クルクミン封入率の向上：脱アミド化とpHシフトにより改質された大豆タンパク質単離物：新規プロテイングルタミナーゼを用いたメカニズム解明

This study elucidates the mechanism of curcumin encapsulation in soy protein isolate (SPI) modified via enzymatic deamidation and pH-shifting. A novel Chryseobacterium sediminis-derived glutaminase (CS-PG) demonstrated superior thermal stability, catalytic efficiency, and specificity over commercial CP-PG. Controlled deamidation by both enzymes enhanced SPI functionality (solubility/emulsification/foaming) with minimal hydrolysis, where CS-PG induced hydrophobic self-assembly and CP-PG promoted hydrophilic domain formation. These distinct conformations dictated binding modes: CS-PG-SPI achieved 92.97 % higher encapsulation efficiency versus SPI through hydrophobic encapsulation, while attained an 85.00 % increase via surface-layer stabilization. pH-shifting further altered SPI conformation by inducing reversible unfolding and refolding, enabling formation of amorphous, stable protein-curcumin complexes. Dual modification significantly enhanced bioaccessibility versus free curcumin-1034 % for CS-SPI-Cur-pH and 1058 % for CP-SPI-Cur-pH. The work establishes enzymatic deamidation as a precision tool for tailoring SPI self-assembly and bioactive delivery in functional foods.