A standardized, innovative method to characterize the structure of aquatic protein hydrolysates

Heliyon

Vincent Fournier¹  Joël Henry²  Alexandre Leduc³ 

[1]DianaAqua, Symrise Group, Elven, France

[2]DianaAqua, Symrise Group, Elven, France

[3]Normandie University, UNICAEN, Sorbonne Universités, MNHN, UPMC Univ Paris 06, UA, CNRS, IRD, Biologie des Organismes et Ecosystèmes Aquatiques (BOREA), 14032, Caen, France

关键词: Food science;    Analytical chemistry;    Protein hydrolysate;    Hydrolysis process;    Peptide profile;    HPSEC;   

DOI  :  

来源: DOAJ

【 摘 要 】

The performances of protein hydrolysates highly depend on their peptide composition (amount, size and diversity), which itself closely depends on raw material origin and the hydrolysis parameters of the manufacturing process. The current analyses that characterize protein hydrolysates provide information on the level of hydrolysis (degree of hydrolysis, DH). However, they need additional describers to better characterize peptide profiles and product standardization. To reach this objective, we developed a fast and standardized method to characterize the abundance and the diversity of low-molecular-weight peptides in protein hydrolysates. This method innovatively combines classical HPSEC and nLC-ESI-MS analytical tools to characterize any kind of hydrolysate, whether solid or liquid, in terms of peptide level and diversity, and then merge peptides into 2D diagrams to visualize comparisons between protein hydrolysates. The targeted applications of this new tool for characterizing complex protein hydrolysates are (i) verifying the standardization of the produced products across batches, and (ii) analyzing and understanding the consequences of the modifications of the hydrolysis process on the molecular profiles of the generated peptides. The sample standardization described in this study is therefore an essential prerequisite for the functional characterization of hydrolysates in vitro.

【 授权许可】

Unknown