In vitro digestibility of β-casein and β-lactoglobulin under simulated human gastric and duodenal conditions: A multi-laboratory evaluation

G. Mandalari, K. Adel-Patient, V. Barkholt, C. Baro, L. Bennett, M. Bublin, S. Gaier, G. Graser, G. S. Ladics, D. Mierzejewska, E. Vassilopoulou, Y. M. Vissers, L. Zuidmeer, N. M. Rigby, L. J. Salt, M. Defernez, F. Mulholland, A. R. Mackie, M. S J Wickham, E. N C Mills

Research output: Contribution to journalArticlepeer-review

Abstract

Initially the resistance to digestion of two cow's milk allergens, β-casein, and β-lactoglobulin (β-Lg), was compared using a "high-protease assay" and a "low-protease assay" in a single laboratory. The low-protease assay represents an alternative standardised protocol mimicking conditions found in the gastrointestinal tract. For the high-protease assay, both proteins were incubated with either pepsin or pancreatin and digestion monitored by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse phase-high performance liquid chromatography. The low-protease assay involved gastroduodenal digestion in the presence or absence of phosphatidylcholine (PC). Both β-casein and β-Lg were susceptible to hydrolysis by pepsin and pancreatin in the high-protease assay. In contrast, the kinetics of β-casein digestion in the low-protease assay were slower, β-Lg being pepsin resistant. During duodenal digestion, β-Lg was gradually degraded and addition of PC slowed digestion. Subsequently, the reproducibility of the low-protease assay was assessed in 12 independent laboratories by visual assessment of the gels and densitometric analysis: the inter- and intra-laboratory variability was affected by sampling and electrophoresis method employed. The low-protease assay was shown to be reproducible. Future studies will extend these findings using a broader panel of proteins.

Original languageEnglish
Pages (from-to)372-381
Number of pages10
JournalRegulatory Toxicology and Pharmacology
Volume55
Issue number3
DOIs
Publication statusPublished - Dec 2009

Keywords

  • β-Casein
  • β-Lactoglobulin
  • Allergy
  • In vitro digestion
  • Physiological protocol

Fingerprint

Dive into the research topics of 'In vitro digestibility of β-casein and β-lactoglobulin under simulated human gastric and duodenal conditions: A multi-laboratory evaluation'. Together they form a unique fingerprint.

Cite this