Thermal stability of myofibrillar protein from Indian major carps

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dc.contributor.authorSankar, T.V.
dc.contributor.authorRamachandran, A.
dc.date.accessioned2017-12-28T06:32:40Z
dc.date.available2017-12-28T06:32:40Z
dc.date.issued2005
dc.description.abstractThe 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.en_US
dc.identifier.citationJ. Sci. Food Agric. 86(4): 563-568en_US
dc.identifier.urihttp://hdl.handle.net/123456789/3230
dc.language.isoenen_US
dc.subjectmyofibrillar proteinen_US
dc.subjectIndian fishen_US
dc.subjectcarpen_US
dc.subjectthermal denaturationen_US
dc.subjectsolubilityen_US
dc.titleThermal stability of myofibrillar protein from Indian major carpsen_US
dc.typeArticleen_US
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