The relationship between the stability of lysozymes mutated at the inside hydrophobic core and secretion was investigated to understand the optimal secretion of mutant lysozymes in the Saccharomyces cerevisiae. S91T mutant lysozyme increased in the methyl residue inside the core greatly increased the conformational stability. The secretion amount of S91T in S. cerevisiae increased greatly compared with wild-type lysozyme. On the other hand, I55V and T40S/I55V mutant lysozymes decreased in methyl residue inside the core brought about their unstable conformation. The secretion amounts of these unstable mutant lysozymes significantly decreased. In addition, the effect of glycosylation on the secretion of these mutants was investigated. The secretion amounts of glycosylated lysozyme S91T/G49N with stable hydrophobic core greatly increased compared with that of glycosylated lysozyme G49N, while those of mutant I55V/G49N and T40S/I55V/G49N with unstable hydrophobic core greatly decreased. These results indicate that the secretion amounts of mutant lysozymes increase in proportion to the hydrophobic core stabilities and that a similar good correlation was obtained with glycosylated lysozymes.

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Journal Article

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Song Y, Sakai J, Saito A, Usui M, Azakami H, Kato A

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