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• pH and ratio largely governed turbidity changes of SMGHs/ κ -C complexes. • pH c exhibited ratio-independent, and pH φ1 , pH max exhibited ratio-dependent behaviors. • SMGHs aggregates and agglomerated SMGHs/ κ -C support the gel strength at acid pH. • SMGHs/ κ -C at acid pH had greater interaction with water to support the gel formation. • SMGHs/ κ -C formed a denser network at acid pH with stronger gel strength. The electrostatic complex coacervation between scallop Patinopecten. yessoensis male gonad hydrolysates (SMGHs) and κ -carrageenan (κ -C) were monitored by using turbidimetry at various pH (1–12) and biopolymer mixing ratio (9:1–1:9). The pH c exhibited ratio-independent behavior, and pH φ1 , pH max exhibited ratio-dependent behavior, respectively. The decreasing ratio enhanced the gel strength of SMGHs/ κ -C at higher pH while inversely at lower pH, ascribing to more SMGHs aggregates and stronger neutralization between positively charged patches in SMGHs and κ -C at lower pH and higher ratio. Moreover, SMGHs/ κ -C gel at acid condition exhibited lower relaxation times (T 21 and T 23). Furthermore, the rheological and relaxation time T 2 data were well associated with microscopy images which indicated that SMGHs/ κ -C gel showed a well-distributed network structure at more acidic domains, supporting stronger gel rigidity and water-holding capacity. [ABSTRACT FROM AUTHOR]

• Protein isolates (pcRPIs) and lipids (pcRLs) of large yellow croaker roes were extracted simultaneously. • The purity of pcRPIs was greater than 70% with vitellogenin, vitellogenin B and vitellogenin C as main proteins. • pcRLs were mainly composed of triglyceride with high level of EPA and DHA content. • pcRPIs exhibited better physicochemical and functional properties than pcR. • pcRPIs had the better oil holding capacity and emulsifying abilities than soy protein isolate. The objective of this study was to simultaneously obtain protein isolates and lipids from the dried powder of large yellow croaker (Pseudosciaena crocea) roes (pcRs) to achieve high-value utilization. Protein isolates and lipids were extracted simultaneously from pcRs by saline and acidic solutions. The purity of the protein isolates from the pcRs (pcRPIs) was greater than 70%, with vitellogenin, vitellogenin B and vitellogenin C as the main proteins. The lipids from pcRs (pcRLs) were mainly composed of triglycerides with high levels of EPA and DHA. The pcRPIs exhibited a higher surface hydrophobicity, water/oil holding capacity and emulsifying ability than those of the pcRs. Moreover, pcRPIs had a better oil holding capacity and emulsifying ability than soy protein isolate. These results suggest that protein isolates and lipids can be simultaneously extracted by saline and acidic solutions, and pcRPIs and pcRLs can be used as functional materials in the food industry. [ABSTRACT FROM AUTHOR]