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http://hdl.handle.net/123456789/6711
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DC Field | Value | Language |
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dc.contributor.advisor | Nambudiri, D D | - |
dc.contributor.author | Bomy Chummar | - |
dc.date.accessioned | 2020-01-03T08:59:47Z | - |
dc.date.available | 2020-01-03T08:59:47Z | - |
dc.date.issued | 2000 | - |
dc.identifier.sici | 171590 | en_US |
dc.identifier.uri | http://hdl.handle.net/123456789/6711 | - |
dc.description.abstract | Freezing ~ considered as an excellent process for preserving the quality of fish for longer periods. But freezing may affect various flesh components, especially the proteins. Sarcoplasmic proteins play a major role in species identification of fish and fishery products. While myofibrillar proteins play a major role in the jellying properties of surimi and surimi based products. The changes to these groups of proteins due to freezing and frozen storage have received much attention. Four species Megalaspis cordyla, Labeo rohita, Penaeus indicus and Parapenaeopsis styli/era were used for the frozen storage study. Samples were stored for 90 days at -18°C and samples were collected at 15 day. intervals and Salt Soluble Nitrogen (SSN), Water Soluble Nitrogen (WSN) and Non-Protein Nitrogen (NPN) content were determined. Electrophoretic pattern of both Salt Soluble Proteins (SSP) and Water Soluble Proteins (WSP) of frozen stored sample were compared with that of the fresh sample. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Department of Processing Technology,College of Fisheries, Panangad | en_US |
dc.subject | Muscle protein | en_US |
dc.subject | Sarcoplasmic protein | en_US |
dc.subject | Myofibrillar proteins | en_US |
dc.subject | Contractile proteins | en_US |
dc.subject | Electrophoretic techniques | en_US |
dc.subject | Isoelectric focusing | en_US |
dc.title | Studies on the electrophoretic pattern of fish/ shellfish proteins subjected to frozen storage | en_US |
dc.type | Thesis | en_US |
Appears in Collections: | PG Thesis |
Files in This Item:
File | Description | Size | Format | |
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171590.pdf | 1.98 MB | Adobe PDF | View/Open |
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