Author： Koma Daisuke Sawai Toshiya Harayama Shigeaki Kino Kuniki
Publisher： Springer Publishing Company
ISSN： 0175-7598
Source： Applied Microbiology and Biotechnology, Vol.73, Iss.1, 2006-11, pp. : 172-180
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Abstract
Twenty-nine aminotransferase genes from Pyrococcus horikoshii</i>, Aeropyrum pernix</i>, and Sulfolobus tokodaii</i> were cloned and expressed in Escherichia coli</i>. The expression of several of the genes at 15, 25, or 37 °C resulted in the formation of insoluble protein aggregates. Therefore, we developed a simple method to express these genes into soluble proteins, by cultivating E</i>. coli</i> clones at a higher temperature. Thus, four genes could be expressed efficiently into soluble and active enzymes by cultivating the respective E</i>. coli</i> clones at 46 °C. Subsequently, the method was applied to the expression into soluble proteins of other aminotransferase genes that were derived from nine species of thermophilic microorganisms.
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