Food Science and Biotechnology

, Volume 26, Issue 1, pp 271–277 | Cite as

Key role of peptidoglycan on acrylamide binding by lactic acid bacteria

  • Dan Zhang
  • Wei Liu
  • Liang Li
  • Hong-Yu Zhao
  • Hong-Yang Sun
  • Ming-Han Meng
  • Sheng Zhang
  • Mei-Li Shao


The primary purpose of this study was to analyze the ability of four peptidoglycan (PGN) from different lactic acid bacteria to bind acrylamide (AA) and to identify the binding mechanism. In this study, to clarify the possible binding interactions among AA and components of PGN, chemical components, surface structure, amino acids component, and functional groups of peptidoglycans were studied. It was found that PGN from Lactobacillus plantarum 1.0065 had the highest ability to bind AA with 87%. Furthermore, a significant positive relation was found between the carbohydrate content of PGN and percentage of bind AA, and the content of four specific amino acids of PGN and AA binding ability were also positive correlated. Thereinto, alanine of PGN had a significant impact on AA binding among four amino acids. Additionally, the C–O (carboxyl, polysaccharides, and arene), C=O amide, and N–H amines groups of PGN were involved in AA binding.


acrylamide lactic acid bacteria peptidoglycan component binding 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Baardseth P, Blom H, Skrede G, Mydland LT, Skrede A, Slinde E. Lactic acid fermentation reduces acrylamide formation and other maillard reactions in french fries. Food Chem. Toxicol. 71: 28–33 (2006)Google Scholar
  2. 2.
    Hariri E, Abboud MI, Demirdjian S, Korfali S, Mroueh M, Taleb RI. Carcinogenic and neurotoxic risks of acrylamide and heavy metals from potato and corn chips consumed by the lebanese population. J. Food Compos. Anal. 42: 91–97 (2015)CrossRefGoogle Scholar
  3. 3.
    Oracz J, Nebesny E, yelewicz D. New treds in quantification of acrylamide in food products. Talanta 86: 23–24 (2011)CrossRefGoogle Scholar
  4. 4.
    Anese M, Bortolomeazzi R, Manzocco L, Manzano M, Giusto C, Nicoli MC. Effect of chemical and biological dipping on acrylamide formation and sensory properties in deep-fried potatoes. Food Res. Int. 42: 142–147 (2009)CrossRefGoogle Scholar
  5. 5.
    Hernandez-Mendoza A, Garcia HS, Steele JL. Screening of Lactobacillus casei strains for their ability to bind aflatoxin B1. Food Chem. Toxicol. 47: 1064–1068 (2009)CrossRefGoogle Scholar
  6. 6.
    Corthier G. The health benefits of probiotics. Danone Nutritopics 29: 1–18 (2004)Google Scholar
  7. 7.
    Hernandez-Mendoza A, Guzman-de-pena D, Garcia HS. Key role of teichoic acids on aflatoxin B1 binding by probiotic bacteria. J. Appl. Microbiol. 107: 395–403 (2009)CrossRefGoogle Scholar
  8. 8.
    El-Nezami H, Mikkänen H, Kankäänpää P, Salminen S, Ahokas J. Ability of Lactobacillus and Propionibacterium strains to remove Aflatoxin B1 from the chicken duodenum. J. Food Protect. 63: 549–552 (2000)CrossRefGoogle Scholar
  9. 9.
    Fazeli MR, Hajimohammadali M, Mokshkani A, Samadi N, Jamalifar H, Khoshayand MR. Aflatoxin B1 binding capacity of autochthonous strains of Lactic acid bacteria. J. Food Protect. 72: 189–192 (2009)CrossRefGoogle Scholar
  10. 10.
