Advertisement

European Food Research and Technology

, Volume 236, Issue 3, pp 567–571 | Cite as

Enzymatic control of the acrylamide level in coffee

  • Minseok ChaEmail author
Original Paper

Abstract

The goal of this work was to show the possibility of removing acrylamide from real foods using bacterial enzymes at relatively high temperatures. Cell-free extracts from Ralstonia eutropha AUM-01 isolated from soil collected from leaf litter on Picnic Point on the UW-Madison campus and a thermophilic strain, Geobacillus thermoglucosidasius AUT-01 isolated from soil collected from hot spring area in Montana, were used to remove acrylamide from coffee. Coffee was chosen because ~39 % of the acrylamide that people consumed is from coffee. Cell extracts containing acrylamide-degrading enzymes, which hydrolyze acrylamide to acrylic acid, were directly applied to coffee. Although acrylamide was not totally degraded at higher concentrations of coffee in water, it was totally disappeared in 100 mg coffee/10 mL ddH20, which ordinary people drink. This is the first approach for applying bacterial enzymes to real food for the removal of acrylamide.

Keywords

Acrylamide Ralstonia spp. Geobacillus spp. Instant coffee 

References

  1. 1.
    Abramsson-Zetterberg L (2003) The dose-reponse relationship at very low doses of acrylamide linear in the flow cytometer-based muse micronucleus assay. Mutat Res 535:215–222CrossRefGoogle Scholar
  2. 2.
    Cha M, Chambliss GH (2011) Characterization of Acrylamidase Isolated from a Newly Isolated Acrylamide-Utilizing Bacterium, Ralstonia eutropha AUM-01. Curr Microbiol 62:671–678CrossRefGoogle Scholar
  3. 3.
    Cha M, Chambliss GH (2012) Cloning and sequence analysis of the heat-stable acrylamidase from a newly isolated thermophilic bacterium, Geobacillus thermoglucosidasius AUT-01. Biodegradation. doi: 10.1007/s10532-012-9557-6 Google Scholar
  4. 4.
    Cheong TK, Oriel PJ (2000) Cloning of a wide-spectrum amidase from Bacillus stearothermophilus BR388 in Eschericia coli and marked enhancement of amidase expressing using directed evolution. Enzy Micro Technol 26:152–158CrossRefGoogle Scholar
  5. 5.
    Cherry AB, Gabaccia AF, Senn HW (1956) The assimilation behavior of certain toxic organic compounds in natural waters. Sewage Ind Waters 28:1137Google Scholar
  6. 6.
    Hogervorst JG, Schouten LJ, Konings EJ, Goldbohm RA, van den Brandt PA (2007) A prospective study of dietary acrylamide intake and the risk of endometrial, ovarian, and breast cancer. Cancer Epidemiol Biomarkers Prev 16:2304–2313CrossRefGoogle Scholar
  7. 7.
    Kimura T (1959) Studies on metabolism of amides in Mycobacteriaceae. J Biochem 46:973–978Google Scholar
  8. 8.
    Kobayashi M, Komeda H, Nagasawa T, Nishiyama M, Horinouchi S, Beppu T, Yamada H, Shimizu S (1993) Amidase coupled with low molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1. Euro J Biochem 217:327–336CrossRefGoogle Scholar
  9. 9.
    Lande SS, Bosch SJ, Howard PH (1979) Degradation and leaching of acrylamide in soil. J Environ Qual 8:133–137CrossRefGoogle Scholar
  10. 10.
    Mottram DS, Wedzicha BL, Dodson AT (2002) Acrylamide is formed in the Maillard reaction. Nature 419:448–449CrossRefGoogle Scholar
  11. 11.
    Nawaz MS, Franklin W, Campbell WL, Heinze TM, Cerniglia CE (1991) Metabolism of acrylonitrile by Klebsiella pneumoniae. Arch Microbiol 156:231–238CrossRefGoogle Scholar
  12. 12.
    Nawaz MS, Franklin W, Cerniglia CE (1992) Degradation of acrylamide by immobilized cells of a Pseudomonas sp. and Xanthomonas maltophilia. Can J Microbiol 39:207–212CrossRefGoogle Scholar
  13. 13.
    Nawaz MS, Khan AA, Seng JE, Leakey JE, Siitomen PH, Cerniglia CE (1994) Purification and characterization of an amidase from an acrylamide-degrading Rhodococcus sp. Appl Environ Microbiol 60:3343–3348Google Scholar
  14. 14.
    Pertsovich S, Guranda D, Podchernyaev D, Yanenko A, Svedas V (2005) Aliphatic amidase from Rhodococcus rhodochrous M8 is related to the nitrilase/cyanide hydratase family. Biochemistry (Moscow) 70:1280–1287CrossRefGoogle Scholar
  15. 15.
    Segerbäck D, Calleman CJ, Schreoder JL, Costa LG, Faustman EM (1995) Formation of N-7-(2-carbamoyl-2-hydroxyethyl)guanine in DNA of the mouse and the rat following intraperitoneal administration of [14C]acrylamide. Carcinogenesis 16:1161–1165CrossRefGoogle Scholar
  16. 16.
    Svensson K, Abramsson L, Becker W, Glynn A, Hellenäs K, Lind Y, Rosen J (2003) Dietary intake of acrylamide in Sweden. Food Chem Tox 41:1581–1586CrossRefGoogle Scholar
  17. 17.
    Skouloubris S, Labigne A, De Reuse H (1997) Identification and characterization of an aliphatic amidase in Helicobacter pylori. Mol Microbiol 25:989–998CrossRefGoogle Scholar
  18. 18.
    Stadler RH, Blank I, Varga N, Robert F, Hau J, Guy PA, Robert M, Riediker S (2002) Acrylamide from Maillard reaction products. Nature 419:449–450CrossRefGoogle Scholar
  19. 19.
    Taeymans D, Wood J, Ashby P (2004) A review of acrylamide: an industry perspective on research, analysis, formation, and control. Crit Rev Food Sci Nutr 44:323–347CrossRefGoogle Scholar
  20. 20.
    Tareke E, Rydberg P, Karlsson P, Eriksson S, Tornqvist M (2000) Acrylamide: a cooking carcinogen? Chem Res Toxicol 13:517–522CrossRefGoogle Scholar
  21. 21.
    Tareke E, Rydberg P, Eriksson S, Tornqvist M (2002) Analysis of acrylamide, a carcinogen formed in heated foodstuffs. J Agric Food Chem 50:4998–5006CrossRefGoogle Scholar
  22. 22.
    White JM, Jones DD, Huang D, Gauthier JJ (1988) Conversion cyanide to formate and ammonia by pseudomonad obtained from industrial wastewater. J Ind Microbiol 3:263–272CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  1. 1.Department of BacteriologyUniversity of Wisconsin-MadisonMadisonUSA
  2. 2.Department of Food ScienceUniversity of Wisconsin-MadisonMadisonUSA
  3. 3.Department of GeneticsUniversity of GeorgiaAthensUSA

Personalised recommendations