EFFECT OF ADDED CYSTEINE AND LYSINE UPON LYSINOALANINE LEVELS IN VARIOUS ALKALINE TREATED FOOD PROTEINS<sup>1</sup>

Warthesen, J. J.; Wood-Rethwill, J. C.

doi:10.1111/j.1745-4565.1980.tb00406.x

Cited by 5 publications

(4 citation statements)

References 19 publications

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“…Surprisingly, addition of cysteine to high-lysine corn caused an increase in the content of LAL (Warthesen and Wood-Rethwill, 1981). A possible explanation is that either cysteine underwent a β-elimination to dehydroalanine or, more likely, cysteine was first oxidized to cystine, which was then converted to dehydroalanine.…”

Section: Preventing Lal Formationmentioning

confidence: 99%

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

Friedman

1999

J. Agric. Food Chem.

307

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: Preventing Lal Formationmentioning

confidence: 99%

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

Friedman

1999

J. Agric. Food Chem.

307

294

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“…Friedman and others () reported that glutathione, L‐cysteine, and other sulfhydryl compounds can reduce LAL formation in alkali‐treated soy protein. In contrast, Warthesen and Wood‐Rethwill () discovered that the formation of LAL in corn is promoted by the addition of L‐cysteine. LAL formation mechanism includes 2 steps: the first step is the generation of dehydroalanine via β‐elimination reaction from cysteine, serine or serine phosphate, or sugar serine; and the 2nd step is dehydrogenation alanine residue double bond with lysine ε‐NH 2 via nucleophilic addition reaction to form LAL (Friedman ).…”

Section: Resultsmentioning

confidence: 96%

“…Additionally, the effect of L‐cysteine on LAL formation in preserved egg albumen and yolk was strongly dependent on its concentration, wherein the promotion of LAL formation was even observed within a certain concentration range (Figure a and b). According to the explanation of Warthesen and Wood‐Rethwill (), L‐cysteine, as a precursor for LAL formation, can be converted to dehydroalanine, either by directly β‐elimination reaction to dehydroalanine or by indirectly oxidation to cystine. The generation of dehydroalanine favors LAL formation by reacting with ε‐NH 2 of lysine.…”

Section: Resultsmentioning

confidence: 99%

Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved Egg

Luo

Zhao

et al. 2014

Journal of Food Science

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To identify inhibitors for lysinoalanine formation in preserved egg, sulfhydryl compounds (glutathione, L-cysteine), carbohydrates (sucrose, D-glucose, maltose), organic acids (L-ascorbic acid, citric acid, DL-malic acid, lactic acid), and sodium sulfite were individually added at different concentrations to a pickling solution to prepare preserved eggs. Lysinoalanine formation as an index of these 10 substances was determined. Results indicate that glutathione, D-glucose, maltose, L-ascorbic acid, citric acid, lactic acid, and sodium sulfite all effectively diminished lysinoalanine formation in preserved egg albumen and yolk. When 40 and 80 mmol/L of sodium sulfite, citric acid, L-ascorbic acid, and D-glucose were individually added into the pickling solution, the inhibition rates of lysinoalanine in the produced preserved egg albumen and yolk were higher. However, the attempt of minimizing lysinoalanine formation was combined with the premise of ensuring preserved eggs quality. Moreover, the addition of 40 and 80 mmol/L of sodium sulfite, 40 and 80 mmol/L of D-glucose, 40 mmol/L of citric acid, and 40 mmol/L of L-ascorbic acid was optimal to produce preserved eggs. The corresponding inhibition rates of lysinoalanine in the albumen were approximately 76.3% to 76.5%, 67.6% to 67.8%, 74.6%, and 74.6%, and the corresponding inhibition rates of lysinoalanine in the yolk were about 68.7% to 69.7%, 50.6% to 51.8%, 70.4%, and 57.8%. It was concluded that sodium sulfite, D-glucose, L-ascorbic, and citric acid at suitable concentrations can be used to control the formation of lysinoalanine during preserved egg processing.

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“…The quantitative determination of LAL is also important nutntionally, because its formation leads to a reduction in lysine and cysteine and consequently to a reduction in the nutritional value of food [9] Since LAL is formed in large quantities following drastic heat treatment, its content could be used as an indicator of the use of correct technological procedures The determination of LAL has been performed by different techniques: amino acid analysis [ lo], electrophoresis [11,12], gas chromatography [ 11,131, gas chromatography coupled with mass spectrometry [3,14], thin layer chromatography [ 15,161, ion ex-change chromatography [16,17], and high performance hquid chromatography (HPLC) [2, [18][19][20] An improvement in the quantitative analysis of LAL by HPLC could be achieved by changing the expenmental conditions, e g column and the composition of the mobile phase…”

Section: Introductionmentioning

confidence: 99%

Determination of lysinoalanine by high performance liquid chromatography

Moret

Cherubin

Rodríguez‐Estrada

et al. 1994

J. High Resol. Chromatogr.

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This work suggests an HPLC method for qualitative and quantitative determination of N-epsilon(2-amino-2-carboxyethyl)-L-lysine (LAL). LAL was released from total hydrolysates of various proteins of animal origin and derivatized with dansyl chloride, The performance of two different columns, Spherisorb 3S TG and mu-Bondapack C-18, was compared; better resolution and quantitative response were obtained with the former. The mobile phase was a mixture of 0.01 M phosphate buffer (pH 7) and acetonitrile. Linear response and quantitative repeatability were tested for both detectors used (UV-Vis set at 254 nm; fluorimetric set at lambda(ex(max))= 360 nm and lambda(em(max))= 525 nm). For LAL standard the minimum detectable amount was 0.05 ng, whereas for LAL in actual samples the amount was 0.5 ng (40 mu g/g of analyzed proteins). Good analytical repeatability was obtained, resulting in CV% of 4.7 and 3.8 for UV and fluorimetric detectors, respectively. LAL recovery was determined using both detectors; the values obtained were 94 % (fluorimetric) and 92 % (UV). Greater noise levels were observed with the fluorimetric detector and its higher sensitivity could not, therefore, be fully utilized, The highest amounts of LAL were found in the casein (2816 mu g/g) and cooked albumin (615 mu g/g) samples

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EFFECT OF ADDED CYSTEINE AND LYSINE UPON LYSINOALANINE LEVELS IN VARIOUS ALKALINE TREATED FOOD PROTEINS¹

Cited by 5 publications

References 19 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

Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved Egg

Determination of lysinoalanine by high performance liquid chromatography

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EFFECT OF ADDED CYSTEINE AND LYSINE UPON LYSINOALANINE LEVELS IN VARIOUS ALKALINE TREATED FOOD PROTEINS1

Cited by 5 publications

References 19 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

Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved Egg

Determination of lysinoalanine by high performance liquid chromatography

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EFFECT OF ADDED CYSTEINE AND LYSINE UPON LYSINOALANINE LEVELS IN VARIOUS ALKALINE TREATED FOOD PROTEINS¹