Graduation date: 1998

A novel method for isolating fish proteins by shifting pH to high acid or high alkali pH was the focus of the study. Biochemical and physicochemical properties of various pH-treated soluble fish proteins as a function of ionic strength were determined. Effect of ionic strength and various storage conditions on gelation properties and stabilization of fish protein isolate (FPI) were also elucidated. At low ionic strength (IS 10 mM NaCl), the solubility of Pacific whiting (PW) proteins was low between pH 5 and 10, but increased significantly as the pH was shifted to either acidic or alkaline pH. The isoelectric point (pi) shifted toward acidic direction as IS increased to 600 mM. High IS (600 mM NaCl) resulted in protein aggregation at low pH but improved myosin heavy chain (MHC) solubility at pH 6 - 10. Changes in total sulfhydryl (SH) content and surface hydrophobicity (S [subscript o]) were associated with the different molecular weight distributions of the soluble proteins. At pH 4 and IS 10-100 mM, MHC was soluble but degraded. At pH 10, the formation of high MW polymers was observed at IS [greater than or equal to] 150 mM. Gels obtained from FPI prepared at pHl1/IS150 and conventional surimi (CS) were superior to FPI prepared at pH 3 and/or other IS levels. There was no correlation between protein solubility and gel properties of FPI. Gelation mechanisms of acid and alkali-treated FPI were identical under the same IS condition. FPI prepared at pH 3 or 11 could be partly refolded at pH 7. No significant difference in texture was observed between alkali-treated protein isolates (AKPI, pH 11) kept frozen at pH 5.5 and 7.0. Strongest gel was found for AKPI with cryoprotectants (C) and without freeze/thaw (FT) cycles at both pH storage (5C & 7C), while poor gel was obtained from AKPI without cryoprotectants (NC) and with FT (5NC-F & 7NC-F). 5NC-F & 7NC-F demonstrated the lowest S [subscript o] and total SH probably suggesting that proteins were more aggregated as a result of hydrophobic interactions and disulfide bonds. Scanning electron microscope (SEM) revealed the most discontinuity of gels from AKPI without cryoprotectants and with FT and showed less protein stability when stored at pH 5.5 than at neutral pH. Raman spectral analysis demonstrated that refolding of AKPI by pH adjustment to 7.0 was achieved, but not identical to the native protein. CS contained higher α-helix content (~50%) than AKPI (~20-30%). Frozen storage induced a decrease and an increase in the α-helix of CS and AKPI samples, respectively. Alkali-treated proteins were slightly less stable than CS during frozen storage. / Graduation date: 2005

The rheological, color, micro-structural, and electrical properties of surimi seafood gels were investigated. Various starches and protein additives at different ratios were evaluated with Alaska pollock surimi under ohmic heating at different heating rates to determine their functional properties and further to compare these properties with those of conventionally cooked gels. Native starches at low concentration were able to enhance rheological properties due to their gelatinization during heating. Pregelatinized starch decreased texture properties; however, it could suppress the undesirable appearance of the final product because its granules could absorb the surrounding water during chopping and perform a higher degree of retrogradation when cooling. A mixture of native and pregelatinized starches showed a positive trend at high concentration. The more starch added, the lower the L* and b* values of the gels. Protein additives improved textural properties, but negatively affected gel colors. Lower moisture content of the final products showed higher strength in texture, but lower lightness values. Gels cooked under ohmic heating with a slow heating rate mostly exhibited better texture properties than conventionally cooked gels. Electrical conductivities increased when temperature increased, resulting in a linear relationship. Electrical conductivity also significantly increased with moisture content, and slightly increased with applied frequency and voltage. There were some changes in the magnitude of electrical conductivity of surimi-starch paste when temperature increased, most obviously seen at a high concentration of native starch with slow ohmic heating. This indicated that starch gelatinization affected the electrical conductivity of surimi-starch paste while heating. / Graduation date: 2003