Effects of the Hydratation process on water-soluble proteins of preserved cod products.

Electrophoresis and chromatography were used to analyse the water-soluble proteins of fresh, salted and dried cod (Gadus mor- hua L.) and of re-hydrated products. Sodium dodecyl sulphate pore gradient gel electrophoresis showed that there was a great loss of water-soluble proteins during stockfish r...

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Bibliographic Details
Main Authors: DI LUCCIA A, ALVITI G, LA MACCHIA C, FACCIA M, GAMBACORTA G, LIUZZI V, SPAGNA MUSSO, SALVATORE
Other Authors: DI LUCCIA, A, Alviti, G, LA MACCHIA, C, Faccia, M, Gambacorta, G, Liuzzi, V, SPAGNA MUSSO, Salvatore
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Applied Science:An Imprint of Elsevier Science Ltd, The Boulevard, Langford Lane, Kidlington Oxford OX5 1GB United Kingdom:011 44 1865 843000, 011 44 1865 843699, EMAIL: nlinfo-f@elsevier.nl OR usinfo-f@elsevier.com OR forinfo-kyf04035@niftyserve.or.jp, INTERNET: http://www.elsevier.nl/, Fax: 011 44 1865 843010 2005
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Online Access:http://hdl.handle.net/11588/111422
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Summary:Electrophoresis and chromatography were used to analyse the water-soluble proteins of fresh, salted and dried cod (Gadus mor- hua L.) and of re-hydrated products. Sodium dodecyl sulphate pore gradient gel electrophoresis showed that there was a great loss of water-soluble proteins during stockfish re-hydration. Furthermore, comparison of the electrophoresis patterns of cod products, under reducing and non-reducing conditions, showed the presence of cross-linked protein aggregates, related to the oxidation of SH groups and oxidative stress. Similar results were obtained by high performance liquid chromatography, which confirmed a great loss of water-soluble proteins and a higher level of SH oxidation in hydrated stockfish samples. Finally, capillary electrophoresis allowed definition of the unfolded state of denatured proteins in salted cod. This technique also proved a fast and useful way to differentiate the two products by analysis of water-soluble proteins.