Abstract
Actin and myosin are the most important contrac- tile proteins in the muscle. Numerous authors developed different methods for isolation and purification of myofibril- lar proteins. The aim of this study was to obtain suitable actin and myosin extracts from post-rigor porcine muscle to be used in further studies, such as testing the proteolytic activity of microbial cultures. Actin and myosin were quantified in the extracts using spectrophotometric methods, yielding 0.17 and 0.22 mg/mL, respectively. The isolation methods pro- posed in this study provided low contaminated extracts, showing purity percentages of 74.36 % in the case of actin and 65.43 % for myosin, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Subsequently, these extracts were sterilized through a 0.22-μm polyvinyli- dene difluoride filter with no significant retention observed. In conclusion, the procedures described in this work for actin and myosin isolation can be recommended for microbiolog- ical studies requiring sterilized pure muscle proteins extracts.
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