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In Vitro Infant Digestion of Whey Protein–Dextran Glycates

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Food Digestion

Abstract

Whey protein–dextran glycates (WD) made from whey protein isolate (WPI) and dextran (DX) of two different molecular masses (10 and 150 kDa) were subjected to an in vitro infant digestion model. The model included physiologically relevant concentrations of porcine gastrointestinal enzymes, as well as phosphatidylcholine and bile salts. Native α-lactalbumin and bovine serum albumin were rapidly digested during the gastric phase, whereas 93 % of β-lactoglobulin (BLG) passed unaltered into the duodenal phase and was completely digested by pancreatin within 150 min. DX-glycated whey protein (WD10; WD150) also survived gastric digestion intact, but was digested by pancreatin. However, after 180 min of duodenal digestion, some glycate and free BLG remained. Titers of free BLG in the duodenal phase were 10-fold higher for WPI compared to the glycates. Duodenal digestion kinetics of the BLG present in WPI, as well as of the free BLG present in WD10 and WD150 followed first-order kinetics. Digestion rate constants (k) were 0.019, 0.010, and 0.012 min−1, for k WPI, k WD10, and k WD150, respectively. Lower rate constants were observed for BLG digestion in glycates as compared to WPI. In conclusion, BLG was digested in glycates, but its digestion was slower in the glycate form. Avoiding high titers of BLG in the duodenum, as well as successful masking of immunogenic peptides by DX, could help in the development of hypoallergenic foods. This work contributes to an understanding of how protein–polysaccharide glycates impact protein digestion in infants.

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References

  1. Abd El-Salam MH, El-Shibiny S (2013) Bioactive peptides of buffalo, camel, goat, sheep, mare, and yak milks and milk products. Food Rev Int 29(1):1–23

    Article  CAS  Google Scholar 

  2. Akhtar M, Dickinson E (2007) Whey protein–maltodextrin conjugates as emulsifying agents: an alternative to gum Arabic. Food Hydrocolloids 21(4):607–616

    Article  CAS  Google Scholar 

  3. Almaas H, Cases AL, Devold TG, Holm H, Langsrud T, Aabakken L, Aadnoey T, Vegarud GE (2006) In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes. Int Dairy J 16(9):961–968

    Article  CAS  Google Scholar 

  4. Arita K, Babiker EE, Azakami H, Kato A (2001) Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE. J Agric Food Chem 49(4):2030–2036

    Article  CAS  Google Scholar 

  5. Bund T, Allelein S, Arunkumar A, Lucey JA, Etzel MR (2012) Chromatographic purification and characterization of whey protein–dextran glycation products. J Chromatogr A 1244:98–105

    Article  CAS  Google Scholar 

  6. Castillo G, Sanz MA, Serrano MA, Hernandez A (2002) Influence of protein source, type, and concentration, and product form on the protein quality of commercial enteral formulas. J Food Sci 67(1):328–334

    Article  CAS  Google Scholar 

  7. Corzo-Martinez M, Soria AC, Belloque J, Villamiel M, Moreno FJ (2010) Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine beta-lactoglobulin. Int Dairy J 20(11):742–752

    Article  CAS  Google Scholar 

  8. Crittenden RG, Bennett LE (2005) Cow's milk allergy: a complex disorder. J Am Coll Nutr 24(6 Suppl):582S–591S

    Article  CAS  Google Scholar 

  9. Damodaran S, Parkin KL, Fennema OR (2008) Fennema's food chemistry. CRC/Taylor & Francis, Boca Raton

    Google Scholar 

  10. Deat E, Blanquet-Diot S, Jarrige JF, Denis S, Beyssac E, Alric M (2009) Combining the dynamic TNO-gastrointestinal tract system with a Caco-2 cell culture model: application to the assessment of lycopene and alpha-tocopherol bioavailability from a whole food. J Agric Food Chem 57(23):11314–11320

    Article  CAS  Google Scholar 

  11. Dickinson PA, Abu Rmaileh R, Ashworth L, Barker RA, Burke WM, Patterson CM, Stainforth N, Yasin M (2012) An investigation into the utility of a multi-compartmental, dynamic, system of the upper gastrointestinal tract to support formulation development and establish bioequivalence of poorly soluble drugs. AAPS J 14(2):196–205

