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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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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spelling ftunivnapoliiris:oai:www.iris.unina.it:11588/111422 2024-06-23T07:51:05+00:00 Effects of the Hydratation process on water-soluble proteins of preserved cod products. DI LUCCIA A ALVITI G LA MACCHIA C FACCIA M GAMBACORTA G LIUZZI V SPAGNA MUSSO, SALVATORE DI LUCCIA, A Alviti, G LA MACCHIA, C Faccia, M Gambacorta, G Liuzzi, V SPAGNA MUSSO, Salvatore 2005 STAMPA http://hdl.handle.net/11588/111422 eng eng 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 volume:93 firstpage:385 lastpage:393 numberofpages:9 journal:FOOD CHEMISTRY http://hdl.handle.net/11588/111422 Atlantic cod Sarcoplasmic protein Dried cod product Cross-linked aggregates info:eu-repo/semantics/article 2005 ftunivnapoliiris 2024-06-10T14:58:45Z 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. Article in Journal/Newspaper atlantic cod IRIS Università degli Studi di Napoli Federico II
institution Open Polar
collection IRIS Università degli Studi di Napoli Federico II
op_collection_id ftunivnapoliiris
language English
topic Atlantic cod
Sarcoplasmic protein
Dried cod product
Cross-linked aggregates
spellingShingle Atlantic cod
Sarcoplasmic protein
Dried cod product
Cross-linked aggregates
DI LUCCIA A
ALVITI G
LA MACCHIA C
FACCIA M
GAMBACORTA G
LIUZZI V
SPAGNA MUSSO, SALVATORE
Effects of the Hydratation process on water-soluble proteins of preserved cod products.
topic_facet Atlantic cod
Sarcoplasmic protein
Dried cod product
Cross-linked aggregates
description 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.
author2 DI LUCCIA, A
Alviti, G
LA MACCHIA, C
Faccia, M
Gambacorta, G
Liuzzi, V
SPAGNA MUSSO, Salvatore
format Article in Journal/Newspaper
author DI LUCCIA A
ALVITI G
LA MACCHIA C
FACCIA M
GAMBACORTA G
LIUZZI V
SPAGNA MUSSO, SALVATORE
author_facet DI LUCCIA A
ALVITI G
LA MACCHIA C
FACCIA M
GAMBACORTA G
LIUZZI V
SPAGNA MUSSO, SALVATORE
author_sort DI LUCCIA A
title Effects of the Hydratation process on water-soluble proteins of preserved cod products.
title_short Effects of the Hydratation process on water-soluble proteins of preserved cod products.
title_full Effects of the Hydratation process on water-soluble proteins of preserved cod products.
title_fullStr Effects of the Hydratation process on water-soluble proteins of preserved cod products.
title_full_unstemmed Effects of the Hydratation process on water-soluble proteins of preserved cod products.
title_sort effects of the hydratation process on water-soluble proteins of preserved cod products.
publisher 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
publishDate 2005
url http://hdl.handle.net/11588/111422
genre atlantic cod
genre_facet atlantic cod
op_relation volume:93
firstpage:385
lastpage:393
numberofpages:9
journal:FOOD CHEMISTRY
http://hdl.handle.net/11588/111422
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