The Molecular Magic of “Meatless” Meats: Structural and Sequence Similarities between Soy Leghemoglobin and Bovine Globins

Abstract

Plant‐based proteins are becoming more prevalent in the modern day due to humanity’s fight against climate change. How do scientists produce plant‐protein that tastes similar to animal‐protein? When comparing bovine hemoglobin (2qss), soy leghemoglobin (2GDM) and bovine myoglobin (2qss), the proteins differ by location, number of heme proteins, oxygen affinity and backbone alignment. Hemoglobin is found in red blood cells of animals. More specifically, myoglobin is found in the red blood cells of muscle tissue in animals. Leghemoglobin, however, is the byproduct of the symbiotic relationship between root nodules on legumes and nitrogen‐fixing bacteria that lives on them. However, all of these proteins are linked by the common molecule, heme. Plant‐based “meat” manufacturers suggest that this heme group, that is embedded in each of these globins, is responsible for this “meaty” taste. Additionally, the presence of umami‐inducing amino acids was investigated and glutamic acid surface prevalence related to flavor. Using the suite of structural analysis applications in the Protein Data Bank, such as FATCAT and fast2BLAST, the structural similarities between bovine hemoglobin, especially the heme itself, bovine myglobin and soy leghemoglobin can be illustrated, both quantitatively and qualitatively (e.g. 3D‐printed models).