Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein

Dragana Stanic, Evanthia Monogioudi, Dilek Ercili Cura, Jelena Radosavljevic, Marina Atanaskovic-Markovic, Olga Vuckovic, Raija Lantto, Maija-Liisa Mattinen, Johanna Buchert, Tanja Cirkovic Velickovic (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of β‐casein (CN). β‐CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to β‐CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS‐PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the β‐CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of β‐CN.
Original languageEnglish
Pages (from-to)1273-1284
Number of pages8
JournalMolecular Nutrition and Food Research
Volume54
Issue number9
DOIs
Publication statusPublished - 2010
MoE publication typeA1 Journal article-refereed

Fingerprint

allergenicity
Caseins
caffeic acid
casein
digestibility
Monophenol Monooxygenase
catechol oxidase
Laccase
Immunoglobulin E
laccase
Digestion
basophils
Basophils
Agaricales
digestion
assays
crosslinking
mushrooms
Enzyme-Linked Immunosorbent Assay
milk allergy

Keywords

  • Allergen
  • bioprocessing
  • casein
  • crosslinking enzymes
  • digestibility

Cite this

Stanic, D., Monogioudi, E., Ercili Cura, D., Radosavljevic, J., Atanaskovic-Markovic, M., Vuckovic, O., ... Cirkovic Velickovic, T. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein. Molecular Nutrition and Food Research, 54(9), 1273-1284. https://doi.org/10.1002/mnfr.200900184
Stanic, Dragana ; Monogioudi, Evanthia ; Ercili Cura, Dilek ; Radosavljevic, Jelena ; Atanaskovic-Markovic, Marina ; Vuckovic, Olga ; Lantto, Raija ; Mattinen, Maija-Liisa ; Buchert, Johanna ; Cirkovic Velickovic, Tanja. / Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein. In: Molecular Nutrition and Food Research. 2010 ; Vol. 54, No. 9. pp. 1273-1284.
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abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of β‐casein (CN). β‐CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to β‐CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS‐PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the β‐CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of β‐CN.",
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author = "Dragana Stanic and Evanthia Monogioudi and {Ercili Cura}, Dilek and Jelena Radosavljevic and Marina Atanaskovic-Markovic and Olga Vuckovic and Raija Lantto and Maija-Liisa Mattinen and Johanna Buchert and {Cirkovic Velickovic}, Tanja",
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Stanic, D, Monogioudi, E, Ercili Cura, D, Radosavljevic, J, Atanaskovic-Markovic, M, Vuckovic, O, Lantto, R, Mattinen, M-L, Buchert, J & Cirkovic Velickovic, T 2010, 'Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein', Molecular Nutrition and Food Research, vol. 54, no. 9, pp. 1273-1284. https://doi.org/10.1002/mnfr.200900184

Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein. / Stanic, Dragana; Monogioudi, Evanthia; Ercili Cura, Dilek; Radosavljevic, Jelena; Atanaskovic-Markovic, Marina; Vuckovic, Olga; Lantto, Raija; Mattinen, Maija-Liisa; Buchert, Johanna; Cirkovic Velickovic, Tanja (Corresponding Author).

In: Molecular Nutrition and Food Research, Vol. 54, No. 9, 2010, p. 1273-1284.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Digestibility and allergenicity assessment of enzymatically crosslinked β‐casein

AU - Stanic, Dragana

AU - Monogioudi, Evanthia

AU - Ercili Cura, Dilek

AU - Radosavljevic, Jelena

AU - Atanaskovic-Markovic, Marina

AU - Vuckovic, Olga

AU - Lantto, Raija

AU - Mattinen, Maija-Liisa

AU - Buchert, Johanna

AU - Cirkovic Velickovic, Tanja

PY - 2010

Y1 - 2010

N2 - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of β‐casein (CN). β‐CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to β‐CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS‐PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the β‐CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of β‐CN.

AB - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of β‐casein (CN). β‐CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to β‐CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS‐PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the β‐CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of β‐CN.

KW - Allergen

KW - bioprocessing

KW - casein

KW - crosslinking enzymes

KW - digestibility

U2 - 10.1002/mnfr.200900184

DO - 10.1002/mnfr.200900184

M3 - Article

VL - 54

SP - 1273

EP - 1284

JO - Molecular Nutrition and Food Research

JF - Molecular Nutrition and Food Research

SN - 1613-4125

IS - 9

ER -