    Article  CAS  Google Scholar 

  12. Dupont D, Mandalari G, Molle D, Jardin J, Leonil J, Faulks RM, Wickham MSJ, Mills ENC, Mackie AR (2010) Comparative resistance of food proteins to adult and infant in vitro digestion models. Mol Nutr Food Res 54(6):767–780

    Article  CAS  Google Scholar 

  13. Dupont D, Mandalari G, Molle D, Jardin J, Rolet-Repecaud O, Duboz G, Leonil J, Mills CEN, Mackie AR (2010b) Food processing increases casein resistance to simulated infant digestion. Mol Nutr Food Res 54(11):1677–1689

  14. Hong S-T, Ha Y-M, Nam M-H, Lee K-W (2012) Improvement of bioactivity of alpha-lactalbumin through Maillard reaction with dextran. FASEB J 26(1_MeetingAbstracts):625–627

    Google Scholar 

  15. Host A (2002) Frequency of cow's milk allergy in childhood. Ann Allergy Asthma Immunol 89(6):33–37

    Article  Google Scholar 

  16. Inglingstad RA, Devold TG, Eriksen EK, Holm H, Jacobsen M, Liland KH, Rukke EO, Vegarud GE (2010) Comparison of the digestion of caseins and whey proteins in equine, bovine, caprine and human milks by human gastrointestinal enzymes. Dairy Sci Technol 90(5):549–563

    Article  CAS  Google Scholar 

  17. Jakobsson I, Lindberg T, Benediktsson B (1982) In vitro digestion of cowʼs milk proteins by duodenal juice from infants with various gastrointestinal disorders. J Pediatr Gastroenterol Nutr 1(2):183–192

    Article  CAS  Google Scholar 

  18. Jimenez-Castano L, Villamiel M, Lopez-Fandino R (2007) Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocolloids 21(3):433–443

    Article  CAS  Google Scholar 

  19. Jimenez-Saiz R, Belloque J, Molina E, Lopez-Fandino R (2011) Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. J Agric Food Chem 59(18):10044–10051

    Article  CAS  Google Scholar 

  20. Kindt TJ, Goldsby RA, Osborne BA, Kuby J (2007) Kuby immunology. W.H. Freeman, New York

    Google Scholar 

  21. Kobayashi K, Hirano A, Ohta A, Yoshida T, Takahashi K, Hattori M (2001) Reduced immunogenicity of beta-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J Agric Food Chem 49(2):823–831

    Article  CAS  Google Scholar 

  22. Kopf-Bolanz KA, Schwander F, Gijs M, Vergeres G, Portmann R, Egger L (2012) Validation of an in vitro figestive system for studying macronutrient decomposition in humans. J Nutr 142(2):245–250

    Article  CAS  Google Scholar 

  23. Lesmes U, McClements DJ (2012) Controlling lipid digestibility: response of lipid droplets coated by beta-lactoglobulin-dextran Maillard conjugates to simulated gastrointestinal conditions. Food Hydrocolloids 26(1):221–230

    Article  CAS  Google Scholar 

  24. Li Z, Luo YK, Feng LG (2011) Effects of Maillard reaction conditions on the antigenicity of alpha-lactalbumin and beta-lactoglobulin in whey protein conjugated with maltose. Eur Food Res Technol 233(3):387–394

    Article  CAS  Google Scholar 

  25. Macfarlane GT, Macfarlane S, Gibson GR (1998) Validation of a three-stage compound continuous culture system for investigating the effect of retention time on the ecology and metabolism of bacteria in the human colon. Microb Ecol 35(2):180–187

    Article  CAS  Google Scholar 

  26. Macierzanka A, Sancho AI, Mills ENC, Rigby NM, Mackie AR (2009) Emulsification alters simulated gastrointestinal proteolysis of beta-casein and beta-lactoglobulin. Soft Matter 5(3):538–550

    Article  CAS  Google Scholar 

  27. Mandalari G, Adel-Patient K, Barkholt V, Baro C, Bennett L, Bublin M, Gaier S, Graser G, Ladics GS, Mierzejewska D, Vassilopoulou E, Vissers YM, Zuidmeer L, Rigby NM, Salt LJ, Defernez M, Mulholland F, Mackie AR, Wickham MSJ, Mills ENC (2009) In vitro digestibility of beta-casein and beta-lactoglobulin under simulated human gastric and duodenal conditions: a multi-laboratory evaluation. Regul Toxicol Pharmacol 55(3):372–381

