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Updated: May 27, 2026

Enzymatic Isolation of Skeletal Muscle Interstitial Extracellular Vesicles
Published on: February 7, 2025
Surface properties of muscle protein extracts
E O'Neill1, D M Mulvihill, P A Morrissey
1Department of Food Chemistry, University College Cork, Cork, Republic of Ireland.
Abstract:
The interfacial properties of proteins extracted from muscle using salt solutions of different concentration and for different extraction times were determined by the drop volume method. At a bulk phase concentration of 10(-2) wt%, it appears that the sarcoplasmic-rich fraction of muscle is more surface active than the salt-soluble fraction. The average equilibrium surface pressure at the air-liquid interface was 21·5 mN m(-1) for an aqueous extract and 20·1 mN m(-1) for a 1m KCl-extract. The equilibrium surface pressure decreased from 21·7 mN m(-1) to 19·50mN m(-1) as the extraction time with Weber-Edsall solution increased from 15 min to 48 h.
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