Proteases are enzymes that hydrolyze proteins into smaller pieces by breaking the peptide bonds. Protease enzyme is produced by all living things on Earth. Pseudomonas sp. KE-38 is a cold adapted bacterium isolated from soil at high altitude in Erciyes mountain, Kayseri. The purpose of this thesis was to clone the cold-active extracellular protease gene from Pseudomonas sp. KE-38, partial purification and characterization of the extracellular protease enzyme. The partial sequence of protease gene from Pseudomonas sp. KE-38 was analysed. The estimated size encoded by this gene after sequence analysis was 105 kDa. However, the size of this enzyme that was purified in this thesis was found to be approximately 50 kDa as evaluated of gelatine zymography analysis. Further investigation of the proteins in the partially purified enzyme sample by Liquid Chromatography Mass Spectrophotometry, revealed the presence of a metalloprotease enzyme with a predicted mass of 50 kDa. These results showed that the purified and characterised protease enzyme was not the same enzyme of which its gene was amplified gene was amplified and sequenced. Nevertheless, the partial characterization of the extracellular metalloprotease was performed, and the optimum temperature and pH was found to be 30°C and 8.0 respectively. The enzyme showed high activity in the presence of calcium, ethanol. The enzyme showed extremely high stability up to 25°C above this temperature; the stability dropped sharply which confirmed that the protease was a cold active enzyme and can have a potential to be used in cold temperature applications.