Purification and Properties of Cold-active Metalloprotease from Curtobacterium luteum and Effect of Culture Conditions on Production |
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Authors: | Mohammed Kuddus and Pramod W Ramteke |
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Institution: | Protein Research Laboratory, Department of Biotechnology, Integral University, Kursi Road Lucknow 226026, India;College of Biotechnology and Allied Sciences, Allahabad Agricultural Institute, Deemed University, Allahabad 211007, India |
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Abstract: | Curtobacterium luteum, a gram-positive psychrotrophic bacterium, secreting an extracellular protease was isolated from the soil of Gangotri glacier, Western Himalaya. The maximum enzyme production was achieved when isolate was grown in a pH-neutral medium containing skim milk at 15°C over 120 hour. The metal ions such as Zn2+ and Cr2+ enhanced enzyme production. The specific activity of purified enzyme was 8090 u/mg after 34.1 fold purification. The 115 kD enzyme was a metalloprotease (activity inhibited by EDTA and EGTA) and showed maximum activity at 20°C and pH 7. The enzyme was active over a broad pH range and retained 84% of its original activity between pH 6–8. There was no loss in enzyme activity when exposed for 3 hours at 4°C–20°C. However, lost 65% of activity at 30°C, and was almost inactivated at 50°C, but was resistant to repeated freezing and thawing. The enzyme activity was stimulated by manganese ions; however, it was inactivated by copper ions. |
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Keywords: | enzymes cold-active metalloprotease Curtobacterium luteum Gangotri glacier |
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