Cloning and Expression as a Tool to Easily Purify a New Highly Thermostable Archaebacterial ß-Galactosidase
Since enzymes from extremophiles are thermostable they could, in theory, be purified very easily after cloning and expression of their genes in mesophiles. This paper demonstrates that the gene of a new ß-galactosidase isolated from the extreme thermophile Sulfolobus solfataricus can be cloned and expressed in E. coli under the control of the archaebacterial promoter. The recombinant enzyme is similar to the native and, as expected, can be easily purified by heat treatment and isoelectric point precipitation. The partial purification and the properties of the recombinant enzyme are described.
KeywordsRecombinant Enzyme Native Enzyme Lactose Hydrolysis Thermophilic Enzyme Thermophilic Organism
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