D-amino acids in organisms and food

Zagon, Jutta; Dehne, Lutz Ingo; Bögl, K. W.

doi:10.1016/s0271-5317(05)80182-4

Cited by 38 publications

(21 citation statements)

References 48 publications

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“…Relatively high concentrations of these DAAs were also present in widely consumed ripened cheeses [21]. Emmental cheese contains as much as 70 mg of total DAAs per 100 g [103]. The DAA content of varied Table 1.…”

Section: 4mentioning

confidence: 99%

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Friedman

2010

Chemistry & Biodiversity

158

108

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Exposure of food proteins to certain processing conditions induces two major chemical changes: racemization of all L-amino acids (LAAs) to D-amino acids (DAAs) and concurrent formation of cross-linked amino acids such as lysinoalanine (LAL). The diet contains both processing-induced and naturally-formed DAA. The latter include those found in microorganisms, plants, and marine invertebrates. Racemization impairs digestibility and nutritional quality. Racemization of LAA residues to their D-isomers in food and other proteins is pH-, time-, and temperature-dependent. Although racemization rates of LAA residues in a protein vary, relative rates in different proteins are similar. The nutritional utilization of different DAAs varies widely in animals and humans. Some DAAs may exert both adverse and beneficial biological effects. Thus, although D-Phe is utilized as a nutritional source of L-Phe, high concentrations of D-Tyr in such diets inhibit the growth of mice. Both D-Ser and LAL induce histological changes in the rat kidney. The wide variation in the utilization of DAAs is illustrated by the fact that, whereas D-Meth is largely utilized as a nutritional source of the L-isomer, D-Lys is not. Similarly, although L-CysSH has a sparing effect on L-Meth when fed to mice, D-CysSH does not. Since DAAs are consumed as part of their normal diet, a need exists to develop a better understanding of their roles in foods, microbiology, nutrition, and medicine. To contribute to this effort, this overview surveys our present knowledge of the chemistry, nutrition, safety, microbiology, and pharmacology of DAAs. Also covered are the origin and distribution of DAAs in food and possible roles of DAAs in human physiology, aging, and the etiology and therapy of human diseases.

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Section: 4mentioning

confidence: 99%

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Friedman

2010

Chemistry & Biodiversity

158

108

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“…D-Ala is the most prevalent D-amino acid in higher plants (Robinson 1976), is found in high concentrations in certain mollusks (Zagon et al 1994), and is an integral part of the structure of bacterial cell walls (Zagon et al 1994). Thus, plants, animals, and processed food can serve as dietary sources of D-Ala and other DAA.…”

Section: D-alaninementioning

confidence: 99%

“…Like D-Ala, D-Asp is part of peptidoglycan structure of bacterial cell walls (Zagon et al 1994). D-Asp is widespread in marine invertebrates (Zagon et al 1994) and is an endogenous amino acid present in nervous and endocrine tissues in mammals (Furuchi and Homma 2005).…”

Section: D-aspartic Acidmentioning

confidence: 99%

“…During food processing, the L-amino acids may be racemized to their mirror image configuration, the D-isomers Masters and Friedman 1979). D-amino acids (DAA) can also be synthesized by microorganisms (Arlorio et al 2009;Friedman 2010;, marine invertebrates (Zagon et al 1994), and to a very limited extent, other animals (Nagata et al 2006). Racemization of L-amino acid residues to their D-isomers in food and other proteins is pH, time, and temperature dependent.…”

Section: Introductionmentioning

confidence: 99%

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Nutritional and medicinal aspects of d-amino acids

2011

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This paper reviews and interprets a method for determining the nutritional value of D-amino acids, D-peptides, and amino acid derivatives using a growth assay in mice fed a synthetic all-amino acid diet. A large number of experiments were carried out in which a molar equivalent of the test compound replaced a nutritionally essential amino acid such as L-lysine (L-Lys), L-methionine (L-Met), L-phenylalanine (L-Phe), and L-tryptophan (L-Trp) as well as the semi-essential amino acids L-cysteine (L-Cys) and L-tyrosine (L-Tyr). The results show wide-ranging variations in the biological utilization of test substances. The method is generally applicable to the determination of the biological utilization and safety of any amino acid derivative as a potential nutritional source of the corresponding L-amino acid. Because the organism is forced to use the D-amino acid or amino acid derivative as the sole source of the essential or semi-essential amino acid being replaced, and because a free amino acid diet allows better control of composition, the use of all-amino-acid diets for such determinations may be preferable to protein-based diets. Also covered are brief summaries of the widely scattered literature on dietary and pharmacological aspects of 27 individual D-amino acids, D-peptides, and isomeric amino acid derivatives and suggested research needs in each of these areas. The described results provide a valuable record and resource for further progress on the multifaceted aspects of D-amino acids in food and biological samples.

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“…The presence of D-Asp in food was reported by many researchers. D-Asp is contained in common foods (Man and Bada, 1987;Zagon et al, 1994), especially in fermented products such as wine ( Kato et al, 1995), in foods treated under alkaline conditions and heating (Man and Bada, 1987). Vegetables and fruits also contain D-Asp (Brückner and Westhauser, 1994).…”

Section: Application To Bio-samplesmentioning

confidence: 99%

Determination of aspartic acid enantiomers in bio-samples by capillary electrophoresis

Tsunoda¹,

Kato²,

Fukushima³

et al. 1999

Biomed. Chromatogr.

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Enantiomeric separation and detection of D,L‐aspartic acid (Asp) derivatized with 4‐fluoro‐7‐nitro‐2,1,3‐benzoxadiazole (NBD‐F) by capillary electrophoresis (CE) using modified cyclodextrins as chiral selectors was studied. Heptakis(2,3,6‐tri‐O‐methyl)‐β‐cyclodextrin(TM‐β‐CD) was most effective for enantiomeric separation of NBD‐D,L‐Asp with optimum conditions of 30 mM TM‐β‐CD in 50 mM phosphate buffer (pH 4.0) and the limit of detection (LOD) attained was 100 nM for each enantiomer. The method proposed in the present study was convenient for both D‐ and L‐Asp determination since the other amino compounds migrated differently and D‐Asp in bio‐samples such as rat pineal gland and foods was determined with a simple sample pretreatment and a short analysis run time. Copyright © 1999 John Wiley & Sons, Ltd.

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D-amino acids in organisms and food

Cited by 38 publications

References 48 publications

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Nutritional and medicinal aspects of d-amino acids

Determination of aspartic acid enantiomers in bio-samples by capillary electrophoresis

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