Proteolytic activity of from strains of Pseudomonas on crude extracts of contractile proteins

Citation
E. Alanis et al., Proteolytic activity of from strains of Pseudomonas on crude extracts of contractile proteins, FOOD CHEM, 67(1), 1999, pp. 45-51
Citations number
22
Categorie Soggetti
Food Science/Nutrition
Journal title
FOOD CHEMISTRY
ISSN journal
03088146 → ACNP
Volume
67
Issue
1
Year of publication
1999
Pages
45 - 51
Database
ISI
SICI code
0308-8146(199910)67:1<45:PAOFSO>2.0.ZU;2-U
Abstract
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.