Protein matrix interactions and adaptogenic bioactive release in high-protein cracker systems enriched with Rhodiola rosea and Eleutherococcus senticosus

Bioactive compounds like phenylpropanoids and phenylethanoids, found in adaptogenic roots Rhodiola rosea (RR) and Eleutherococcus senticosus (ES), are commonly used in supplements. Crackers made with pulse protein isolates represent a vehicle to deliver these compounds. This study investigated interactions of RR and ES root powders with protein isolates (pea (PPI), faba bean (FBPI), lentil (LPI) and lupin (LuPI)) and their impact on dough and cracker physicochemical properties. In addition, in vitro bioaccessibility was studied. Root powders significantly increased dough consistency, with RR promoted protein aggregation. In the crackers, a reduced lightness and increased yellowness was shown, particularly with RR. FBPI_control crackers were the hardest and stiffest, while root addition generally softened texture. FTIR revealed that secondary structure changes influenced in vitro bioaccessibility, with β-sheets and protein aggregates limiting and random coil enhancing release of bioactives. Combining adaptogenic roots with pulse proteins is a promising strategy for producing functional high-protein crackers. • ES and RR roots modified the dough consistency and protein aggregation behavior. • Protein secondary structure (β-type protein aggregates) modulated cracker hardness. • α-Helix restricted the release of eleutheroside B and E and tyrosol. • Protein source modified the release of bioactive compounds and the bioaccessibility.