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Thermal stability of myofibrillar protein from Indian major carps

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Title Thermal stability of myofibrillar protein from Indian major carps
Not Available
 
Creator Sankar T V
Ramachandran, A.
 
Subject myofibrillar protein
Indian fish
carp
thermal denaturation
solubility
turbidity
ATPase activity
SH groups
surface hydrophobicity
 
Description Not Available
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 (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.
Not Available
 
Date 2022-09-16T10:23:54Z
2022-09-16T10:23:54Z
2005-03
 
Type Research Paper
 
Identifier Sankar, T. V. and Ramachandran, A. (2005) Thermal stability of myofibrillar protein from Indian major carps. Journal of the Science of Food and Agriculture. 85(4): 563-568.
0022-5142
http://krishi.icar.gov.in/jspui/handle/123456789/74274
 
Language English
 
Relation Not Available;
 
Publisher Wiley