Open AccessEffect of succinylation on the secondary structures, surface, and thermal properties of date palm pollen protein concentrate
Author(s) -
Haïfa Sebii,
Sirine Karra,
Brahim Bchir,
Zeineb Nhouchi,
Abir Mokni Ghribi,
Romdhane Karoui,
Christophe Blecker,
Souhail Besbes
Publication year - 2020
Publication title -
journal of food science and technology/journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.656
H-Index - 68
eISSN - 0975-8402
pISSN - 0022-1155
DOI - 10.1007/s13197-020-04577-1
Subject(s) - succinylation , succinic anhydride , solubility , chemistry , denaturation (fissile materials) , lysine , differential scanning calorimetry , food science , pulmonary surfactant , chemical engineering , biophysics , biochemistry , organic chemistry , nuclear chemistry , amino acid , biology , thermodynamics , physics , engineering
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.