Collagen characteristics of farmed Atlantic salmon with firm and soft fillet texture

The possible role of collagen in texture variations among Atlantic salmon (Salmo salar L.) grown under commercial conditions at a Norwegian farm was studied. The texture was determined instrumentally as the breaking strength, and collagen and its salt (SSC), acid (ASC), pepsin (PSC) and insoluble (IF) fractions were analysed in order to determine the collagen aggregation degree. The collagen solubility and its overall amino acid (AA) composition showed no correlation to the breaking strength, but a positive correlation was observed between the breaking strength and glycine (r = 0.74) and alanine (r = 0.87) contents of the PSC fraction. Salmon with high breaking strength had higher Tpeak (temperature of transition) and ΔH (enthalpy of transition), and the collagen seemed to have triple helix structures mainly stabilized by covalent associations as compared to salmon with low breaking strength. The glycosylation degree was also positively correlated to the breaking strength (r = 0.88, p ⩽ 0.05). It is concluded that firmness of salmon muscle was not related to the total amount of collagen in the muscle, but rather higher collagen stability.