Published 2001

Read in Norwegian

Publication details

Journal : Journal of Muscle Foods , vol. 12 , p. 1–17 , 2001

Publisher : Blackwell Publishing

International Standard Numbers :
Printed : 1046-0756
Electronic : 1745-4573

Publication type : Academic article

Contributors : Pedersen, Mona Elisabeth; Kulseth, Mari Ann; Kolset, Svein Olav; Velleman, S.; Eggen, Kyrre

Issue : 1

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Kjetil Aune
Chief Librarian


Biochemical composition of muscle is an important factor that affects meat quality. Studies have revealed that the collagen content alone cannot be considered a reliable parameter for textural properties. This study focuses on the expression of two collagen interacting proteoglycans, decorin and fibromodulin, in two muscles differing in texture, M. semitendinosus (ST) and M. psoas major (PM). The difference in texture was confirmed by Warner Bratzler shear force measurements. The proteoglycan expression level was determined both on protein and mRNA level by SDS-gel electrophoresis and Northern blots, and related to the collagen expression. The tougher muscle, ST contained more decorin than the tender muscle PM, but less decorin per collagen. However, the difference in fibromodulin level per collagen was not significant between the two muscles, indicating that decorin is a better parameter to study in relation to textural properties in bovine muscle.