    Wang L, Yue TL, Yuan YH, Wang ZL, Ye MQ, Cai R. A new insight into the adsorption mechanism of patulin by the heat-inactive Lactic acid bacteria cells. Food Control 50: 104–110 (2015)CrossRefGoogle Scholar
  11. 11.
    Hamidi A, Mirnejad R, Yahaghi E, Behnod V, Mirhosseini A, Amani S, Sattari S, Darian EK. The aflatoxin B1 isolating potential of two Lactic acid bacteria. Asian Pac. J. Trop. Biomed. 3: 732–736 (2013)CrossRefGoogle Scholar
  12. 12.
    Hernandez-Mendoza A, González-Córdova AF, Vallejo-Córdoba B, García HS. Effect of oral supplementation of Lactobacillus reuteri in reduction of intestinal absorption of aflaoxin B1 in rats. J. Basic Microb. 51: 1–6 (2011)CrossRefGoogle Scholar
  13. 13.
    Serrano-Niño JC, Cavazos-Garduño A, Cantú-Cornelio F, González-Córdova AF, Vallejo-Córdoba B, Hernández-Mendoza A, García HS. In vitro r edu ced availability of aflatoxin B1 and acrylamide by bonding interactions with teichoic acids from lactobacillus strains. LWT-Food Sci. Technol. 64: 1334–1341 (2015)CrossRefGoogle Scholar
  14. 14.
    Hwang KT, Lee W, Kim GY, Lee J, Jun W. The binding of aflatoxin B1 modulates the adhesion properties of Lactobacillus casei KCTC 3260 to HT29 colon cancer cell line. Food Sci. Biotechnol. 14: 866–870 (2005)Google Scholar
  15. 15.
    Tripathi P, Beaussart A, Andre G, Rolain T, Lebeer S, Vanderleyden J. Towards a nanoscale view of Lactic acid bacteria. Micron 43: 1323–1330 (2012)CrossRefGoogle Scholar
  16. 16.
    Wu Z, Pan DD, Guo YX, Zeng XQ. Structure and anti-inflammatory capacity of peptidoglycan from Lactobacillus acidophilus in RAW-264.7 cells. Carbohyd. Polym. 96: 466–473 (2013)CrossRefGoogle Scholar
  17. 17.
    Baik JE, Jang YO, Kang SS, Cho K, Yun CH, Han SH. Differential profiles of gastrointestinal proteins interacting with peptidoglycans from Lactobacillus plantarum and Staphylococcus aureus. Mol. Immunol. 65: 77–85 (2015)CrossRefGoogle Scholar
  18. 18.
    Chen KK, Liu C, He Y, Jiang HB, Lu ZQ. A short-type peptidoglycan recognition protein from the silkworm: Expression, characterization and involvement in the prophenoloxidase activation pathway. Dev. Comp. Immunol. 45: 1–9 (2014)CrossRefGoogle Scholar
  19. 19.
    Wu Z, Pan DD, Guo YX, Sun YY, Zeng XQ. Peptidoglycan diversity and antiinflammatory capacity in Lactobacillus strains. Carbohyd. Polym. 128: 130–137 (2015)CrossRefGoogle Scholar
  20. 20.
    Vinderola CG, Bailo N, Reinheimer JA. Survival of probiotic microflora in Argentinian yogurts during refrigerated storage. Food Res. Int. 33: 97–102 (2000)CrossRefGoogle Scholar
  21. 21.
    Vemula H, Ayon NJ, Gutheil WG. Cytoplasmic peptidoglycan intermediate levels in Staphylococcus aureus. Biochimie 121: 72–78 (2016)CrossRefGoogle Scholar
  22. 22.
    Mei MAQ, Elbashir AA, Schmitz OJ. Determination of acrylamide in sudanese food by high performance liquid chromatography coupled with LTQ Qrbitrap mass spectrometry. Food Chem. 176: 342–349 (2015)CrossRefGoogle Scholar
  23. 23.
    Marcotte L, Kegelaer G, Sandt C, Barbeau J, Lafleur M. An alternative infrared spectroscopy assay for the quantification of polysaccharides in bacterial samples. Anal. Biochem. 361: 7–14 (2007)CrossRefGoogle Scholar
  24. 24.
