Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid

Rawel, Harshadrai M.; Rohn, Sascha; Kruse, H.‐P.; Kröll, J.

doi:10.1016/s0308-8146(02)00155-3

Cited by 202 publications

(158 citation statements)

References 24 publications

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“…They reported that there was a reduction in structured elements and increase in unordered structure upon incubation of protein with coffee specific phenolic compounds. Rawel et al (2002b) reported that upon interaction of chlorogenic acid with bovine serum albumin (BSA), there was a reduction in a helix with a parallel increase in remaining structures, indicating destructing effect on BSA. Contrary to these results Kanakis et al (2011) reported different results for b lactoglobulin upon interaction with polyphenols.…”

Section: Results and Discussion Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

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Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

2016

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The present study evaluated the effect of removal of polyphenols on the structural properties of protein isolates extracted from sunflower seed and kernel. The structural and thermal changes in protein upon phenolic interaction were studied using circular dichroism, differential scanning calorimetry, thermal gravimetric analysis, X-ray diffraction, sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE), and Fourier Transform Infrared (FT-IR) spectroscopy. Presence of phenolic compounds in proteins decreased the ordered structure content with parallel increase in unordered structure content. Denaturation temperature was higher for protein isolates with phenolic compounds while, enthalpy decreased upon phenolic interaction. In the presence of phenolic compounds, higher mass loss was observed upon heating. Crystalinity and crystal size got increased after removal of phenolic compounds. Protein isolates from kernels had higher percentage of crystalinity and crystal size as compared to seed protein isolates. Higher molecular weights were observed for protein isolates with phenolic compounds. Presence of polyphenols reduced the hydrophobicity as well the sulfhydryl content and increased the particle size of proteins.

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Section: Results and Discussion Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

“…Various researchers have revealed the structural changes in proteins upon phenolic interaction (Ali et al 2013;Rawel et al 2002b;Jia et al 2016). Modification of protein structure upon phenolic interaction has direct implication on the behaviour of protein during processing, preparation, consumption and storage in food systems.…”

Section: Introductionmentioning

confidence: 99%

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

2016

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“…The interaction of the aromatic ring of caffeic acid with aromatic residues such as tyrosine and tryptophan of the protein may be responsible for quenching of fluorescence intensity based on tryptophan fluorescence experiments (Suryaprakash et al, 2000). Such interactions can be confirmed as shown by the progressive decrease in the amount of free tryptophan (Suryaprakash et al, 2000;Rawel et al, 2002b). From the progressive quenching and the red shift observed in the maximum fluorescence emission of derivatized BSA, it can be deduced that conformational changes induced by the modification lead to a further exposure of tryptophan residues to the polar solvent (Jackman & Yada, 1989;Gerbanowski et al, 1999).…”

Section: Characterization Of Structural Changes In Protein-phenolderimentioning

confidence: 90%

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Kröll

Rawel

Rohn

2003

FSTR

Self Cite

331

273

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Secondary plant metabolites are important native food components, which are becoming more and more interesting due to their physiological effects on human beings. One of the largest groups of these compounds is represented by plant phenols. This review summarizes the structure, classification and distribution of the phenolic compounds in plant foods, their chemistry and signification with regard to food processing and -storage as well as their physiological effects. This work focuses mainly on such reactions of the phenolic substances with proteins and enzymes that lead to covalent bonds. The derivatives formed have been characterized in terms of changes in their physicochemical and structural properties. The effect on the proteolytic in vitro digestion has been also illustrated. Further aspects reported include the influence on enzyme activity and -kinetic parameters. The different aspects of the nutritional-physiological consequences of such reactions in food and body, especially considering their significance to food science and technology are discussed.

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“…Depending on the type of protein, solubility decreased in the following order WPC < EWP < SPI and it was not correlated with AMM changes, which were the least for SPI. Thus, also other factors such as changes in isoelectric point, conformation and density of molecule could affect protein solubility [43]. Temperature rise during interactions contributed to greater solubility decrease.…”

Section: Solubility Of Proteins After Interactions With Hcasmentioning

confidence: 99%

Changes in properties of food proteins after interaction with free and β-cyclodextrin encapsulated hydroxycinnamic acids

Budryn

Zaczyńska

Rachwał-Rosiak

2015

Eur Food Res Technol

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Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid

Cited by 202 publications

References 24 publications

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Changes in properties of food proteins after interaction with free and β-cyclodextrin encapsulated hydroxycinnamic acids

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