Abstract

ABSTRACTStabilization of fish actomyosin (AM) was investigated with respect to freeze‐ and heat‐induced denaturation as affected by concentration of sodium lactate (SL), lithium lactate and sucrose. Recovered Ca2+ ATPase activity was used as a measure of denaturation. Optimum cryoprotection was gained with 6% (w/v) SL. However, SL of similar quality from another source destablized AM at low concentration and was less effective at higher concentrations. Lithium lactate was not an effective cryoprotectant. For heat stabilization, SL was two times more effective than sucrose with an optimum concentration of 25%. Sodium lactate appears to have good potential as a cxyoprotectant and stabilizer of AM.

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