초록
<P><B>ABSTRACT</B></P><P>Recombinant yeast strains displaying aheterologous cellulolytic enzymes on their cell surfaces using a glycosylphosphatidylinositol (GPI) anchoring system are a promising strategy for bioethanol production from lignocellulosic materials. A crucial step for cell wall localization of the enzymes is the intracellular transport of proteins in yeast cells. Therefore, the addition of a highly efficient secretion signal sequence is important to increase the amount of the enzymes on the yeast cell surface. In this study, we demonstrated the effectiveness of a novel signal peptide (SP) sequence derived from the <I>Saccharomyces cerevisiae SED1</I> gene for cell‐surface display and secretory production of cellulolytic enzymes. Gene cassettes with SP sequences derived from <I>S. cerevisiae SED1</I> (<I>SED1</I>SP), <I>Rhizopus oryzae</I> glucoamylase (<I>GLUA</I>SP), and <I>S. cerevisiae</I> α‐mating pheromone (<I>MFα1</I>SP) were constructed for cell‐surface display of <I>Aspergillus aculeatus</I> β‐glucosidase (BGL1) and <I>Trichoderma reesei</I> endoglucanase II (EGII). These gene cassettes were integrated into the <I>S. cerevisiae</I> genome. The recombinant strains with the <I>SED1</I>SP showed higher cell‐surface BGL and EG activities than those with the conventional SP sequences (<I>GLUA</I>SP and <I>MFα1</I>SP). The novel SP sequence also improved the secretory production of BGL and EG in <I>S. cerevisiae</I>. The extracellular BGL activity of the recombinant strains with the <I>SED1</I>SP was 1.3‐ and 1.9‐fold higher than the <I>GLUA</I>SP and <I>MFα1</I>SP strains, respectively. Moreover, the utilization of <I>SED1</I>SP successfully enhanced the secretory production of BGL in <I>Pichia pastoris</I>. The utilization of the novel SP sequence is a promising option for highly efficient cell‐surface display and secretory production of heterologous proteins in various yeast species. Biotechnol. Bioeng. 2016;113: 2358–2366. © 2016 Wiley Periodicals, Inc.</P>