Effect of succinylation on the secondary structures, surface, and thermal properties of date palm pollen protein concentrate

Haifa Sebii; Sirine Karra; Brahim Bchir; Zeineb Nhouchi; Abir Mokni Ghribi; Romdhane Karoui; Christophe Blecker; Souhail Besbes

doi:10.1007/s13197-020-04577-1

Effect of succinylation on the secondary structures, surface, and thermal properties of date palm pollen protein concentrate

J Food Sci Technol. 2021 Feb;58(2):632-640. doi: 10.1007/s13197-020-04577-1. Epub 2020 Jun 24.

Authors

Haifa Sebii¹, Sirine Karra¹, Brahim Bchir¹, Zeineb Nhouchi², Abir Mokni Ghribi¹, Romdhane Karoui², Christophe Blecker³, Souhail Besbes¹

Affiliations

¹ Laboratory of Analysis Valorization and Food Safety, University of Sfax, National Engineering School of Sfax, Soukra Road, BP W-3038 Sfax, Tunisia.
² University of Artois, EA 7394, Institut Charles Viollette, F-62300 Lens, France.
³ Gembloux Agro-Bio Tech, Laboratory of Food Science and Formulation, University of Liège, Passage des Déportés 2 B, B-5030 Gembloux, Belgium.

Abstract

The present study was attempted to investigate the effect of succinylation, as chemical modification, on the functionality of male date palm pollen protein concentrate (MDPPPC). Succinylation was applied at two levels, 4 and 8 mol of succinic acid per mole of lysine. 4 M and 8 M were compared to the native MDPPPC. Findings proved that succinylation improved the surface properties of pollen protein including solubility and surfactant activity. Increased solubility of succinylated MDPPPC has been noticed especially in pH superior to pHi. The results from the differential scanning calorimetry showed a significant decrease (P < 0.05) of the denaturation temperature and the heat enthalpy for succinylated MDPPPC. β turn of succinylated MDPPPC increased significantly (P < 0.05) at the expense of β sheet indicating that the protein gained more mobility after succinylation which explains the enhancement of the functional properties and promotes the use of succinylated protein as a techno-functional ingredient.

Keywords: Protein concentrate; Secondary structures; Succinylation; Surface properties; Thermal properties.