Skip to main content

d-Amino Acids in Fermentative Foods

  • Chapter
  • First Online:
D-Amino Acids

Abstract

In recent years, d-amino acids have been shown to be present, in a free or bound state, in a wide variety of foods and beverages, and to exhibit properties that differ from those of l-isomers. It is anticipated that as more is learned about the properties of d-amino acids in foods, they will be applied for the improvement of food characteristics. In this section, we will summarize what is known about the distribution and metabolism of d-amino acids in foods and beverages, especially fermented types, as well as what is known about the enzymes involved in the metabolism of d-amino acids. In addition, applications in which d-amino acids are being used to improve the characteristics of food are described.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Abe H, Park JN, Fukumoto Y, Fujita E, Tanaka T, Washio T, Otsuka S, Shimizu T, Watanabe K (1999) Occurrence of d-amino acids in fish sauces and other fermented fish products. Fish Sci 65:637–641

    CAS  Google Scholar 

  • Brückner H, Hausch M (1989) Gas chromatographic detection of d-amino acids as common constituents of fermented foods. Chromatographia 28:487–492

    Article  Google Scholar 

  • Brückner H, Westhauser T (2003) Chromatographic determination of l- and d-amino acids in plants. Amino Acids 24:43–55

    Article  PubMed  Google Scholar 

  • Eliot AC, Kirsch JF (2004) Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu Rev Biochem 73:383–415

    Article  CAS  PubMed  Google Scholar 

  • Erbe T, Brückner H (2000) Chromatographic determination of amino acid enantiomers in beers and raw materials used for their manufacture. J Chromatogr A 881:81–91

    Article  CAS  PubMed  Google Scholar 

  • Gogami Y, Ito K, Kamitani Y, Matsushima Y, Oikawa T (2009) Occurrence of d-serine in rice and characterization of rice serine racemase. Phytochemistry 70:380–387

    Article  CAS  PubMed  Google Scholar 

  • Gogami Y, Okada K, Oikawa T (2011) High-performance liquid chromatography analysis of naturally occurring d-amino acids in sake. J Chromatogr B 879:3259–3267

    Article  CAS  Google Scholar 

  • Kato S, Ishihara T, Hemmi H, Kobayashi H, Yoshimura T (2011) Alternations in d-amino acid concentrations and microbial community structures during the fermentation of red and white wines. J Biosci Bioeng 111:104–108

    Article  CAS  PubMed  Google Scholar 

  • Kato S, Hemmi H, Yoshimura T (2012) Lysine racemase from a lactic acid bacterium, Oenococcus oeni: structural basis of substrate specificity. J Biochem 152:505–508

    Article  CAS  PubMed  Google Scholar 

  • Kawai M, Sekine-Hayakawa Y, Okiyama A, Ninomiya Y (2012) Gustatory sensation of (l)- and (d)-amino acids in humans. Amino Acids 43:2349–2358

    Article  CAS  PubMed  Google Scholar 

  • Lam H, Oh DC, Cava F, Takacs CN, Clardy J, de Pedro MA, Wandor MK (2009) d-Amino acids govern stationary phase cell wall remodeling in bacteria. Science 325:1552–1555

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Lee SG, Hong SP, Song JJ, Kim SJ, Kwak MS, Sung MH (2006) Functional and structural characterization of thermostable d-amino acid aminotransferases from Geobacillus spp. Appl Environ Microbiol 72:1588–1594

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Lim YH, Yokoigawa K, Esaki N, Soda K (1993) A new amino acid racemase with threonine α-epimerase activity from Pseudomonas putida: purification and characterization. J Bacteriol 175:4213–4217

    CAS  PubMed  PubMed Central  Google Scholar 

  • Liu JL, Liu XQ, Shi YW (2012) Expression, purification, and characterization of alanine racemase from Pseudomonas putida YZ-26. World J Microbiol Biotechnol 28:267–274

    Article  CAS  PubMed  Google Scholar 

  • Matsui D, Oikawa T, Arakawa N, Osumi S, Lausberg F, Stäbler N, Freudl R, Eggeling L (2009) A periplasmic, pyridoxal-5′-phosphate-dependent amino acid racemase in Pseudomonas taetrolens. Appl Microbiol Biotechnol 83:1045–1054

