Abstract
The cDNA copies of the two endo‐β‐1,4‐glucanase genes, egl1 and egl3, from the filamentous fungus Trichoderma reesei were expressed in yeast Saccharomyces cerevisiae under the control of the yeast phosphoglycerate kinase gene promoter. Active EGI and EGIII enzyme was produced and secreted by yeast into the growth medium. The recombinant EGI enzyme was larger and more heterogeneous in size than the native enzyme secreted by Trichoderma, due to differences in the extent of N‐glycosylation between these two organisms. The morphology of the yeast cells producing EGI or EGIII was clearly different from control strain. Copyright © 1987 John Wiley & Sons Ltd.
| Original language | English |
|---|---|
| Pages (from-to) | 175-185 |
| Number of pages | 11 |
| Journal | Yeast |
| Volume | 3 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Sept 1987 |
| MoE publication type | A1 Journal article-refereed |
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