2003
DOI: 10.1021/jf021229w
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Effects of Non-covalent Interactions with 5-O-Caffeoylquinic Acid (Chlorogenic Acid) on the Heat Denaturation and Solubility of Globular Proteins

Abstract: The non-covalent interactions between the monomeric phenolic compound chlorogenic acid (5-CQA) and bovine serum albumin (BSA), lysozyme, and alpha-lactalbumin were characterized, and their effect on protein properties was examined. 5-CQA had a low affinity for all three proteins, and these interactions seemed to show a negative cooperativity. 5-CQA-BSA binding decreased with increasing temperature, whereas pH (pH 3.0 compared to pH 7.0) and ionic strength had no pronounced effect. At high 5-CQA/protein molar r… Show more

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Cited by 235 publications
(179 citation statements)
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“…This increase in gel strength might be attributed to the cross-linking activity of phenolic compounds present in the seaweed extract which could induce the formation of both covalent and non-covalent bonds of gel matrix (Prigent et al 2003). The result is in accordance with that of Balange and Benjakul (2009b) who reported the increases in breaking force and deformation of mackerel surimi with the addition of kiam wood extract containing phenolic compound.…”
Section: Quantification Of Total Phenolic Contentsupporting
confidence: 87%
See 1 more Smart Citation
“…This increase in gel strength might be attributed to the cross-linking activity of phenolic compounds present in the seaweed extract which could induce the formation of both covalent and non-covalent bonds of gel matrix (Prigent et al 2003). The result is in accordance with that of Balange and Benjakul (2009b) who reported the increases in breaking force and deformation of mackerel surimi with the addition of kiam wood extract containing phenolic compound.…”
Section: Quantification Of Total Phenolic Contentsupporting
confidence: 87%
“…In the gels with and without WSE, the decrease in solubility suggests the formation of protein aggregates during setting and heating (Balange and Benjakul 2009a). Also hydrophobic interactions may occur between phenolic compounds and hydrophobic amino acids such as alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, tryptophan, cysteine and glycine residues (Prigent et al 2003). The lower solubility obtained in the present investigation is very well correlating with higher gel strength and lower expressible moisture when added with 2 % WSE in surimi gel.…”
Section: Effect Of Wse On Expressible Moisturementioning
confidence: 99%
“…Covalent interactions of proteins and polyphenols oxidized to quinones decrease the number of free primary amino groups of the proteins, cause protein dimerization, and reduce their solubility. Side chains of lysine and tyrosine in proteins appeared the most susceptible residues to react with oxidized polyphenols [22][23][24]. Non-covalent interactions including hydrogen and ionic bonds and hydrophobic interactions cause an increase in proteins denaturation enthalpy and temperature and this type of bonding may be digested by human digestive tract enzymes and the released hydroxycinnamic acids may be active as antioxidants in the body [25].…”
Section: Resultsmentioning
confidence: 99%
“…Chlorogenic acid content was measured with a spectrophotometer (Prigent et al 2003) using ten graft unions. The samples were weighed, ground in liquid nitrogen, transferred to 10-mL centrifuge tube containing 5 mL 80% methanol, placed in refrigerator at 4°C after shaking extraction for about 4 h, and centrifuged at 3500 r/min at 4°C for 8 min, after which the supernatant passed through C-18 solid-phase extraction column (column Steps were 80% methanol, 100% methanol, 100% diethyl ether, and 100% methanol cycle) using 80% methanol as a control and absorbance was measured using 756 UV-visible spectrophotometer at 324 nm wavelength.…”
Section: Measurement Methodsmentioning
confidence: 99%