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

• Published in: Food Chemistry
• Main Authors: Moreno Conde, Helena María, Montero García, Pilar, Gómez Guillén, M. C., Fernández Martín, Fernando, Mørkøre, T., Borderías, A. Javier
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 2012
• Subjects: Atlantic salmon; Salmo salar
• Online Access: http://hdl.handle.net/10261/58605; https://doi.org/10.1016/j.foodchem.2012.02.160

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 T peak (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. © 2012 Elsevier Ltd. All rights reserved. Peer Reviewed