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In the present study the effect of ice storage on physico-chemical and functional properties of proteins from Indian major carps with special emphasis on gel forming ability have been assessed for a period of 22 days. The solubility profile of proteins in high ionic strength buffer and calcium adenosine triphosphatase (ATPase) enzyme activity reduced significantly (p<0.05), while that of total volatile base nitrogen (TVB-N) increased significantly (p< 0.05) at the end of 22 days of ice storage. The major protein fraction showed association-dissociation-denaturation phenomenon during ice storage as revealed by gel filtration profile and viscosity measurements. The gel forming ability of three fish species both in fresh and during different periods of ice storage was assessed by measuring the gel strength of heat induced gel. Among the three species the gel strength of the gel obtained from Catla catla and Cirrhinus mrigala was higher (586 and 561 g.cm) than the gel obtained from Labeo rohita (395 g.cm) in fresh condition. The gel forming ability of three species was significantly affected (p<0.05) during ice storage. The TVB-N values of fish meat as a function of ice storage was within the prescribed limit up to 17 days of the ice storage.

The effects of ethanolic pineapple peel extract (PPE) powder at various concentrations (0–1.50%, w/w) on the gelling properties of silver carp surimi were investigated. The pineapple peel extract produced with 0–100% ethanol, revealed that 100% ethanol had the highest bioactive properties. Surimi gels with added PPE powder demonstrated improved gel strength (504.13 ± 11.78 g.cm) and breaking force (511.64 ± 11.80 g) up to 1% PPE addition; however, as PPE concentration increased beyond 1%, the gel strength decreased. Similarly, with the addition of 1% PPE powder, more hydrophobic bonds and fewer sulfhydryl groups and free amino groups were seen. However, the gels with PPE powder added showed a slight reduction in the whiteness of the surimi gels. FTIR analysis indicated that the fortification with PPE powder brought about the secondary structure of myofibrillar proteins; peaks shifted to the β-sheet region (PPE gels) from the α-helix region (control). SEM analysis indicated that the gel with 1% PPE powder had a relatively organized, finer and denser gel architecture. Overall results suggested that the addition of PPE powder up to 1% to the surimi gels enhanced the gelling properties as well as the microstructure of the surimi.

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