R

Raffaele Mezzenga

ETH Zurich

ORCID: 0000-0002-5739-2610

Publishes on Supramolecular Self-Assembly in Materials, Lipid Membrane Structure and Behavior, Proteins in Food Systems. 639 papers and 36.1k citations.

639Publications
36.1kTotal Citations
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Top publicationsby citations

Sustainable technologies for water purification from heavy metals: review and analysis
Cited by 1.5k

Water pollution is a global problem threatening the entire biosphere and affecting the life of many millions of people around the world. Not only is water pollution one of the foremost global risk factors for illness, diseases and death, but it also contributes to the continuous reduction of the available drinkable water worldwide. Delivering valuable solutions, which are easy to implement and affordable, often remains a challenge. Here we review the current state-of-the-art of available technologies for water purification and discuss their field of application for heavy metal ion removal, as heavy metal ions are the most harmful and widespread contaminants. We consider each technology in the context of sustainability, a largely neglected key factor, which may actually play a pivotal role in the implementation of each technology in real applications, and we introduce a compact index, the Ranking Efficiency Product (REP), to evaluate the efficiency and ease of implementation of the various technologies in this broader perspective. Emerging technologies, for which a detailed quantitative analysis and assessment is not yet possible according to this methodology, either due to scarcity or inhomogeneity of data, are discussed in the final part of the manuscript.

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Gang Wei, Zhiqiang Su, Nicholas P. Reynolds et al.|Chemical Society Reviews|2017
Cited by 894Open Access

Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.

Modification approaches of plant-based proteins to improve their techno-functionality and use in food products
Cited by 706Open Access

Plant-based proteins have recently attracted particular interest owing to their sustainable origins, economical costs and health benefits compared to animal-based counterparts. However, most of them have limited applications due to their inferior functionality, which is the consequence of poor-aqueous solubility, complexity and sensitivity to environmental stress conditions such as pH, salt and temperature. Additionally, plant proteins are often embedded in hemicellulose, lignin and other poorly digestible polysaccharides, which further reduce their bioavailability. Therefore, the modulation of plant proteins to improve their technological and industrial applications, and make them more accessible in general, is highly sought after. The modification of plant proteins by altering their physicochemical properties provides the possibility to improve and diversify their technofunctionality and biological activities as well as addressing their limitations. The selection of protein modification method should be done carefully from the final application view especially in food products since it can influence the protein functional, nutritional and organoleptic properties. Therefore, discussing different modification methods with their advantages and disadvantages is particularly timely. This review highlights and discusses the modification methods for plant proteins in order to make their applications in foods more feasible by improving their flavor, nutrition and techno-functional attributes, which will open up new opportunities within different plant-based food products.

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