Computational evaluation of the effect of processing on the trypsin and alpha‐amylase inhibitor from Ragi (Eleusine coracana) seed

Abstract

Ragi, also known as Finger millet, has been promoted as a healthy alternative to major cereals such as rice and wheat. It is a well‐known source of various minerals, dietary fiber, and a primary source of carbohydrate in parts of Asia and Africa. Ragi is a drought resistant crop, hence, useful for adapting to the current climate change and depleting water resource conditions in various parts of the world. However, the Ragi is known to have poor digestibility, primarily due to the presence of antinutritional compounds like alpha‐amylase and trypsin inhibitor. We have studied temperature, static electric fields (SEFs) and oscillating electric fields (OEFs) to evaluate the secondary structure changes of alpha‐amylase and trypsin inhibitor molecule in Ragi. This was simulated at three temperatures: 300, 343, and 373 K with SEF and OEF at an intensity of 1 V/nm with a frequency of 2.45 GHz (for OEF). STRIDE analysis exhibits various changes in the secondary structure of the protein, especially the loop connecting the alpha helices together. Thermal processing alone has also affected the second alpha helix of the molecule. Overall, the SEFs of 1 V/nm are found to have resulted in the most secondary structure deviations in terms of root mean square deviation and radius of gyration.

STABILITY OF OMEGA-3 COMPOUNDS COMPLEX WITH PPAR-γ RECEPTOR AS AN ANTI-OBESITY USING MOLECULAR DYNAMIC SIMULATION

“…The lower value of SASA, the more stable the system complex [12]. This analysis is not correlated with the RMSD value that presented DHA has better stability in PPAR-γ receptor than DPA and HPA.…”

“…The identification of SASA was carried out to predict the protein conformation changes during the simulation, which can be accessed by water molecules [12]. SASA was analyzed during 100 ns of MD trajectory simulation, which is shown in fig.…”