Purification and some properties of achromobacter protease ia from achromobacter lyticus m497 1
Masaki, T.; Suzuki, H.; Soejima, M.
Agricultural and Biological Chemistry 50(12): 3087-3092
1986
ISSN/ISBN: 0002-1369 DOI: 10.1080/00021369.1986.10867886
Accession: 006230908
A protease with strict specificity to lysyl peptide bonds like that of Achromobacter protease I was purified from a crude enzyme powder obtained from a culture filtrate of Achromobacter lyticus M497-1 and characterized. The purified enzyme had the following differences from protease I. The enzyme had an isoelectric point of 5.3, lower than the value of 6.9 for protease I. The amino acid composition of the enzyme had higher proportions of His, Glu, and Gly and lower proportions of Arg and Thr protease I. The enzyme was unstable (30% residual activity) in the presence of 7 M urea (pH 8.0, 30.degree.C, 20 min); protease I was resistant to the same conditions (80% residual activity). The kcat/Km values for the hydrolysis of Tos-Lys-OMe and Lys-pNA by the enzyme were lower than those of protease I.