    Article  CAS  Google Scholar 

  28. Mandalari G, Mackie AM, Rigby NM, Wickham MSJ, Mills ENC (2009) Physiological phosphatidylcholine protects bovine beta-lactoglobulin from simulated gastrointestinal proteolysis. Mol Nutr Food Res 53:S131–S139

    Article  Google Scholar 

  29. Moreno FJ, Mackie AR, Mills ENC (2005) Phospholipid interactions protect the milk allergen alpha-lactalbumin from proteolysis during in vitro digestion. J Agric Food Chem 53(25):9810–9816

    Article  CAS  Google Scholar 

  30. Nodake Y, Fukumoto S, Fukasawa M, Sakakibara R, Yamasaki N (2010) Reduction of the immunogenicity of beta-lactoglobulin from cow's milk by conjugation with a dextran derivative. Biosci Biotechnol Biochem 74(4):721–726

    Article  CAS  Google Scholar 

  31. Oliver CM, Melton LD, Stanley RA (2006) Creating proteins with novel functionality via the Maillard reaction: a review. Crit Rev Food Sci Nutr 46(4):337–350

    Article  CAS  Google Scholar 

  32. Purama RK, Goswami P, Khan AT, Goyal A (2009) Structural analysis and properties of dextran produced by Leuconostoc mesenteroides NRRL B-640. Carbohydr Polym 76(1):30–35

    Article  CAS  Google Scholar 

  33. Simonsen L, Hovgaard L, Mortensen PB, Brondsted H (1995) Dextran hydrogels for colon-specific drug delivery.5. Degradation in human intestinal incubation models. Eur J Pharm Sci 3(6):329–337

    Article  CAS  Google Scholar 

  34. Varshosaz J (2012) Dextran conjugates in drug delivery. Expert Opin Drug Deliv 9(5):509–523

    Article  CAS  Google Scholar 

  35. Walthall K, Cappon GD, Hurtt ME, Zoetis T (2005) Postnatal development of the gastrointestinal system: a species comparison. Birth Defects Res Part B-Dev Reprod Toxicol 74(2):132–156

    Article  CAS  Google Scholar 

  36. Wang Q, Ismail B (2012) Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey protein. Int Dairy J 25(2):112–122

    Article  Google Scholar 

  37. Weiner HL, da Cunha AP, Quintana F, Wu H (2011) Oral tolerance. Immunol Rev 241(1):241–259

    Article  CAS  Google Scholar 

  38. Zhu D, Damodaran S, Lucey JA (2008) Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions. J Agric Food Chem 56(16):7113–7118

    Article  CAS  Google Scholar 

  39. Zhu D, Damodaran S, Lucey JA (2010) Physicochemical and emulsifying properties of whey protein isolate (WPI)–dextran conjugates produced in aqueous solution. J Agric Food Chem 58(5):2988–2994

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This project was funded by the National Institute of Food and Agriculture of the US Department of Agriculture (award number 2011-67017-20097). We would like to express our sincere thanks to Prof. Dr. Adam Macierzanka from the Institute of Food Research (Norwich, UK) and INRA STLO—Agrocampus Ouest, UMR (Rennes, France) for his valuable advice on the use of physiological surfactants and elongation of the simulated duodenal phase. We would also like to thank Prof. Dr. Srinivasan Damodaran from UW-Madison for his valuable input and graduate student support.

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Authors and Affiliations

  1. Department of Food Science, University of Wisconsin–Madison, Madison, WI, 53706, USA

    Franziska H. Böttger, Mark R. Etzel & John A. Lucey

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  1. Franziska H. Böttger
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  2. Mark R. Etzel
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  3. John A. Lucey
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Correspondence to Franziska H. Böttger.

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Böttger, F.H., Etzel, M.R. & Lucey, J.A. In Vitro Infant Digestion of Whey Protein–Dextran Glycates. Food Dig. 4, 76–84 (2013). https://doi.org/10.1007/s13228-013-0032-6

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  • DOI: https://doi.org/10.1007/s13228-013-0032-6

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