Growth response of mice and Tetrahymena pyriformis to lysinoalanine-supplemented wheat gluten

Sternberg, M.; Kim, Chong Y.

doi:10.1021/jf60225a028

Cited by 10 publications

(4 citation statements)

References 9 publications

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“…The PER of wheat gluten in rats increased from 0.65 to 1.62 on addition of 0.3% lysine and to 1.19 with an equimolar amount of LAL (Sternberg and Kim, 1979). In contrast, although the PER of 0.62 of gluten in mice also increased (to 0.85) with lysine addition, it decreased to 0.31 with LAL.…”

Section: Nutrition and Safetymentioning

confidence: 83%

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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: Nutrition and Safetymentioning

confidence: 83%

“…LAL as a Source of Lysine. The microorganisms Aspergillus niger, Bacillus subtilis, Erwinia chrysanthemi, Escherichia coli, and Tetrahymena pyriformis can utilize LAL as a source of lysine (Karayiannis et al, 1979a;Sternberg and Kim, 1979). They appear to be able to incorporate LAL-derived lysine but not LAL into proteins.…”

Section: Nutrition and Safetymentioning

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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“…Alkali treatment of protein is accompanied by loss of nutritional efficiency, because of racemization, destruction or chemical change of the essential amino acids, including the formation of crosslinked amino acids. 13 ) As LAL and OAL are known to have a nephro-toxic effect to rat 14 ,15) or mouse, 16,17) confirmation of the safety of these substances for man is an urgent need.…”

mentioning

confidence: 99%

Gas Chromatography-Mass Spectrometry of Lysinoalanine and the Related Crosslinked Amino Acids in Alkali-treated Food Proteins

Hasegawa

Iwata

1982

Agricultural and Biological Chemistry

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“…A further consideration in the evaluation of the Tetruhymena assay for available lysine, and yet another possible explanation for the higher microbiological assay values for lysine in the heat-damaged fish meals C and G, is that Tetrahymena can utilize lysinoalanine as a source of lysine whereas, in general, higher animals do not have this ability (Sternberg & Kim, 1979).…”

Section: Availability Of Methionine Tryptophan and Lysine As Measurementioning

confidence: 99%

Nutritional availability of methionine, lysine and tryptophan in fish meals, as assessed with biological, microbiological and dye-binding assay procedures

Hewitt¹,

Ford²

1985

Br J Nutr

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1. In vitro assay procedures were applied in the measurement of available amino acids in a selection of fish meals representing good-and poor-quality product. Results were assessed by comparing them with results from chick-growth assays.Available methionine and tryptophan were assayed microbiologically with Streptococcus zymogenes, after predigestion of the test samples with papain or pronase. Results for methionine were correlated with chick-growth assays (r 0.86 for papain, 0.91 for pronase; P < 0.01). Compared with the chick assays, papain tended to give lower, and pronase higher, results. Finer milling of the test samples did not influence the pronase values.Results for available tryptophan were also correlated with chick-growth assays (r 0.95 for papain, 0.96 for pronase; P < 0,001). Compared with the chick values, papain gave markedly lower results and pronase marginally higher ones. Finer milling of the test samples increased the papain values by about 50% but had no effect with pronase. Available lysine was assayed microbiologically with Tetrahymena pyriformis and with a dye-binding procedure (DBL). The results correlated with the chick-growth assays (r 0.99 for DBL, P < 0.001; 0.85 for Tetrahymena, P < 0.01) but both methods overrated the poorer-quality samples.True nitrogen digestibilities and amino acid digestibilities were determined with chickens by the 'ileal analysis' procedure: the amino acid digestibilities were significantly higher and similar to the corresponding availabilities as measured in chick-growth assays.6. Ball milling a poor-quality fish meal caused a marked fall in its N digestibility, whereas similar treatment of a good-quality meal caused a slight increase. An explanation for this finding is proposed. 7.Strep. zymogenes assays following pronase digestion of the test samples gave precise and acceptably accurate measures of the biologically available methionine and tryptophan in the test samples. For available lysine, Tetrahymena and DBL values for the poorer-quality samples were notably higher than the chick-growth assay; possible reasons for this are discussed. The ileal analysis procedure underestimated true N digestibility. 2. 3. 4.5.

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Growth response of mice and Tetrahymena pyriformis to lysinoalanine-supplemented wheat gluten

Cited by 10 publications

References 9 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

Gas Chromatography-Mass Spectrometry of Lysinoalanine and the Related Crosslinked Amino Acids in Alkali-treated Food Proteins

Nutritional availability of methionine, lysine and tryptophan in fish meals, as assessed with biological, microbiological and dye-binding assay procedures

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