    Article  CAS  PubMed  Google Scholar 

  • Mills DA, Rawsthorne H, Parker C, Tamir D, Makarova K (2005) Genomic analysis of Oenococcus oeni PSU-1 and its relevance to winemaking. FEMS Microbiol Rev 29:465–475

    CAS  PubMed  Google Scholar 

  • Mutaguchi Y, Ohmori T, Akano H, Doi K, Ohshima T (2013a) Distribution of d-amino acids in vinegars and involvement of lactic acid bacteria in the production of d-amino acids. Springer Plus 2:691

    Article  PubMed  PubMed Central  Google Scholar 

  • Mutaguchi Y, Ohmori T, Wakamatsu T, Doi K, Ohshima T (2013b) Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species. J Bacteriol 195:5207–5215

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Oikawa T (2014) Bioindustry 31:33–40 (in Japanese)

    CAS  Google Scholar 

  • Okazaki S, Suzuki A, Mizushima T, Kawano T, Komeda H, Asano Y, Yamane T (2009) The novel structure of a pyridoxal 5′-phosphate-dependent fold-type I racemase, α-amino-ε-caprolactam racemase from Achromobacter obae. Biochemistry 48:941–950

    Article  CAS  PubMed  Google Scholar 

  • Palani K, Burley SK, Swaminathan S (2013) Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5′-phosphate. Acta Crystallogr Sect F: Struct Biol Cryst Commun 69:15–19

    Article  CAS  Google Scholar 

  • Rubio-Barroso S, Santos-Delgadoa MJ, Martín-Olivara C, Polo-Díeza LM (2006) Indirect chiral HPLC determination and fluorimetric detection of d-amino acids in milk and oyster samples. J Dairy Sci 89:82–89

    Article  CAS  PubMed  Google Scholar 

  • Satomura T, Kawakami R, Sakuraba H, Ohshima T (2002) Dye-linked d-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J Biol Chem 277:12861–12867

    Article  CAS  PubMed  Google Scholar 

  • Satomura T, Ishikura M, Koyanagi T, Sakuraba H, Ohshima T, Suye S (2015) Dye-linked d-amino acid dehydrogenase from the thermophilic bacterium Rhodothermus marinus JCM9785: characteristics and role in trans-4-hydroxy-l-proline catabolism. Appl Microbiol Biotechnol 99:4265–4275

    Article  CAS  PubMed  Google Scholar 

  • Solms J, Vuataz L, Egli RH (1965) The taste of l- and d-amino acids. Experientia 21:692–694

    Article  CAS  PubMed  Google Scholar 

  • Takahashi S, Furukawara M, Omae K, Tadokoro N, Saito Y, Abe K, Kera Y (2014) A highly stable d-amino acid oxidase of the thermophilic bacterium Rubrobacter xylanophilus. Appl Environ Microbiol 80:7219–7229

    Article  PubMed  PubMed Central  Google Scholar 

  • Tanizawa K, Asano S, Masu Y, Kuramitsu S, Kagamiyama H, Tanaka H, Soda K (1989) The primary structure of thermostable d-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with l-amino acid aminotransferases. J Biol Chem 264:2450–2454

    CAS  PubMed  Google Scholar 

  • Yonaha K, Misono H, Yamamoto T, Soda K (1975) d-Amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties. J Biol Chem 250:6983–6989

    CAS  PubMed  Google Scholar 

  • Yorifuji T, Ogata K, Soda K (1971) Arginine racemase of Pseudomonas graveolens. I. Purification, crystallization, and properties. J Biol Chem 246:5085–5092

    CAS  PubMed  Google Scholar 

  • Yoshimura T, Esaki N (2003) Amino acid racemases: functions and mechanisms. J Biosci Bioeng 96:103–109

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Toshihisa Ohshima .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2016 Springer Japan

About this chapter

Cite this chapter

Mutaguchi, Y., Kobayashi, J., Oikawa, T., Ohshima, T. (2016). d-Amino Acids in Fermentative Foods. In: Yoshimura, T., Nishikawa, T., Homma, H. (eds) D-Amino Acids. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56077-7_22

Download citation

Publish with us

Policies and ethics