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SUMMARY: Mutants affected in production of alkaline extracellular protease (xpr mutants) have been characterized. The alkaline protease produced by the xpr mutants, except for that of the structural gene mutant, was indistinguishable from the wild-type protease on the basis of isoelectric focusing in polyacrylamide gels, SDS-PAGE and thermal stability. Some revertants of xpr mutants were temperature sensitive for protease production, but the thermal stability of the revertant protease was not altered. The xpr mutants grew as rapidly as the wild-type with glutamic acid, leucine or urea as sole nitrogen source. The pleiotropic xpr mutants which produced lowered levels of extracellular RNAase also produced less extracellular acid proteases (4 to 40% of wild-type). These results suggest that the pleiotropic xpr mutants may affect secretion. However, production of phosphatase(s) (which was secreted but located primarily in the cell envelope) was much less affected in these mutants (65 to 100% of wild-type). A possible explanation for these results is that at least one step (component) of the secretion pathway for the extracellular proteases and RNAases is not shared by the phosphatase(s).

Characterization of Saccharomycopsis lipolytica Mutants Producing Lowered Levels of Alkaline Extracellular Protease