M

939 T r C

236 Val r Ala

Note: The mutagenized DCase genes of thermostable enzyme-producing strains were analyzed and the locations of the nucleotide changes were determined. The amino acid substitutions resulting from the mutations were deduced.

Note: The mutagenized DCase genes of thermostable enzyme-producing strains were analyzed and the locations of the nucleotide changes were determined. The amino acid substitutions resulting from the mutations were deduced.

sured (Table 5). The thermostabilities of the enzymes increased cumulatively with the accumulation of the individual mutations. Among the mutant enzymes with two amino acid changes, a mutant with mutations of the 203rd amino acid, proline, to glutamate, and the 236th, valine, to alanine, showed a thermostability increase of about 17 °C. Among the mutant enzymes with three amino acid changes, a mutant enzyme from KNK455M that had mutations of the 57th amino acid to tyrosine, the 203rd to glutamate, and the 236th to alanine, showed about 19 °C increase in thermostability.

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