Summary
The aspartic protease gene of a zygomycete fungus Mucor pusillus was expressed in Saccharomyces cerevisiae under the control of the yeast GAL7 promoter. A putative preproenzyme with an NH2-terminal extension of 66 amino acids directed by the gene was processed in yeast cells and the mature enzyme, whose NH2-terminus was identical to that of the Mucor enzyme, was efficiently secreted into the medium at a concentration exceeding 150 mg/l. The enzyme secreted from the recombinant yeast was more glycosylated than the native Mucor enzyme but its enzymatic properties were almost identical with those of the native enzyme, which has been used as a milk coagulant in cheese manufacture.
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Yamashita, T., Tonouchi, N., Uozumi, T. et al. Secretion of Mucor rennin, a fungal aspartic protease of Mucor pusillus, by recombinant yeast cells. Mol Gen Genet 210, 462–467 (1987). https://doi.org/10.1007/BF00327198
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DOI: https://doi.org/10.1007/BF00327198