Identification of the Secondary Structure of Protein Isolated from Deoiled Cake Flour of Mahua (Madhuca Latifolia)

Abstract

The establishment of structures of protein is of primary importance before deciding its suitability for application in the fields of foodomics and pharmaceuticals. Out of the several techniques Fourier Transform Infrared Spectroscopy (FTIR) is a recognized analytical tool employed for ascertaining the structure of protein, in particular for the identification of the secondary structure of protein. The present investigation deals with the characterization of the proteins isolated from Madhuca latifolia (Mahua) de-oiled cake flour by FTIR. The proteins were isolated by two different methods: reverse micellar method using bis (2-ethylehexyl) sodium sulfosuccinate reverse micelle (RMP) and alkali treated method from aqueous system (ATP). The spectral bands in the range 4000-400 cm-1 for both the proteins were analyzed and compared. The Fourier second derivatives consisting of eight bands were applied to investigate the amide I region (1700-1600 cm-1) of both the proteins. The percentage of α-helix, β-sheet, unordered conformation and turn in RMP were found to be 12.69 %, 40.28 %, 12.14 % and 34.89 %, respectively, whereas in ATP these structures occurred in 12.50 %, 33.20 %, 12.00 % and 42.48%, respectively. These findings may be helpful to determine the functional properties of the extracted de-oiled cake flour proteins and hence its applications could be explored accordingly