Mechanisms of heat damage in proteins

Hurrell, Richard F.; Carpenter, K. J.; Sinclair, William John; Otterburn, M. S.; Asquith, R. S.

doi:10.1079/bjn19760044

Cited by 100 publications

(16 citation statements)

References 43 publications

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“…That the dairy products contained no e-(y-glutamyl)lysine bond could support such an idea, since milk itself does not contain any intrinsic transglutaminases. Besides the catalytic action of the intrinsic transglutaminases, heating was reported to induce formation of e-(y-glutamyl)lysine bonds due to chemical dehydration between the y-carboxyl group of glutamate and eamino group of lysine (57)(58)(59). Thus in the presence of transglutaminase, cooking itself results in e-Cy-glutamyOlysine formation in proteins.…”

Section: Microbial Transglutaminase Derived From a Variant Of Streptomentioning

confidence: 97%

Some Characteristics of a Microbial Protein Cross-Linking Enzyme: Transglutaminase

Seguro

Nio

Motoki

1996

ACS Symposium Series

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Some characteristics of a transglutaminase derived from a variant of Streptoverticillium mobaraense (MTGase) were investigated. MTGase catalyzes the crosslinking of most food proteins, such as caseins, soybean globulins, gluten, actin, myosins, and egg proteins, through the formation of ε-(γ-glutamyl)lysine bond, as well as the well-known guinea pig liver enzyme. Molecular weight as determined by SDS--PAGE and mass spectrometry was 38,000 and 37,824, respectively. This indicates MTGase is a simple, monomelic enzyme. Inhibitory effects by thiol-modifying agents as well as copper, lead, and zinc ions on MTGase indicate that MTGase is a thiol-enzyme. For digestion of the MTGase-catalyzed crosslinked proteins, γ-glutamyltransferase was found to cleave the ε-(γ-glutamyl)lysine bond into lysine and glutamate. Lysine in the ε-(γ-glutamyl)lysine bond was, actually, utilized as an essential amino acids in rats.In tertiary and quaternary structures of protein molecules, bonds and interactions such as hydrogen bond, disulfide bond, electrostatic, and van der Waal's hydrophobic interactions, greatly contribute to their formation and maintenance. Especially in food, not only these, but also other bonds, particularly those found in connective tissues, are very important in the expression of textures or how food feels in the mouth. Among such bonds and interactions, e-(y-glutamyl)lysine crosslinking is considered noteworthy. To illustrate, transglutaminase (protein-glutamine yglutamyltransferase, EC 2.3.2.13) primarily catalyzes an acyl transfer reaction between the y-carboxyamide group of peptide-bound glutaminyl residue and a variety of primary amines (1-6). If no amines are present in the reaction system, transglutaminase catalyzes the hydrolysis of the y-carboxyamide group of the glutaminyl residue, resulting in deamidation (1-7). When the e-amino group of peptide-bound lysyl residue acts as a substrate, peptide chains are covalently connected through e-(y-glutamyl)lysine bonds (Figure 1). A typical example of such transglutaminase-catalyzed protein crosslinking reaction is the termination of bleeding in wound healing (blood coagulation) by Factor Xllla, an activated form of plasma transglutaminase (8-9). Another example of such a reaction is the setting phenomenon or "suwari" of salted, ground fish protein pastes in Japanese kamaboko

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Section: Microbial Transglutaminase Derived From a Variant Of Streptomentioning

confidence: 97%

Some Characteristics of a Microbial Protein Cross-Linking Enzyme: Transglutaminase

Seguro

Nio

Motoki

1996

ACS Symposium Series

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“…Good agreement was observed between the FDNB-reactive lysine values determined by the 'direct' and by the 'difference' methods, indicating that the bound lysine residues regenerated the same amount of lysine on acid-hydrolysis before and after FDNB treatment. This is in contrast to the behaviour of lactulosyl-lysine after early Maillard reactions (Hurrell et al 1983) and bound lysine after caffeic acid reactions (Hurrell et al 1982) but similar to the behaviour of glutamyl-lysine or aspartyl-lysine (Hurrell et al 1976). Karel et al (1975) reported that a-amino adipic acid could be formed from lysine during lipid oxidation.…”

Section: Discussionmentioning

confidence: 50%

Reactions of proteins with oxidizing lipids

1985

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1. The reactions between protein-bound amino acids and oxidizing lipid were investigated in a whey protein-methyl linolenate (C18 &water model system. The extent of fat oxidation was followed by measuring oxygen uptake, hydroperoxide formation and hydrocarbon (ethane and pentane) formation.2. Significant losses occurred with lysine (up to 71 %), tryptophan (up to 31 %) and histidine (up to 57%).Methionine was extensively oxidized to its sulphoxide but less than 2% was further oxidized to the sulphone. No other amino acids were affected.3. Increasing storage temperature (20", 37", 55") resulted in an enhancement of fat oxidation reactions and amino acid degradation.4. Increasing water activity (0.28, 0.65, 0.90) increased losses of lysine and tryptophan but had no influence on the oxidation of methionine, the level of remaining hydroperoxides or 0, uptake. Hydrocarbons were decreased.5. Limitation of 0, uptake to 1 mol/mol lipid instead of excess 0, (0, uptake about 2.5 mol/mol lipid in 4 weeks) significantly reduced the degradation of lysine and tryptophan but had less influence on the oxidation of methionine. The level of remaining hydroperoxides was increased but hydrocarbons were unaffected.

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“…Rbc 111), erythrocytes yielded 62% trans3 and 38% cis-3. Traces of syn-(ethy1,methyl)bimane (14), syn-( 1-bromoethyl,methyl)(ethyl,methyl)bimane (19) and syn-(1-hydroxyethyl,methyl)(ethyl,methyl) bimane (15) were found. Up to 23% unreacted 2 was recovered in some runs.…”

Section: Htsmentioning

confidence: 97%

“…The effect of the transformation of cystine S-S links into lanthionine S bonds has been extensively investigated with respect to crosslinking in proteins [13,141, the dyeing and solubility properties of wool [ 15-171 and hair [ 181, and the nutritional availability of proteins [19]. In all cases, the results suggest the occurrence of basic structural modifications.…”

Section: Introductionmentioning

confidence: 94%