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Updated: Apr 12, 2026
Forming Giant-sized Polymersomes Using Gel-assisted Rehydration
Published on: May 26, 2016
Pressure-driven depolymerization of Antarctic krill aggregates: Structural reconfiguration and gelation-enhanced
Na Li1, Qingcheng Meng1, Xin Zhao2
1SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Liaoning Province Key Laboratory for Marine Food Science and Technology, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.
Abstract:
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.
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