南極オキアミ凝集体の圧力駆動解重合：構造再編成とゲル化強化機能

This study investigated the effects of ultra-high pressure (UHP) technology as a non-thermal method on the depolymerization, structure, and functional properties of Antarctic krill protein (AKP) aggregates. UHP treatment significantly improved AKP functionality. Solubility notably increased from 91.4 % (Control) to 97.1 % at 600 MPa, concomitant with a pressure-dependent decrease in turbidity. Particle size analysis confirmed a depolymerization effect, with the main particle size peak shifting from 232.8 nm (Control) to 72.25 nm (600 MPa). Structural analysis revealed UHP-induced protein unfolding, evidenced by a 29.8 % increase in surface hydrophobicity (at 400 MPa), a decrease in total sulfhydryl content, and a conformational transition from α-helix (32.50 % in control) to β-sheet (30.40 % at 600 MPa). These structural modifications significantly enhanced gelation functionality; the storage modulus peaked at 600 MPa, corresponding to the formation of a dense and uniform microscopic network.