Hydrolytic activities of exogenous proteases obtained from Pseudomonas upon
crude extracts of contractile proteins were studied. Four strains were use
d: C61 and C20, isolated from beef samples, and P. fragi (ATCC-4973) and P.
fluorescens (NRRL-B-1244). Proteolytic activity was tested on crude extrac
ts of actomyosin, myosin + actin + regulatory proteins, actin and high mole
cular weight proteins obtained from postrigor beef by differential precipit
ation according to their solubility in salt solutions of various ion streng
ths. Electrophoresis analysis showed considerable degradation of actomyosin
in samples treated with a C61 enzymatic extract. Myosin degradation was si
milar for treatments with proteases obtained from C61 and P. fragi. Actin d
egradation was similar for all enzymatic extracts. The most active protease
was a 46.8 kDa enzyme produced by C60. P. fragi produced two proteases of
49.2 kDa and 34.2 kDa, P. fluorescens one of 46.1 kDa, and C20 one of 49.2
kDa. (C) 1999 Elsevier Science Ltd. All rights reserved.