Abstract
An aqueous 1% solution of sodium dodecyl sulphate (SDS) will completely dissolve the myofibrillar proteins of fresh cod flesh, and of cod flesh stored at –14° until it is very tough. With the aim of detecting the formation of detergent stable intermolecular protein crosslinks during cold storage of cod flesh, a comparison has been made of the weight and z‐average molecular weights of the mixture of components in detergent solutions prepared from fresh cod flesh and cod flesh stored at –14° for various periods of time. This comparison has shown that very few, if any, such crosslinks are formed during cold storage of the flesh. By separately determining the average molecular weights of the individual constituent myofibrillar proteins in detergent solutions, probable limits to the extent of intermolecular crosslinking in the cold stored flesh by detergent‐stable bonds could be established.