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Thermal stability of myofibrillar protein from Indian major carps
Author(s) -
Sankar Thazhakot V,
Ramachandran Alappat
Publication year - 2005
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1956
Subject(s) - catla , labeo , myofibril , food science , biology , solubility , fish <actinopterygii> , chemistry , zoology , biochemistry , fishery , organic chemistry
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 (7.60 mg ml −1 ) in the case of rohu compared with that from catla and mrigal (5 mg ml −1 ). Although the specific AM ATPase activity was similar (0.43–0.5 µmol P min −1 mg P −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 ( k d ) 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. Copyright © 2004 Society of Chemical Industry