Intermolecular interaction and complex coacervation between bovine serum albumin and gum from whole flaxseed (Linum usitatissimum L.)

Li, Jun; Shim, Youn Young; Wang, Yong; Reaney, Martin J.T.

doi:10.1016/j.foodhyd.2015.02.035

Cited by 88 publications

(53 citation statements)

References 48 publications

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“…In previous studies, changes in the turbidity of whey protein isolate and flaxseed gum mixtures were reported to be caused by acid titration (Weinbreck et al., 2003). Another study of flaxseed gum and BSA showed similar results (Liu et al., ). As a result, we evaluated the relationship between pH and R .…”

Section: Resultssupporting

confidence: 62%

“…Weinbreck et al, 2003). Another study of flaxseed gum and BSA showed similar results (Liu et al, 2015). As a result, we evaluated the relationship between pH and R. Transmission of KC-HP mixtures varied from R = 8:1 to 1:8 as a function of pH, as shown in Figure 4.…”

Section: Food Engineering Materialsmentioning

confidence: 62%

“…The storage modulus ( G ′) was higher than the loss modulus ( G ″) for all samples with different pH values; both the G ′ and G ″ increased with frequency and did not intersect, suggesting that a highly interconnected gel‐like network structure was formed (Nishinari, ). In previous studies, a gel‐like network structure was found between bovine serum albumin (BSA) and KC (Chai and ), between BSA and gum from whole flaxseed (Liu, Shim, Wang, & Reaney, ), and in an ovalbumin‐chitosan coacervate (Xiong et al., ). These data indicated that the KC‐HP coacervate behaved more like a viscoelastic solid (Kim & Yoo, ).…”

Section: Resultsmentioning

confidence: 98%

See 2 more Smart Citations

Effects of Mixing Ratio and pH on the Electrostatic Interactions of Hydrolyzed Alaska Pollock Protein and κ‐Carrageenan

Cui

Xue

et al. 2018

Journal of Food Science

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Section: Resultssupporting

confidence: 62%

Section: Food Engineering Materialsmentioning

confidence: 62%

Section: Resultsmentioning

confidence: 98%

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Effects of Mixing Ratio and pH on the Electrostatic Interactions of Hydrolyzed Alaska Pollock Protein and κ‐Carrageenan

Cui

Xue

et al. 2018

Journal of Food Science

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“…Electrostatic interactions were first identified as a primary force guiding the formation of coacervates of gelatin and acacia gum (Tiebackx, 1911). Since this pioneering work coacervate formation has been studied for many protein and polysaccharide systems, including FG and BSA (Liu, Shim, Wang, & Reaney, 2015). Soluble and insoluble FG‐BSA coacervate formations are determined by solution pH and ionic strength as these factors can affect the ionization of amino and carboxylic groups on biopolymer structures and interactions between charge groups in solution.…”

Section: Resultsmentioning

confidence: 99%

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

Shim

Reaney

2020

Food Science & Nutrition

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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.

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“…Both EAI and ES were significantly decreased after protease treatment due to depletion of FG proteins. FG readily forms coacervates with BSA for example (Liu, Shim, Wang, & Reaney, 2015). FG is a naturally occurring coacervate between negatively charged polysaccharide chains and positively charged albumins.…”

Section: Resultsmentioning

confidence: 99%

Conlinin in flaxseed (Linum usitatissimum L.) gum and its contribution to emulsification properties

et al. 2016

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a b s t r a c tFlaxseed gum (FG) is a mixture of natural polysaccharide and protein derived from flaxseed (Linum usitatissimum L.) that has potential for thickening foods, stabilizing emulsions, and gelling solutions. The composition and identities of proteins in FG have never been reported. In this study, gum prepared from whole flaxseed was deglycosylated by treating it with trifluoromethanesulfonic acid (TFMS). The resultant proteins were separated by 2D-gel electrophoresis. The major protein spots with estimated molecular weights (MW) of 10e11 kDa and 11e12 kDa were excised, digested with trypsin, and analyzed using matrix-assisted laser ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Peptide MS of tryptic digestion fragments was compared to MS of peptides from gene models available through National Center for Biotechnology Information (NCBI) database. Fragments consistent with the seed storage protein conlinin, the low-molecular-mass 2S storage flaxseed protein, were identified as the major spot constituents. Emulsification properties of FG were determined before and after protease hydrolysis with emulsion activity index (EAI) and emulsion stability (ES) as indicators. Both EAI and ES decreased from 98.7 ± 5.4 to 59.9 ± 3.2 m 2 /g and from 66.4 ± 1.1 to 42.1 ± 2.0%, respectively, after protease treatment. Conlinin is the major protein associated with FG and it plays a fundamental role in determining FG emulsification properties.

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Intermolecular interaction and complex coacervation between bovine serum albumin and gum from whole flaxseed (Linum usitatissimum L.)

Cited by 88 publications

References 48 publications

Effects of Mixing Ratio and pH on the Electrostatic Interactions of Hydrolyzed Alaska Pollock Protein and κ‐Carrageenan

Effects of Mixing Ratio and pH on the Electrostatic Interactions of Hydrolyzed Alaska Pollock Protein and κ‐Carrageenan

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

Conlinin in flaxseed (Linum usitatissimum L.) gum and its contribution to emulsification properties

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