PEA PROTEIN IS A SUSTAINABLE, VEGETABLE-BASED, PROTEIN SOURCE THAT HAS SHOWN PROMISE IN THE PRODUCTION OF MEAT AND DAIRY ANALOGUES. IN ORDER TO IMPROVE OUR KNOWLEDGE AND UNDERSTANDING OF PEA PROTEIN, WE WILL PRODUCE BIOINFORMATIC MODELS OF PEA PROTEIN SUBFRACTIONS VICILIN, LEGUMIN, AND CONVICILIN, AND WE WILL IDENTIFY LIPID BINDING REGIONS THEREIN. THESE STRUCTURAL MODELS WILL BE INTERPRETED THROUGH TECHNIQUES THAT QUANTIFY THE BONDING MECHANISMS IN PEA PROTEIN SECONDARY STRUCTURES. THESE MODELS WILL THEN BE USED TO UNDERSTAND EMULSIFICATION AND GELLING PROPERTIES OF PEA PROTEIN AND PROTEIN SUBFRACTIONS OVER SHELF LIFE, THUS CREATING A FULL LINK BETWEEN IN SILICO MODELS AND REAL-WORLD PERFORMANCE. THEY WILL ALSO BE APPLIED IN ORDER TO BETTER UNDERSTAND OUR NOVEL PROCESSING TECHNIQUE, COLD EXTRUSION. BY SUBJECTING PEA PROTEIN ISOLATE TO TEMPERATURES BETWEEN 0 AND -30°C, THE HYDROPHOBIC REGIONS WILL DENATURE, WHILE THE SINGLE SCREW EXTRUDER SUBJECTS THE ISOLATE TO HIGH SHEAR FORCES AND MOLECULAR REARRANGEMENT. THIS WILL CREATE PROTEINS WITH STRONG EMULSION STABILITY AND ACTIVITY, AS WELL AS UNIQUELY SOFT GELS THAT ARE HELD TOGETHER THROUGH HYDROPHOBIC BONDS. COMBINING STRUCTURE FUNCTION RELATIONSHIPS BETWEEN IN SILICO MODELS AND REAL WORLD PERFORMANCE, INTRODUCING COLD EXTRUSION AS A FORM OF PROTEIN MODIFICATION, AND CONFIRMING THE SHELF LIFE OF PEA PROTEIN GELS THROUGH ESTABLISHED RHEOLOGICAL TECHNIQUES.

Purdue University, West Lafayette IN

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