Heat-labile proteases in molecular biology applications |
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Authors: | Moran A J Hills M Gunton J Nano F E |
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Affiliation: | Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, V8W 3P6, Victoria, BC, Canada. |
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Abstract: | Thermolabile proteases were identified in three Gram-negative psychrotrophic bacteria. The protease from the psychrotrophic strain A9 was purified and its application to common molecular biology techniques was demonstrated. Heat-stable molecular biology enzymes (Taq polymerase and PvuII) were digested by a heat-labile protease, which was then inactivated by a mild heat treatment. The clear benefit of using heat-labile proteases arises in situations where further reactions may be accomplished without an intermediate purification step, thereby saving time and avoiding the possibility of product loss. |
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Keywords: | Protease Psychrotrophic bacterium Polymerase chain reaction Molecular biology |
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