Authors: Saipriya Ramalingam, Jamshid Rahimi, Ashutosh Singh
Published in: CSBE-SCGAB Technical Conferences » AGM Charlottetown 2022
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Description: With the world shifting its attention towards more sustainable protein sources, mung bean, in recent times has garnered research acclaim as a functional food. Its high protein and wholesome amino acid availability puts it at par with other legumes such as soy and kidney beans. Mung bean seed protein consists of three storage globulin sub-units namely 7S, 8S, and 11S, of which 8S (vicilin) is the major sub-unit. In this study, a molecular dynamic approach has been taken using 2CV6, the crystal structure of 8S? globulin. GROMACS software was used to perform simulation studies by varying thermal and pressure parameters i.e., (300K, 373K, and 398K at 3Kbar, 5Kbar, and 7Kbar) respectively. The aforementioned pressure and temperature parameters were chosen to mimic experimental work such as HPP and extrusion to analyze the effect processing had on the secondary structure of the protein. Ramachandran plots were used to study the changes in torsional angles of the amino acid residues, while solvent accessible surface area (SASA) calculations defined the amino acid residues accessible to solvents and ligands. Results reveal that the protein undergoes significant compaction upon increasing temperature and pressure. STRIDE analysis shows that 2° structures such as ?-helices and ?- sheets undergo conformational changes to form turns and coils, indicating increased randomness. Hence, this study can be a gateway to understanding the functional properties of mung bean protein when subjected to heat and pressure.
Keywords: 8S mung bean, GROMACS, protein secondary structure, radius of gyration
Conference name: CSBE/SCGAB 2022 Annual Conference, Charlottetow, PEI, 24-27 July 2022.
Session name: Food and Bioprocessing7
Publication type: Presentation
Language 1: en
Rights: Canadian Society for Bioengineering