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Saccharomyces cerevisiae  is a robust host for heterologous protein expression. The efficient expression of cellulases in  S. cerevisiae  is important for the consolidated bioprocess that directly converts lignocellulose into valuable products. However, heterologous proteins are often  N -hyperglycosylated in  S. cerevisiae , which may affect protein activity. In this study, the expression of three heterologous proteins, β-glucosidase, endoglucanase and cellobiohydrolase, was found to be  N -hyperglycosylated in  S. cerevisiae . To block the formation of hypermannose glycan, these proteins were expressed in strains with deletions in key Golgi mannosyltransferases (Och1p, Mnn9p and Mnn1p), respectively. Their extracellular activities improved markedly in the  OCH1  and  MNN9  deletion strains. Interestingly, truncation of the  N -hypermannose glycan did not increase the specific activity of these proteins, but improved the secretion yield. Further analysis showed  OCH1  and  MNN9  deletion up-regulated genes in the secretory pathway, such as protein folding and vesicular trafficking, but did not induce the unfolded protein response. The cell wall integrity was also affected by  OCH1  and  MNN9  deletion, which contributed to the release of secretory protein extracellularly. This study demonstrated that mannosyltransferases disruption improved protein secretion through up-regulating secretory pathway and affecting cell wall integrity and provided new insights into glycosylation engineering for protein secretion.

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N-hypermannose glycosylation disruption enhances recombinant protein production by regulating secretory pathway and cell wall integrity in Saccharomyces cerevisiae