2014
DOI: 10.1016/j.idairyj.2013.10.011
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Cross-linking with microbial transglutaminase: Relationship between polymerisation degree and stiffness of acid casein gels

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Cited by 32 publications
(20 citation statements)
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“…Peptide bonds between terminal functional groups, referred to as isopeptide bonds, are not susceptible to most proteolytic enzymes and remain therefore intact after total enzymatic protein hydrolysis; subsequent amino acid analysis by chromatographic techniques enables the determination of the N-ε-(γ-glutamyl)-lysine isopeptide [29]. Although the isopeptide content was shown to be an important driver for the stiffness of acid-induced casein gels, polymer size still has to be taken into account [30][31][32]. Besides TGase, oxidoreductases were applied, which have a completely different cross-linking mechanism: firstly, the enzymes oxidise specific functional groups that react further in non-enzymatic reactions.…”
Section: Cross-linking Enzymesmentioning
confidence: 99%
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“…Peptide bonds between terminal functional groups, referred to as isopeptide bonds, are not susceptible to most proteolytic enzymes and remain therefore intact after total enzymatic protein hydrolysis; subsequent amino acid analysis by chromatographic techniques enables the determination of the N-ε-(γ-glutamyl)-lysine isopeptide [29]. Although the isopeptide content was shown to be an important driver for the stiffness of acid-induced casein gels, polymer size still has to be taken into account [30][31][32]. Besides TGase, oxidoreductases were applied, which have a completely different cross-linking mechanism: firstly, the enzymes oxidise specific functional groups that react further in non-enzymatic reactions.…”
Section: Cross-linking Enzymesmentioning
confidence: 99%
“…This leads to a variety of covalent bonds so that the total number of cross-links can hardly be determined by amino acid analysis [23]. Monogioudi et al [33] applied 31 P nuclear magnetic resonance spectroscopy after phosphorylation of hydroxyl groups to quantify cross-links formed in β-casein after oxidation of tyrosine residues by tyrosinase (EC 1.14.18.1). Recently, cross-linking with laccase (EC 1.10.3.2) was tested for its potential to improve the structure of stirred yoghurt gels in a post-fermentation step because of the acidic pH optimum of the enzyme.…”
Section: Cross-linking Enzymesmentioning
confidence: 99%
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