Multiple proteases from Streptomyces moderatus. II. Physicochemical and enzymatic properties of the extracellular proteases.
The physicochemical and enzymatic properties of five different extracellular proteases of Streptomyces moderatus were studied. The first protease was found to be a metal chelator sensitive protease with a Mr of 21,000 +/- 1000 a and a pI of 4.6. The second enzyme was an anionic trypsin-like protease (Mr 19,000 +/- 1000; pI 3.8) with a Km value of 4.76 X 10(-4) M on N-benzoyl-L-arginine-p-nitroanilide. A Km value of 1.52 X 10(-4) M was obtained when N-benzoyl-L-arginine ethyl ester was used as the substrate. The other three enzymes were found to be serine alkaline proteases with Mr's of 22,000, 29,000, and 23,000 +/- 1000 and with respective pI's of 7.8, 8.4, and 9.2. All the proteases showed optimum activity in the alkaline pH range. One of the three proteases was found to possess chymotrypsin and elastase-like properties. All five proteases were found to be unstable at temperatures above 60 degrees C. Except the trypsin-like protease, which was stable only in acidic pH, all other enzymes were found to be stable over a wide range of pH.
Chandrasekaran
S
S
Biochemistry Laboratory, Central Leather Research Institute, Madras, India.
Dhar
S C
SC
D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013816:Thermodynamics
D011480:Protease Inhibitors; D010447:Peptide Hydrolases