Effect of pectin adsorption on the hydrophobic binding sites of β-lactoglobulin in solution and in emulsion systems

Benjamin, Ofir; Lassé, Moritz; Silcock, Patrick; Everett, David W.

doi:10.1016/j.idairyj.2011.12.007

Cited by 22 publications

(5 citation statements)

References 26 publications

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“…A possible explanation could be that pectin would interact with proteins via hydrophobic interactions involving the methoxyl groups of pectin . It is, however, difficult to generalize this effect, as opposite trends were also reported in the literature . Presumably, the type of pectin (and notably its degree of methoxylation), the type of protein, and the probe used to assess surface-exposed hydrophobicity are of importance in that respect.…”

Section: Resultsmentioning

confidence: 97%

“…44 It is, however, difficult to generalize this effect, as opposite trends were also reported in the literature. 45 Presumably, the type of pectin (and notably its degree of methoxylation), the type of protein, and the probe used to assess surface-exposed hydrophobicity are of importance in that respect. Previous studies showed that protein oxidation is also a relevant parameter that affects surface hydrophobicity.…”

Section: Resultsmentioning

confidence: 99%

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Protein Oxidation and In Vitro Gastric Digestion of Processed Soy-Based Matrices

Duque-Estrada

Berton‐Carabin

Nieuwkoop

et al. 2019

J. Agric. Food Chem.

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Process conditions that are applied to make structured soy-protein-based food commonly include high temperatures. Those conditions can induce protein oxidation, leading to a decrease in their susceptibility to proteolysis by digestive enzymes. We aimed to investigate the effects of thermomechanical processing on oxidation and in vitro gastric digestion of commercial soy protein ingredients. Samples were sheared at 100 to 140 °C and characterized for acid uptake, carbonyl content, electrophoresis, and surface hydrophobicity. The enzymatic hydrolysis was determined in simulated gastric conditions. Protein ingredients were already oxidized and showed higher surface hydrophobicity and hydrolysis rate compared with those of the processed matrices. However, no clear correlation between the level of carbonyls and the hydrolysis rate was found. Therefore, we conclude that gastric digestion is mostly driven by the matrix structure and composition and the available contact area between the substrate and proteolytic enzymes.

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Protein Oxidation and In Vitro Gastric Digestion of Processed Soy-Based Matrices

Duque-Estrada

Berton‐Carabin

Nieuwkoop

et al. 2019

J. Agric. Food Chem.

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show abstract

“…At the same ion concentration, the increase of the divalent ions group was significantly higher than potassium ion group. That might be attributed to the electrostatic shielding effect generated by metal ions, which strengthened the hydrophobic interaction among protein molecules and promoted the hydrophobic aggregation between egg yolk proteins, leading the tryptophan residues to be wrapped in hydrophobic structures inside the protein ( Benjamin et al, 2012 ). Compared with monovalent ion, divalent ions carried more positive charges and had stronger shielding ability, thus resulting in a large increase in the fluorescence intensity.…”

Section: Resultsmentioning

confidence: 99%

Divalent metal ions under low concentration environment improved the thermal gel properties of egg yolk

Li,

Zhang,

et al. 2024

Poultry Science

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“…A theory that Octadecatetraenoic acid was suitable for detecting some protein was raised in reference [3][4] . Then, Canadian scientists Haskard et al [5][6][7] put forward an idea that PRODAN probe can be used to detect the protein surface hydrophobicity. However, considering the cases that the hydrophobic values detected by CPA and ANS were usually different cannot be explained reasonably, and the drew back that when using the probe method, the interaction between ion probe and protein may be take place, the Fluorescent probe method was not the optimal scheme to solve the problem of protein hydrophobicity.…”

Section: Related Workmentioning

confidence: 99%

Analysis on hydrophobic properties of proteins based on Giraph

Fan¹,

He²,

Wang³

2015

Advances in Intelligent Systems Research

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The previous experiments have shown that hydrophobic properties of 20 kinds of human's amino acid are different. It was of great significance to study whether hydrophobicity of proteins had a role in the research of the intimate relationship of proteins. Besides, it is also very important to balance the proteins'structure and function. Because of the highly complex data produced by hydrophobic proteins, it is suggested to build a computational graph model to solve this problem. In this paper, Giraph platform is used to calculate the data that come from protein interaction database (DIP). After analyzing the big graph models composed of protein data, this thesis compared the results with those of Cytoscape which is a traditional protein analysis software and finally came to the same conclusions. What's more, Cytoscape didn't work when the data of proteins were huge. But Giraph turned out to be more accurate and efficient.

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Effect of pectin adsorption on the hydrophobic binding sites of β-lactoglobulin in solution and in emulsion systems

Cited by 22 publications

References 26 publications

Protein Oxidation and In Vitro Gastric Digestion of Processed Soy-Based Matrices

Protein Oxidation and In Vitro Gastric Digestion of Processed Soy-Based Matrices

Divalent metal ions under low concentration environment improved the thermal gel properties of egg yolk

Analysis on hydrophobic properties of proteins based on Giraph

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