Gas-Liquid Chromatography and Mass Spectrometry of Lanthionine, Lysinoalanine, and S-Carboxyethylcysteine

Sakamoto, Munenori; Nakayama, Fumitaka; Kajiyama, Koh-ichi

doi:10.1007/978-1-4684-3282-4_41

Cited by 9 publications

(3 citation statements)

References 33 publications

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“…(B) Mechanisms of OH --catalyzed transformation of a protein cystine to dehydroalanine. Related studies on the determination of LAL in processed proteins and foods by GC after derivatization to n-butyl esters of N(O)-trifluoroacetyl derivatives are described by Buser and Erbersdobler (1984), Hasegawa and Iwata (1982), Hasegawa et al (1987), Sakamoto et al (1977), and Schwass and Finley (1984).…”

Section: Discussionmentioning

confidence: 99%

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Friedman

1999

J. Agric. Food Chem.

310

294

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Heat and alkali treatments of foods, widely used in food processing, result in the formation of dehydro and cross-linked amino acids such as dehydroalanine, methyldehydroalanine, beta-aminoalanine, lysinoalanine (LAL), ornithinoalanine, histidinoalanine (HAL), phenylethylaminoalanine, lanthionine (LAN), and methyl-lanthionine present in proteins and are frequently accompanied by concurrent racemization of L-amino acid isomers to D-analogues. The mechanism of LAL formation is a two-step process: first, hydroxide ion-catalyzed elimination of H(2)S from cystine and H(2)O, phosphate, and glycosidic moieties from serine residues to yield a dehydroalanine intermediate; second, reaction of the double bond of dehydroalanine with the epsilon-NH(2) group of lysine to form LAL. Analogous elimination-addition reactions are postulated to produce the other unusual amino acids. Processing conditions that favor these transformations include high pH, temperature, and exposure time. Factors that minimize LAL formation include the presence of SH-containing amino acids, sodium sulfite, ammonia, biogenic amines, ascorbic acid, citric acid, malic acid, and glucose; dephosphorylation of O-phosphoryl esters; and acylation of epsilon-NH(2) groups of lysine. The presence of LAL residues along a protein chain decreases digestibility and nutritional quality in rodents and primates but enhances nutritional quality in ruminants. LAL has a strong affinity for copper and other metal ions and is reported to induce enlargement of nuclei of rats and mice but not of primate kidney cells. LAL, LAN, and HAL also occur naturally in certain peptide and protein antibiotics (cinnamycin, duramycin, epidermin, nisin, and subtilin) and in body organs and tissues (aorta, bone, collagen, dentin, and eye cataracts), where their formation may be a function of the aging process. These findings are not only of theoretical interest but also have practical implications for nutrition, food safety, and health. Further research needs are suggested for each of these categories. These overlapping aspects are discussed in terms of general concepts for a better understanding of the impact of LAL and related compounds in the diet. Such an understanding can lead to improvement in food quality and safety, nutrition, microbiology, and human health.

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Section: Discussionmentioning

confidence: 99%

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Friedman

1999

J. Agric. Food Chem.

310

294

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“…Gas-liquid chromatography has been also utilized (Sakamoto et al, 1975(Sakamoto et al, ,1977Hasegawa and Okamoto, 1980;Hasegawa and Iwate, 1982). All employ the use of trifluoroacetylbutyl esters and a means to volatilize the hydrolysate mixture before analysis.…”

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confidence: 99%

Lysinoalanine in foods

Maga¹

1984

J. Agric. Food Chem.

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The formation of lysinoalanine has been primarily associated with the alkaline treatment or heat processing of proteins. The chemistry, food occurrences, nutritional significance, and methods available for the analysis of this phenomenon, relative to the literature, are discussed.Lysinoalanine (LAL) [JV'-(DL-2-amino-2-carboxyethyl)-L-lysine] represents a unique amino acid that apparently has been present in our food supply for centuries, especially in products that undergo alkaline processing and/or heating of a protein-containing food. In addition, Gross et al. (1975) report that LAL is a natural constituent of cinnamycin and duramycin, which are two peptides present in certain species of Streptomyces.However, it was not until the mid 1960s that LAL was actually identified (Patchornik and Sokolovsky, 1964b;Bohak, 1964). Since that time numerous studies have been reported in an attempt to more completely understand its formation mechanism(s), ways of minimizing its formation, and levels present in foods and, most importantly, to identify its specific nutritional and potential toxicological significance relative to food processing and preparation. Several reviews have appeared that discuss certain aspects of the above (Sternberg and Kim, 1977;de Groot et al., 1977;Struthers, 1981), but no review has attempted to provide an inclusive overview of the entire subject. Thus, the primary objective of this review is to more extensively discuss the literature to date in an effort to summarize our knowledge of LAL in food and to point out areas that need further investigation or clarification.

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“…The LAL content of protein and food samples has been determined by electrophoresis (Miro & Garcia-Dominguez, 1967), gas-liquid chromatography with mass spectrometry detection (Sakamoto et al 1977), thin-layer chromatography (Sternberg et al 1975a;Haagsma & Gortemaker, 1979), high-pressure liquid chromatography (Wood-Rethwill & Warthesen, 1980) and ion-exchange chromatography by use of an automatic amino acid analyser (Slump, 1977). It may be difficult to establish sometimes the real identity of a band or peak in the chromatogram obtained by one of the above-mentioned techniques if other compounds are present having the same position as LAL.…”

Section: Determination Of Lalmentioning

confidence: 99%

Aspects of the formation of lysinoalanine in milk and milk products

Koning¹,

Rooijen²

1982

Journal of Dairy Research

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SUMMARYTreatment of food proteins with heat and/or alkali may convert some of the constituent amino acids into the unnatural amino acid lysinoalanine (LAL), which has been found to cause kidney damage (nephrocytomegaly) when fed to rats. LAL may be produced by β-elimination of a phosphoseryl, of a glycosylated seryl or of a cystyl residue followed by a nucleophilic addition to a lysyl residue. The formation of LAL in αs0-, αsl- and β-casein is discussed in relation to the location of phosphoseryl residues immediately adjacent to lysyl residues. The influence of pH, temperature and exposure time on the formation of LAL in whole casein is described in detail. The formation of LAL can be prevented by the addition of reducing agents, dephosphorylation or chemical modification of the є-amino group of lysine. The LAL content of foodstuffs can be measured accurately by ion-exchange chromatography and a survey is given of the LAL content of commercial milk and milk products.The biological effects of free and protein-bound LAL are discussed. It seems that renal changes due to the presence of LAL in the diet are species-specific to the rat although recent findings have shown that no effect is observed in rats fed a mixed diet containing proteins with and without protein-bound LAL. When LAL is removed from the diet, nephrocytomegaly disappears. From these results it may be concluded that the health risks for man, connected with the eating of proteins which have been subjected to treatment with heat and/or alkali, are small.The decrease in lysine content of milk and milk products due to formation of LAL is small (0–1 or 2%) in comparison with the decrease in available lysine possibly caused by the Maillard reaction (0–24%) and so the decrease in nutritive value of food products due to LAL formation may be neglected.

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Gas-Liquid Chromatography and Mass Spectrometry of Lanthionine, Lysinoalanine, and S-Carboxyethylcysteine

Cited by 9 publications

References 33 publications

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Lysinoalanine in foods

Aspects of the formation of lysinoalanine in milk and milk products

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