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Nov 29, 2012 - Nowadays we face a globalized market, therefore the need to protect ... The complexity of interactions between milk protein (casein and whey protein) during milk ... PPINs derived from large-scale experiments portrait a global.

ALTRIFORMAGGI Autenticità, Legislazione, TRadizione e Innovazione per la valorizzazione delle produzioni casearie Avellino,  29/11/2012 – 1/12/2012  

ISBN 9788896394083  


DAAA, Università degli Studi del Molise, via De Sanctis, 86100 Campobasso, Italy


ISA-CNR, via Roma, 64, 83100 Avellino, Italy


Randall Division of Cellular and Molecular Biophysics, New Hunt’s House King’s College, SE1 1UL London, UK

*[email protected] Nowadays we face a globalized market, therefore the need to protect and enhance the “Made in Italy” products is a priority for the food industry. Scientific research in this field relates to the consumers’ need for high quality, convenience, safety and taste. Recent advances in genome and proteome research and their potential biotechnological exploitation offer a unique opportunity to enhance and select food quality as well as fight fraud in a rational way. The quality features (conservation, flavor, aging and solubility of milk proteins) of diary products can be investigated by the analysis of the Protein-Protein Interactions (PPIs) and Protein-Solvent Interactions (PSIs) that are involved. The complexity of interactions between milk protein (casein and whey protein) during milk transformation are strongly influenced by the chemical and chemical-physical properties of milk, physical treatments (i.e. temperature, pressure etc.) and by the enzymes from milk born microorganisms or from microorganisms added as starter. These interaction, that are specific for each type of traditional food product, could be the basis of the authenticity signature of the each traditional product. Therefore bioinformatics approaches could be represent a useful and rapid tool to identify such a signature. A bioinformatical approach to the analysis of PPIs and PSIs will be devised in terms of inspection of available large-scale maps of PPIs of different microorganisms present in pasteurized food and PSIs of milk proteins. We will tackle the problem of food quality and conservation by devising rigorous computational methods that can extract crucial protein interactions to develop QIs. These tools will benefit the wider Systems Biology community, because in the last years high-throughput proteomics has allowed for the drafting of large PPI networks (PPINs) of many taxa. Accurate descriptions of these assemblies must reflect the cellular context in which they usually operate and the many factors that may have conditioned their evolution and function. PPINs derived from large-scale experiments portrait a global picture of the proteins’ connectivity and offer an intricate and comprehensive picture of the detected interactions. The detailed analysis of a particular function necessary for food control and quality may benefit from the study of smaller and accurately selected sub-networks, containing high confidence interactions resulting from the cross-mapping of multiple sources of information for the nodes (proteins), such as gene expression data, domain profiles and structural information. By reducing further the scale of details analysed in a given PPIN, one could focus only on special proteins in the network, like multi-partner proteins ('hubs'). In particular, we will concentrate on protein hubs that have a resolved 3D-structure and for which we know accurate binding details. For the study of PSIs we have already devised computational methods for the analysis of interaction with water for the Prion food-borne pathologies and for the role of solvent in conformational changes and aggregation. Aggregation has been shown to be involved in the solubility loss in milk concentrate powder, therefore we will apply the same methodology to proteins critical for the production of cheese.

Sessione 1.1. Marchi di qualità e difesa delle produzioni casearie