    Hall MB. Efficacy of reducing sugar and phenol-sulfuric acid assays for analysis of soluble carbohydrates in feedstuffs. Anim. Feed Sci. Tech. 185: 94–100 (2013)CrossRefGoogle Scholar
  25. 25.
    Lahtinen SJ, Haskard CA, Ouwehand AC, Salminen SJ, Ahokas JT. Binding of aflatoxin B1 to cell wall components of Lactobacillus rhamnosus strain GG. Food Addit. Contam. 21: 158–164 (2004)CrossRefGoogle Scholar
  26. 26.
    Zoghi A, Khosravi-Darani K, Sohrabvandi S. Surface binding of toxins and heavy metals by probiotics. Mini-Rev. Med. Chem. 14: 84–98 (2014)CrossRefGoogle Scholar
  27. 27.
    Fuchs S, Sontag G, Stidl R, Ehrlich V, Kundi M, Knasmuller S. Detoxification of patulin and ochratoxin A, two abundant mycotoxins, by Lactic acid bacteria. Food Chem. Toxicol. 46: 1398–1407 (2008)CrossRefGoogle Scholar
  28. 28.
    Turbic A, Ahokas JT, Haskard CA. Binding of mutagens to exopolysaccharide produced by Lactobacillus plantarum mutant strain 301102S. J. Dairy Sci. 91: 2960–2966 (2002)Google Scholar
  29. 29.
    Zhao H F, Zhou F, Qi YQ, Piotr D, Bai FL, Piotr W, Zhang BL. Screening of Lactobacillus strains for their ability to bind Benzo(a)pyrene and the mechanism of the process. Food Chem. Toxicol. 59: 67–71 (2013)CrossRefGoogle Scholar
  30. 30.
    Haskard C, Binnion C, Ahokas J. Factors affecting the sequestration of aflaoxin by Lactobacillus rhamnosus strain GG. Chem.-Biol. Interact. 128: 39–49 (2000)CrossRefGoogle Scholar
  31. 31.
    Hatab S, Yue T, Mohamad O. Removal of patulin from apple juice using inactivated Lactic acid bacteria. J. Appl. Microbiol. 112: 892–899 (2012)CrossRefGoogle Scholar
  32. 32.
    Guo C, Yuan Y, Yue T, Hatab S, Wang Z. Binding mechanism of patulin to heattreated yeast cell. Lett. Appl. Microbiol. 55: 453–459 (2012)CrossRefGoogle Scholar
  33. 33.
    Deng Y, Dixon JB, White N, Loeppert RH, Juo ASR. Bonding between polyacrylamide and smectite. Colloid. Surface A 281: 82–91 (2006)CrossRefGoogle Scholar
  34. 34.
    Koutsidis G, Simons SPJ, Thong YH, Haldoupis Y, Mojica-Lazaro J, Wedzicha BL, Mottram DS. Investigations on the effect of amino acids on acrylamide, pyrazines, and Michael addition products in model systems. J. Agr. Food Chem. 57: 9011–9015 (2009)CrossRefGoogle Scholar
  35. 35.
    Niderkorn V, Morgavi D, Aboab B, Lemaire M, Boudra H. Cell wall component and mycotoxin moieties involved in the binding of fumonisin B1 and B2 by Lactic acid bacteria. J. Appl. Microbiol. 106: 977–985 (2009)CrossRefGoogle Scholar
  36. 36.
    Zamora R, Delgado RM, Hidalgo FJ. Model reactions of acrylamide with selected amino compounds. J. Agr. Food Chem. 58: 1708–1713 (2010)CrossRefGoogle Scholar

Copyright information

© The Korean Society of Food Science and Technology and Springer Science+Business Media Dordrecht 2017

Authors and Affiliations

  • Dan Zhang
    • 1
  • Wei Liu
    • 2
  • Liang Li
    • 1
  • Hong-Yu Zhao
    • 1
  • Hong-Yang Sun
    • 1
  • Ming-Han Meng
    • 1
  • Sheng Zhang
    • 1
  • Mei-Li Shao
    • 1
  1. 1.College of Food ScienceNortheast Agricultural UniversityHarbin, HeilongjiangChina
  2. 2.Tongjiang entry-exit inspection and Quarantine BureauTongjiang, HeilongjiangChina

Personalised recommendations