A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): enzyme production and characterization.
A novel psychro-tolerant bacterium, Curtobacterium luteum, secreting an extracellular protease was isolated from the soil of Gangotri glacier, Western Himalaya. Maximum enzyme production was achieved when the strain was grown in a pH-neutral medium containing skim milk at 15 degrees C over 120 h. The metal ions such as Zn(2+) and Cr(2+) enhanced enzyme production. The specific activity of purified enzyme was 8,090 units/mg after 34.1-fold purification. The 115 kDa enzyme was a metalloprotease (activity inhibited by EDTA and EGTA) and showed maximum activity at 20 degrees C and pH 7. The enzyme was active over a broad pH range and retained 84% of its original activity between pH 6 and 8. There was no loss in enzyme activity when exposed for 3 h at 4-20 degrees C. However, the enzyme lost 65% of activity at 30 degrees C, and was almost inactivated at 50 degrees C, but was resistant to repeated freezing and thawing. The enzyme activity was stimulated by manganese ions; however, it was inactivated by copper ions.
Kuddus
Mohammed
M
Department of Biotechnology, Integral University, Lucknow, India. kuddus_biotech@yahoo.com
Ramteke
Pramod W
PW
D000192:Actinomycetales / Q000201:enzymology* / Q000302:isolation & purification*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D003080:Cold Temperature; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D046448:Ice Cover; D007194:India; D008274:Magnesium / Q000378:metabolism; D045726:Metalloproteases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D012988:Soil Microbiology
D001426:Bacterial Proteins; D045726:Metalloproteases; D008274:Magnesium