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Decorin and fibromodulin expression in two bovine muscles (M. Semitendinosus and M. Psoas Major) differing in texture

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Kjetil Aune

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kjetil.aune@nofima.no

Journal of Muscle Foods ; Volume 12. p. 1–17. 2001

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

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.

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