| Autor: |
Mandalari, G. Adel-Patient, K. Barkholt, V. Baro, C. Bennett, L. Bublin, M. Gaier, S. Graser, G. Ladics, G.S. Mierzejewska, D. Vassilopoulou, E. Vissers, Y.M. Zuidmeer, L. Rigby, N.M. Salt, L.J. Defernez, M. Mulholland, F. Mackie, A.R. Wickham, M.S.J. Mills, E.N.C. |
| Jazyk: |
angličtina |
| Rok vydání: |
2009 |
| Popis: |
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. © 2009 Elsevier Inc. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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