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Structural changes and dynamic rheological properties of sarcoplasmic proteins from striped catfish ( Pangasius hypophthalmus ) treated by various pH-shift processes were investigated. Isoelectric precipitation of acid-extracted sarcoplasmic proteins led to the lowest solubility in water. Sarcoplasmic proteins were unfolded after extremely acidic and alkaline extraction, exposing tryptophan and aliphatic residues. The alpha-helical structure was converted to beta-sheet following acidic extraction, whereas alkaline treatment did not disturb the alpha-helical structure of sarcoplasmic proteins. Disulfide formation, hydrogen bonding via tyrosine residues, and hydrophobic interactions occurred under extreme pH extraction. Acidic extraction induced denaturation and aggregation of sarcoplasmic proteins to a greater extent than did alkaline treatment. Hydrophobic interactions via aliphatic and aromatic residues were formed during isoelectric precipitation. Sarcoplasmic proteins were partially refolded after isoelectric precipitation followed by neutralization. Sarcoplasmic proteins prepared from an alkaline pH-shift process readily aggregated to form a gel at 45.10 degrees C, whereas higher thermal denaturation temperatures (>80 degrees C) and gel points ( approximately 78 degrees C) were observed in acid-treated sarcoplasmic proteins. The pH condition used for extraction, precipitation, and neutralization greatly affected structural changes of sarcoplasmic proteins, leading to different thermal and dynamic rheological properties.

The effect of washing treatments (water and alkali washing) and alkali extraction/acid precipitation on the physicochemical and textural properties of striped catfish (Pangasius hypophthalmus) muscle protein was compared. Alkali extraction/acid precipitation process resulted in the highest protein recovery of 98.77% (dry weight basis) and lowest fat content of 0.98% (dry weight basis). The extractable proteins of fish protein isolates (FPI) at various ionic strengths (0 to 0.6 M NaCl) exhibited majority of protein at 38 kDa with trace amount of others. Unsaturated fatty acids, namely, oleic, linoleic, and docosahexaenoic acid, were greatly reduced in FPI. Water-washed mince (W) exhibited higher autolytic activity than mince (M), suggesting the presence of myofibril-bound proteinase(s). Autolytic activity was lowest in the FPI. Breaking force of striped catfish gels was greatly improved when set at 40 degrees C for 30 min, regardless of preparation treatment. The typical water washing process was effective to improve gel-forming ability of striped catfish. FPI gels contained the lower total sulfhydryl content, indicating the greater extent of disulfide bond formation as compared to that of washed mince. The FPI gels showed higher breaking force but lower deformation values than W and alkali-washed (AW) gels. Addition of NaCl improved deformation, but adversely affected breaking force of FPI gel. Whiteness of FPI gel increased with NaCl addition.

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