscopy laboratory techniques, spectrum analysis techniques

KW - multi-methodological approach laboratory techniques

KW - optical microscopy laboratory techniques, imaging and microscopy techniques

KW - rheometry mathematical and computer techniques

KW - spectrophotometry laboratory techniques, spectrum analysis techniques

KW - Biochemistry and Molecular Biophysics

KW - Methods and Techniques

KW - ACIDIFICATION

KW - BINDING

KW - GUM TRAGACANTH

KW - GUMS

KW - LACTOGLOBULINS

KW - PH

KW - STRUCTURE

KW - β-LACTOGLOBULIN

KW - Chemistry and biochemistry

KW - Food sciences

U2 - 10.1016/j.ijbiomac.2012.02.020

DO - 10.1016/j.ijbiomac.2012.02.020

M3 - Journal article

C2 - 22390848

SN - 0141-8130

VL - 50

SP - 925

EP - 931

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - 4

ER -

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

Abstract

Keywords

Access to Document

OpenUrl availability

Fingerprint

Cite this