Ramachandran, A; Sankar, T V(Society of Chemical Industry, November 26, 2004)
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Abstract:
The characteristics and stability of natural actomyosin (NAM) from rohu (Labeo rohita), catla
(Catla catla) and mrigal (Cirrhinus mrigala) were investigated. The total extractable actomyosin (AM)
was higher (7.60mgml−1) in the case of rohu compared with that from catla and mrigal (5mgml−1).
Although the specific AM ATPase activity was similar (0.43–0.5 μmolPmin−1 mgP−1) among the three
species, the total ATPase activity was lower in mrigal (25 μmol g−1 meat) compared with the other species
(37 μmol g−1 meat). The inactivation rate constants (kd) of AM Ca ATPase activity showed differences in
the stabilities of actomyosin among these fish, the actomyosin from catla being least stable. The NAM
from these species was stable up to 20 ◦C at pH 7.0. Catla AM became unstable at 30 ◦C, while rohu and
mrigal AM could withstand up to 45 ◦C. The thermal denaturation with respect to solubility, turbidity,
ATPase activity, sulphhydryl group and surface hydrophobicity showed noticeable changes at around
these temperatures