Abstract
Gel strength enhancement of Pacific whiting surimi was studied by using an α2-macroglobulin (α2-M)-enriched plasma fraction (FIV-1) and a transglutaminase (TG)-enriched plasma fraction (FI-S). Fluorescent amine-incorporating activity was detected in FIV-1, FI-S, and bovine plasma protein (BPP), indicating potential protein cross-linking activity by α2-M and TG. Inhibition of autolytic activity was observed with FIV-1 and BPP. FIV-1 in combination with bovine serum albumin, fibrinogen, or FI-S enhanced gelation more than FIV-1 alone. These results indicate various components in BPP function both to enhance gelation of Pacific whiting surimi and to inhibit proteolysis. Keywords: Plasma protein; transglutaminase; α2-macroglobulin; surimi; gelation
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