Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 63, Issue 27, Pages 6157-6171Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.5b02384
Keywords
MALDI-TOF-MS; protein profiling; peptide profiling; milk analysis; speciation; thermal treatment
Funding
- Italian Ministry of Economy and Finance [191/2009]
- Regione Campania for the Project QUARC - Qualita delle produzioni tipiche campane ed il suo territorio: approcci innovativi ed integrati per rafforzare la competitivita del sistema Agroalimentare, bando CAMPUS [A.G.C.6 - settore 1]
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Adulteration of ovine, caprine, and buffalo milks with more common bovine material occurs for eeonomic reasons and seasonal availability. Frauds are also associated with the use of powdered milk instead of declared, fresh material. In this context, various analytical methods have been adapted to dairy science applications with the aim to evaluate adulteration of milk samples, although time-consuming, suitable only for speciation or thermal treatment analysis, or useful for a specific fraud type. An integrated MALDI-TOF-MS platform for the combined peptidomic and proteomic profiling of milk samples is here presented, which allows rapid detection of illegal adulterations due to the addition of either nondeclared bovine material to water buffalo) goat, and ovine milks or of powdered bovine milk to the fresh counterpart. Peptide and protein markers of each animal milk were identified after direct analysis of a large number of diluted skimmed and/or enriched diluted skimmed filtrate samples. In parallel, markers of thermal treatment were characterized in different types of commercial milks. Principal components scores of ad hoc prepared species- or thermal treatment-associated adulterated milk samples were subjected to partial least-squares regression, permitting a fast accurate estimate of the fraud extents in test samples at either protein and peptide level. With respect to previous reports on MALDI-TOF-MS protein profiling methodologies for milk speciation, this study extends that approach to the analysis of the thermal treatment and introduces an independent, complementaty peptide profiling measurement, which integrates protein data with additional information on peptides, validating final results and ultimately broadening the method applicability.
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