isolation, purification, and identification of coconut protein through sds-page, hplc, and maldi-tof/tof-ms

Coconut palm (cocos nucifera l.) is rich in protein and consumed worldwide, coconut protein as a plant protein contains many nutrients and is beneficial for human health, but its allergic components also need to be considered. therefore, further research on coconut protein is of great significance. in this study, nine proteins were identified through matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry (maldi-tof/tof-ms). three proteins, namely, (1) 63 kda globulin-like protein [elaeis guineensis], (2) 63 kda globulin-like protein [phoenix dactylifera], and (3) glutelin type-a 3-like [e. guineensis] were initially found in coconut proteins. to further purify and identify the coconut protein, we used dialysate membrane and high-performance liquid chromatography-ultraviole (hplc-uv) to concentrate and separate the extracted protein. two types of 63 kda globulins were further purified and identified, namely, p. dactylifera and e. guineensis proteins with 564 and 398 amino acids, respectively, were identified. swiss-model was used to predict the tertiary structure of the 63 kda globulins and showed that the structures of the coconut proteins were mostly similar to those of vicilin. this work provided a feasible and simple separation approach for the isolation and purification of coconut protein, and predicts the structure of newly identified protein.