Nutritech - Rethinking the Food Chain

1st Congress on Food Structure Design: Innovation in food structure properties-relationships

3.11.2014 11:14


1st Congress On Food Structure Design organized by COST Action FA1001 (The application of innovative fundamental food-structure-property relationships to the design of foods for health, wellness and pleasure) was held on 15 – 17 October in Porto, Portugal. The conference gathered an interdisciplinary team of scientists from different research areas (food engineering, biophysics, applied soft matter, food technology, applied human nutrition, creative design) in the frame of an integrated process & product design approach. The focus was on three main sub-topics; I. Engineering of structures for tailored delivery of health-related functionalities, II. Process and product engineering for food properties generation/preservation/delivery, III. Sharing knowledge and technologies between academia and industry for healthy foods design. Over 30 oral presentations and over 100 posters were presented during the conference. The Congress on Food Structure Design will be organized every 2 years and the 2nd of the series will be held in October 2016 in Antalya, Turkey.

VTT's research scientists Natalia Rosa-Sibakov and Dilek Ercili-Cura presented two posters. Rosa-Sibakov presented a poster titled "Wet grinding and microfluidization of wheat bran preparations: Improvement of dispersion stability by structural disintegration". In this work, the good potential of wet grinding and microfluidization to produce wheat bran-based beverages was demonstrated. Both technologies clearly improved the dispersion stability of wheat bran particles due to the drastic disintegration of the structure of wheat bran fractions. Ercili-Cura's poster was titled: "Colloidal properties and surface activity of oat protein particles with/without transglutaminase treatment". Colloidal size and charge of oat protein particles in aqueous dispersions were studied and related to their surface active properties at air-water interface. Transglutaminase treatment rendered oat proteins with improved stability against extensive dissociation/re-association upon dilution at neutral pH, and increased the net negative charge.

Download posters:

Rosa-Sibakov et al 2014

Ercili-Cura et al 2014

Read more about the conference and the COST Action FA1001:

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