Globally, 1.3 billion tons of food is wasted annually, with few uses other than landfilling, anaerobic digestion, or composting. Food waste (FW) repurposing provides an alternative waste management strategy toward meeting goal 12 of the United Nations sustainable development goals. Here, we present an integrated biorefinery technology, repurposing potato peel waste (PPW) for manufacturing multiple biobased value-added products.We report an integrated biorefinery comprising three stepwise processes: ultrasonic extraction to recover extractives for high activity antioxidants' production, optimized hydrolysis and dehydration of glucose resulting in the highest reported yields (54%) of 5hydroxymethylfurfural (HMF), directly from potato peels, for manufacturing biobased chemical precursors, and finally, pyrolysis of the residual lignin into biochar for remediating pesticide contaminated water, improving water quality. As a best-case scenario, we obtain revenues of about $6300 per MT of dry PPW. This provides the opportunity for successful translation of our technology to an economically profitable process using zero value food waste. This study provides a sustainable valorization blueprint that can be extended to other types of FW for improving the economics of biomass-based biorefineries by manufacturing multiple renewable products.

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It is important to have sustainable and edible scaffolds to produce cultivated meat. In this research, three-dimensional (3D) porous scaffolds were developed by soy protein amyloid fibrils for cultivated meat applications. Food-safe biological and physical cross-linking methods using microbial transglutaminase and temperature-controlled water vapor annealing technique were employed to crosslink soy protein amyloid fibrils, resulting in the production of 3D scaffolds. The generated 3D scaffolds had pores with sizes ranging from 50 to 250 μm, porosities of 72–83%, and compressive moduli of 3.8–4.2 kPa, depending on the type of soy protein used in the process (β-conglycinin (7S), glycinin (11S) and soy protein isolate (SPI)). When present with pepsin, these scaffolds can degrade within an hour but remain stable in phosphate-buffered saline for at least 30 days. The soy protein amyloid fibril scaffolds enabled C2C12 mouse skeletal myoblasts proliferate and differentiate without adding cell adhesive proteins or other coatings. The results demonstrate the potential of abundant and inexpensive soy protein amyloid fibrils to be utilized as scaffold materials for cultivated meat in the food industry.

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