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Title: Protein hyperproduction in fungi by design

Journal Article · · Applied Microbiology and Biotechnology

The secretion of enzymes used by fungi to digest their environment has been exploited by humans for centuries for food and beverage production. More than a century after the first biotechnology patent, we know that the enzyme cocktails secreted by these amazing organisms have tremendous use across a number of industrial processes. Secreting the maximum titer of enzymes is critical to the economic feasibility of these processes. Traditional mutagenesis and screening approaches have generated the vast majority of strains used by industry for the production of enzymes. Until the emergence of economical next generation DNA sequencing platforms, the majority of the genes mutated in these screens remained uncharacterized at the sequence level. In addition, mutagenesis comes with a cost to an organism’s fitness, making tractable rational strain design approaches an attractive alternative. As an alternative to traditional utagenesis and screening, controlled manipulation of multiple genes involved in processes that impact the ability of a fungus to sense its environment, regulate transcription of enzyme-encoding genes, and efficiently secrete these proteins will allow for rational design of improved fungal protein production strains.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
AC05-76RL01830; AC02-05CH11231; AC0576RL01830
OSTI ID:
1463032
Alternate ID(s):
OSTI ID: 1468613; OSTI ID: 1513534
Report Number(s):
PNNL-SA-137094; PII: 9265
Journal Information:
Applied Microbiology and Biotechnology, Journal Name: Applied Microbiology and Biotechnology; ISSN 0175-7598
Publisher:
SpringerCopyright Statement
Country of Publication:
Germany
Language:
English
Citation Metrics:
Cited by: 8 works
Citation information provided by
Web of Science

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