Lysinoalanine Formation in Protein Food Ingredients

Sternberg, M.; Kim, C. Y.

doi:10.1007/978-1-4757-9113-6_5

Cited by 53 publications

(22 citation statements)

References 6 publications

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“…1 ,2,7) The formation of LAL by heating in the acidic and neutral pH regions has also been reported. 14 ) As shown in Table I, the finding of significant amounts of LAL in pidan and raw Chinese noodles seems to be based on alkaline exposure of these foods during processing and storage. In the foods which were not exposed to an alkaline medium (egg, soybean prod" ucts, meat products), the LAL content was slightly increased by heating.…”

Section: Lal Content In Commercial Foodsmentioning

confidence: 95%

Determination of the Lysinoalanine Content in Commercial Foods by Gas Chromatography-selected Ion Monitoring

Hasegawa

Mukai

Gotoh

et al. 1987

Agricultural and Biological Chemistry

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Section: Lal Content In Commercial Foodsmentioning

confidence: 95%

Determination of the Lysinoalanine Content in Commercial Foods by Gas Chromatography-selected Ion Monitoring

Hasegawa

Mukai

Gotoh

et al. 1987

Agricultural and Biological Chemistry

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“…Besides the concentration of the reaction educts, LAL formation in foods is enhanced by a strong alkaline pH [4,21,22], temperatures within a range of 70 8C to 105 8C [4,22], and the addition of divalent cations, mainly calcium [4,20,23]. Moreover, the three-dimensional steric structure of casein is more pronounced to form LAL during heat treatment compared to plant-derived proteins like that from soy or wheat [24].…”

Section: Characterisation Of the Lal-fortified Model Proteinmentioning

confidence: 99%

“…These results indicate that the experimental conditions chosen for the preparation of LAL-MP are suitable for a selective LAL-fortification of casein. The application of higher temperatures and/or longer heating times is expected to result either in an advanced degradation of LAL [4,21,22,[25][26][27].…”

Section: Characterisation Of the Lal-fortified Model Proteinmentioning

confidence: 99%

Selective fortification of lysinoalanine, fructoselysine and Nε-carboxymethyllysine in casein model systems

Faist¹,

Müller²,

Drusch³

et al. 2001

Nahrung

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In the present study, a promising strategy to study nutritional effects of selected chemical reaction products formed in heat treated protein containing foods is addressed. In due course, a selective fortification of different marker compounds for lysine damage in casein-sugar mixtures was performed to provide model systems being applicable to investigate biological effects of the cross-link lysinoalanine (LAL), the MRPs fructoselysine (FL) and N epsilon-carboxymethyllysine (CML) in a casein-linked preparation. The three different model proteins, casein-LAL, casein-FL and casein-CML were prepared by heating casein either in strong alkaline conditions at 105 degrees C for 1 h, in the presence of glucose at 65 degrees C for 68 h, or in the presence of glyoxylic acid at 37 degrees C for 19 h. Finally, the degree of lysine modification achieved was 39%, 75% and 55% for the casein-LAL, casein-FL and casein-CML, respectively. The calculation of lysine recovery and the respective analysis of each single modified casein (LAL-, FL- and CML-MP) for the selected fortified compound and each other compound vice versa proved that the individual procedure provides a specific fortification for LAL, FL and CML, respectively. The modified proteins are suitable as reference model proteins to be investigated for specific biological and toxicological effects of casein-linked LAL, FL and CML.

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“…It is known in the literature that the alkaline treatments of the proteins which contain phosphoserine eliminate its phosphate to form dehydroalanine, then lysinoalanine and histidinoalanine was formed through a reaction between dehydroalanine with lysine or histidine (7,8). However, the present preparation of phosphoprotein did not include any alkaline procedure.…”

Section: Resultsmentioning

confidence: 90%

Presence of lysinoalanine and histidinoalanine in bovine dentin phosphoprotein

et al. 1984

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Trypsin digestion and successive calcium-induced precipitation of the insoluble bovine dentin matrix effectively separated the collagen and phosphoprotein fractions which were firmly associated together in this material. Amino acid analysis by four different systems revealed that the lysinoalanine and histidinoalanine, which had been previously reported to occur in the human dentin collagen, were concentrated in the phosphoprotein fraction but were not present in the collagen fraction. Furthermore, it was found that the free-type phosphoprotein which was isolated from EDTA extract of dentin powder also contained both "cross-linking" amino acids. The results indicated the both "cross-links" distributed within the dentin phosphoprotein and were not likely to contribute the unique stability of dentin collagen.

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Lysinoalanine Formation in Protein Food Ingredients

Cited by 53 publications

References 6 publications

Determination of the Lysinoalanine Content in Commercial Foods by Gas Chromatography-selected Ion Monitoring

Determination of the Lysinoalanine Content in Commercial Foods by Gas Chromatography-selected Ion Monitoring

Selective fortification of lysinoalanine, fructoselysine and Nε-carboxymethyllysine in casein model systems

Presence of lysinoalanine and histidinoalanine in bovine dentin phosphoprotein

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