The properties of natural actomyosin (NAM) containing 2% or 8% fish protein hydrolysate (FPH-2, FPH-8) or 8% sucrose-sorbitol blend (SuSo) were compared to control NAM before and after freeze-thaw treatment. Surface hydrophobicity of control and FPH-2 increased after freeze-thaw treatment, while that of FPH-8 did not change, which may be related to greater thermostability of actin and myosin in FPH-8 as observed by differential scanning calorimetry. The cooked gel of freeze-thawed control had 39% expressible moisture after an 8.5% cook loss, whereas gels of freeze-thawed SuSo, FPH-2 and FPH-8 had significantly lower expressible moisture (15-22%) and no cook loss. Gels of freeze-thawed FPH-2 and FPH-8 were similar to unfrozen control gel in hardness, cohesiveness and gumminess. This study demonstrates that FPH effectively stabilised NAM protein structure and function during freeze-thaw treatment.
Copyright © 2012 Elsevier Ltd. All rights reserved.