Complex coacervation of an arabinogalactan-protein extracted from the Meryta sinclarii tree (puka gum) and whey protein isolate

Wee, May Sui Mei; Salleh, Nurhazwani; Tan, Kevin Wei Jie; Goh, Kelvin K.T.; Sims, Ian M.; Matía-Merino, Lara

doi:10.1016/j.foodhyd.2014.03.005

Cited by 47 publications

(18 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similar effects of NaCl (0–100 mM) on dynamic shear behavior were observed on coacervates formed between sodium caseinate and pectin (Weinbreck, Wientjes, et al, 2004). Structural breakdown or rearrangement of the WPI‐FG coacervates under applied shearing force might contribute to shear‐thinning behavior (Wee et al, 2014). Flaxseed gum polysaccharide chains formed the highest strength of electrostatic attractive forces with WPI molecules at pH 3.4 with no charge screening effects caused by dissolved salt ions.…”

Section: Resultsmentioning

confidence: 99%

Ionic strength and hydrogen bonding effects on whey protein isolate–flaxseed gum coacervate rheology

Shim

Reaney

2020

Food Science & Nutrition

View full text Add to dashboard Cite

Whey protein isolate (WPI) was mixed with anionic flaxseed (Linum usitatissimum L.) gum (FG), and phase transition during coacervate formation was monitored. Effects of ionic strength and hydrogen bonding on coacervation of WPI‐FG system and corresponding rheological properties were investigated. During coacervate formation, structural transitions were confirmed by both turbidimetry and confocal laser scanning microscopy. Increasing ionic strength with sodium chloride (50 mM) decreased optical density (600 nm) at pHmax. Correspondingly, pHc and pHϕ1 decreased from pH 5.4 to 4.8 and from 5.0 to 4.6, respectively, while pHϕ2 increased from pH 1.8 to 2.4. Sodium chloride suppressed biopolymer electrostatic interactions and reduced coacervate formation. Adding urea (100 mM) shifted pHϕ1, pHmax, and pHϕ2 from 4.8, 3.8, and 1.8 to 5.0, 4.0, and 2.2, respectively, while pHc was unaffected. Optical density (600 nm) at pHmax (0.536) was lower than that of control in the absence of urea (0.617). This confirmed the role of hydrogen bonding during coacervate formation in the biopolymer system composed of WPI and FG. Dynamic shear behavior and viscoelasticity of collected coacervates were measured, and both shear‐thinning behavior and gel‐like properties were observed. Addition of sodium chloride and urea reduced ionic strength and hydrogen bonding, resulting in decreased WPI‐FG coacervate dynamic viscosity and viscoelasticity. The disturbed charge balance contributed to a loosely packed structure of coacervates which were less affected by altered hydrogen bonding. Findings obtained here will help to predict flaxseed gum behavior in protein‐based foods.

show abstract

Section: Resultsmentioning

confidence: 99%

Ionic strength and hydrogen bonding effects on whey protein isolate–flaxseed gum coacervate rheology

Shim

Reaney

2020

Food Science & Nutrition

View full text Add to dashboard Cite

show abstract

“…Associative phase separation follows two structure‐forming events involving spinodal decomposition or nucleation and growth‐type kinetics . First, the formation of soluble complexes giving the first initial rise in scattering intensity during a pH acid titration (denoted by pH c ); and secondly, the formation of insoluble complexes where macroscopic phase separation occurs and a rapid rise in scattering intensity occurs (denoted by pH ϕ1 ) . These pH values are determined by extending tangent lines from either side of the rise in a plot of scattering intensity (or optical density) versus pH.…”

Section: Factors Affecting Complex Formationmentioning

confidence: 99%

“…Under low ionic strength conditions, slight conformational changes in biopolymers leads to enhanced solubility, which gives greater access to the charged sites on it and supports complexation . Further, salting‐in allows for more sites to be available for electrostatic interactions to occur, and helps eliminate short‐range repulsions between biopolymers . Higher turbidity and shifts in pH c and pH ϕ1 to higher pH values are evidence for the salting‐in effect …”

Section: Factors Affecting Complex Formationmentioning

confidence: 99%

“…56 First, the formation of soluble complexes giving the first initial rise in scattering intensity during a pH acid titration (denoted by pH c ); and secondly, the formation of insoluble complexes where macroscopic phase separation occurs and a rapid rise in scattering intensity occurs (denoted by pH 1 ). 2,24,58,59 These pH values are determined by extending tangent lines from either side of the rise in a plot of scattering intensity (or optical density) versus pH. The terms 'soluble' and 'insoluble' are used to describe the coacervation in the literature relating to biopolymer interactions, and do not reflect 'solubility' in terms of functionality testing.…”

Section: Intrinsic Factors Phmentioning

confidence: 99%

“…64,66 Further, salting-in allows for more sites to be available for electrostatic interactions to occur, and helps eliminate short-range repulsions between biopolymers. 59 Higher turbidity and shifts in pH c and pH 1 to higher pH values are evidence for the salting-in effect. 58…”

Section: Ionic Strengthmentioning

confidence: 99%

See 2 more Smart Citations

Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

2018

View full text Add to dashboard Cite

Controlling the interactions between plant proteins and polysaccharides can lead to the development of novel electrostatic complexed structures that can give unique functionality. This in turn can broaden the diversity of applications that they may be suitable for. Overwhelmingly in the literature, work and reviews relating to coacervation have involved the use of animal proteins. However, with the increasing demand for plant-based protein alternatives by industry and consumers, a greater understanding of how they interact with polysaccharides is essential to control structure, functionality and applicability. This review discusses the factors governing the nature of protein-polysaccharide interactions, their functional attributes and industrial applications, with special attention given to plant proteins. © 2018 Society of Chemical Industry.

show abstract

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

Zheng,

Van der Meeren,

Sun

2023

Aggregate

View full text Add to dashboard Cite

For more than a decade, the discovery of liquid–liquid phase separation within living organisms has prompted colloid scientists to understand the connection between coacervate functionality, phase behavior, and dynamics at a multidisciplinary level. Although the protein–polysaccharide was the first system in which the coacervation phenomenon was discovered and is widely used in food systems, the phase state and relaxation dynamics of protein–polysaccharide complex coacervates (PPCC) have rarely been discussed previously. Consequently, this review aims to unravel the relationship between PPCC dynamics, thermodynamics, molecular architecture, applications, and phase states in past studies. Looking ahead, solving the way molecular architecture spreads to macro‐functionality, that is, establishing the relationship between molecular architecture–dynamics–application, will catalyze novel advancements in PPCC research within the field of foods and biomaterials.

show abstract

Complex coacervation of an arabinogalactan-protein extracted from the Meryta sinclarii tree (puka gum) and whey protein isolate

Cited by 47 publications

References 28 publications

Ionic strength and hydrogen bonding effects on whey protein isolate–flaxseed gum coacervate rheology

Ionic strength and hydrogen bonding effects on whey protein isolate–flaxseed gum coacervate rheology

Review on plant protein–polysaccharide complex coacervation, and the functionality and applicability of formed complexes

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

Contact Info

Product

Resources

About