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Selected enzymes (alpha-amylase, trypsin, and lysozyme) were allowed to react with some simple phenolic and related compounds (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, m-, o-, and p-dihydroxybenzenes, quinic acid, and p-benzoquinone). The derivatized enzymes obtained were characterized in terms of their activity. In vitro experiments showed that the enzymatic activity of the derivatives was adversely affected. This enzyme inhibition depended on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. The decrease in the activity was accompanied by a reduction in the amount of free amino and thiol groups, as well as tryptophan residues, which resulted from the covalent attachment of the phenolic and related compounds to these reactive nucleophilic sites in the enzymes. The enzyme inhibition correlates well with the blocking of the mentioned amino acid side chains.
Secondary plant metabolites are important native food components, which are becoming more and more interesting due to their physiological effects on humans. Some representatives of these compounds are very reactive and can interact with other main food components like proteins resp. enzymes. This work deals with the reactions of selected enzymes (trypsin, alpha-chymotrypsin and alpha-amylase) with simple phenolic and related substances (caffeic acid, chlorogenic acid, ferulic acid, gallic acid, meta-, ortho- and para-dihydroxybenzene, 1,4-benzoquinone, quinic acid). The derivatives formed were characterized in terms of their activity and selected physicochemical properties. In vitro experiments showed that the proteolytic digestion of food proteins with trypsin and alpha-chymotrypsin derivatives was adversely affected. This decrease depends on the reactivity of the phenolic and related substances tested as well as on the kind of substrate applied. Reactions of phenolic compounds with other enzymes (alpha-amylase and lysozyme) showed similar results with regard to physicochemical properties and their activities.
Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid
(2002)
Bovine serum albumin (BSA) was modifed by covalent attachment of chlorogenic acid using different concentrations at pH 9. The derivatization was accompanied by a reduction of lysine, cysteine and tryptophan residues. The isoelectric points were shifted to lower pH values and formation of high molecular weight fractions was noted. The structural changes were studied using circular dichroism, differential scanning calorimetry (DSC), intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The results showed that the content of alpha-helix decreased with a parallel increase in unordered structures with higher degrees of derivatization. DSC revealed a decrease in both denaturation temperature and enthalpy. Surface hydrophobicity declined, indicating that hydrophilic regions were exposed on the molecular surface. Proteolytic digestion showed that, at a lower degree of derivatization,the tryptic degradation was most adversely effected, whereas the peptic digestion declined with increasing modification. A trypsin inhibitory effect of the breakdown products released from derivatized BSA was also observed.
Soy glycinin (SG) and soy trypsin inhibitor (STI) were derivatized by chlorogenic- and caffeic acid (cinnamic acids, C6 - C3 - structure), and by gallic acid representing hydroxybenzoic acids (C6 - C1 - structure). Further, the flavonoids, flavone, apigenin, kaempferol, quercetin and myricetin (C6 - C3 - C6 - structure) were also caused to react with soy proteins to estimate the influence of the number and the position of hydroxy substituents. The derivatization caused a reduction of lysine, cysteine and tryptophan residues in the soy proteins. The isoelectric points of the derivatives were shifted to lower pH values and formation of high molecular fractions was documented. The derivatives were characterized in terms of their solubility at different pH-values to document the influence on the functional properties. The structural changes induced were studied using circular dichroism (CD), differential scanning calorimetry (DSC) , intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The influence of derivatization on the in-vitro digestibility with trypsin, chymotrypsin, pepsin and pancreatin was also assessed. The effect on the trypsin inhibitor activity of all the resulting STI derivatives was studied, the latter being reduced.
Selected food proteins (myoglobin and soy glycinin) were caused to react with flavonoids (apigenin and quercetin) to estimate the influence of the number and the position of hydroxy substituents. The protein derivatives formed have been charcterized in terms of their properties where they showed changes in the content of free amino groups, tryptophan, and thiol groups. The myoglobin derivatives have also been characterized in terms of their solubility at different pH-values to document the influence on the functional properties. The influence of myoglobin derivatives on the in vitro digestibility with trypsin was also demonstrated, with the digestion of the derivatized myoglobin being favored.
Background/Aims: Prostaglandin E(2) (PGE(2)) is known to inhibit the lipopolysaccharide (LPS)-induced tumor necrosis factor alpha (TNFalpha) formation in Kupffer cells via an increase in cAMP. Four receptor-subtypes have been cloned for PGE(2) so far. Two of them, the EP2-receptor and the EP4-receptor are linked to stimulatory Gs-proteins and could mediate the inhibition by PGE(2) of TNFalpha-formation.Methods: The significance of both receptors for PGE(2)- dependent inhibition of LPS-induced TNFalpha-formation was studied using Kupffer cells of mice in which either one of the two receptors had been eliminated by homologous recombination.Results: The mRNAs of both receptors were expressed in wild type mouse Kupffer cells. Exogenous PGE(2) inhibited TNFalpha-formation in Kupffer cells lacking either EP2-receptor or EP4-receptor to a similar extent as in control cells, however, 10-fold higher PGE(2) concentrations were needed for half maximal inhibition in cells lacking the EP4-receptor than in control or EP2-receptor- deficient cells. The response to endogenous PGE(2) was blunted in EP4-receptor-deficient mice only and especially after prolonged incubation. Conclusions: The data indicate, that PGE(2) can inhibit TNFalpha-formation via both the EP2- and the EP4-receptor and that, however, the EP4-receptor appears to be physiologically more relevant in Kupffer cells since it conferred a high affinity response to PGE(2).