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Type: Journal article
Title: Deletion of creB in Aspergillus oryzae increases secreted hydrolytic enzyme activity
Author: Hunter, A.
Morris, T.
Jin, B.
Saint, C.
Kelly, J.
Citation: Applied and Environmental Microbiology, 2013; 79(18):5480-5487
Publisher: Amer Soc Microbiology
Issue Date: 2013
ISSN: 0099-2240
Statement of
A. J. Hunter, T. A. Morris, B. Jin, C. P. Saint, J. M. Kelly
Abstract: Aspergillus oryzae has been used in the food and beverage industry for centuries, and industrial strains have been produced by multiple rounds of selection. Targeted gene deletion technology is particularly useful for strain improvement in such strains, particularly when they do not have a well-characterized meiotic cycle. Phenotypes of an Aspergillus nidulans strain null for the CreB deubiquitinating enzyme include effects on growth and repression, including increased activity levels of various enzymes. We show that Aspergillus oryzae contains a functional homologue of the CreB deubiquitinating enzyme and that a null strain shows increased activity levels of industrially important secreted enzymes, including cellulases, xylanases, amylases, and proteases, as well as alleviated inhibition of spore germination on glucose medium. Reverse transcription-quantitative PCR (RT-qPCR) analysis showed that the increased levels of enzyme activity in both Aspergillus nidulans and Aspergillus oryzae are mirrored at the transcript level, indicating transcriptional regulation. We report that Aspergillus oryzae DAR3699, originally isolated from soy fermentation, has a similar phenotype to that of a creB deletion mutant of the RIB40 strain, and it contains a mutation in the creB gene. Collectively, the results for Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, and Penicillium decumbens show that deletion of creB may be broadly useful in diverse fungi for increasing production of a variety of enzymes.
Keywords: Spores, Fungal
Aspergillus nidulans
Aspergillus oryzae
Gene Expression Profiling
Gene Deletion
Real-Time Polymerase Chain Reaction
Ubiquitin-Specific Proteases
Rights: Copyright © 2013, American Society for Microbiology. All Rights Reserved.
DOI: 10.1128/AEM.01406-13
Grant ID:
Appears in Collections:Aurora harvest 4
Molecular and Biomedical Science publications

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