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The Molecular Biology of Secreted Enzyme Production by Fungi
Abstract
Enzymes from filamentous fungi are already widely exploited, but new applications for known enzymes and new enzymic activities continue to be found. In addition, enzymes from less amenable non-fungal sources require heterologous production and fungi are being used as the production hosts. In each case there is a need to improve production and to ensure quality of product. While conventional, mutagenesis-based, strain improvement methods will continue to be applied to enzyme production from filamentous fungi the application of recombinant DNA techniques is beginning to reveal important information on the molecular basis of fungal enzyme production and this knowledge is now being applied both in the laboratory and commercially. We review the current state of knowledge on the molecular basis of enzyme production by filamentous fungi. We focus on transcriptional and post-transcriptional regulation of protein production, the transit of proteins through the secretory pathway and the structure of the proteins produced including glycosylation.
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Citations
Cited by
(2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00075 · Cited by 1,611
Growth of Filamentous Fungi in Submerged Culture: Problems and Possible Solutions
Gibbs, P. A., Seviour, R. J., & Schmid, F. (2000) · Critical Reviews in Biotechnology · doi:10.1080/07388550091144177 · Cited by 329
Tucker, S. C., & Casadevall, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052702799 · Cited by 306
The Secretion Pathway in Filamentous Fungi: A Biotechnological View
Conesa, A., Punt, P. J., van Luijk, N., & van den Hondel, C. A. M. J. J. (2001) · Fungal Genetics and Biology · doi:10.1006/fgbi.2001.1276 · Cited by 274
Metadata
- Authors
- Archer, D. B., & Peberdy, J. F.
- Venue
- Critical Reviews in Biotechnology
- Publisher
- Informa UK Limited
- Published
- 1997-01
- Volume
- 17
- Issue
- 4
- Pages
- 273-306
- ISSN
- 0738-8551 (ISSN-L)
- 1549-7801
- OpenAlex
- W1975044278
- Cited by
- 208
- References
- 0
- FWCI
- 2.92
- Type
- journal article
- Language
- en
- Open access
- closed
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