is a biotechnologically important filamentous fungus with the remarkable ability to secrete large amounts of enzymes, whose production is strongly affected by both the carbon and nitrogen sources. While the carbon metabolism regulators are extensively studied, the regulation of enzyme production by the nitrogen metabolism regulators is still poorly understood. In this study, the GATA transcription factor Are1, which is an orthologue of the global nitrogen regulator AREA, was identified and characterized for its functions in regulation of both protease and cellulase production in . Deletion of the gene abolished the capability to secrete proteases, and complementation of the gene rescued the ability to produce proteases. Quantitative RT-PCR analysis revealed that the transcripts of protease genes and were also significantly reduced in the Δ strain when grown in the medium with peptone as the nitrogen source. In addition, deletion of resulted in decreased cellulase production in the presence of (NH)SO. Consistent with the reduction of cellulase production, the transcription levels of the major cellulase genes, including , , , and were dramatically decreased in Δ. Sequence analysis showed that all promoter regions of the tested protease and cellulase genes contain the consensus GATA elements. However, the expression levels of the major cellulase transcription activator Xyr1 and the repressor Cre1 had no significant difference between Δ and the parental strain QM9414, indicating that the regulatory mechanism deserves further investigation. Taken together, these results demonstrate the important role of Are1 in the regulation of protease and cellulase production in , although these processes depend on the kind of nitrogen sources. The findings in this study contribute to the understanding of the regulation network of carbon and nitrogen sources in filamentous fungi.
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http://dx.doi.org/10.3390/ijms20174100 | DOI Listing |
Int J Biol Macromol
January 2025
Forest Product Biotechnology/Bioenergy Group, Department of Wood Science, University of British Columbia, 2424 Main Mal, Vancouver V6T 1Z4, Canada. Electronic address:
Modern enzyme cocktails often include lytic polysaccharide monooxygenase (LPMO) as an accessory enzyme that enhances cellulose accessibility during hydrolysis. Although lignin is known to generally impede cellulose hydrolysis, previous research has demonstrated lignin's potential to act as a co-factor in boosting LPMO activity and that the negative impact of lignin limiting enzyme accessibility can be mitigated by sulfonated. When sulphonated lignin was added to microcrystalline cellulose (Avicel) the activity of the lytic polysaccharide monooxygenase (LPMO) was boosted, as determined when using a quartz crystal microbalance and dissipation monitoring (QCM-D).
View Article and Find Full Text PDFAppl Biochem Biotechnol
January 2025
Department of Botany, Maharshi Dayanand University, Rohtak, 124001, India.
Cellulase was effectively immobilized onto an epoxy-bound chitosan-modified zinc metal-organic framework (epoxy/ZIF-8/CS/cellulase) support, yielding a conjugation rate of 0.64 ± 0.02 mg/cm2 and retaining 80.
View Article and Find Full Text PDFFood Chem X
January 2025
College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian, PR China.
Steam explosion (SE) and cellulase treatment are potentially effective processing methods for by-products, for use in high-value applications. The treatment conditions were optimized by response surface methodology, increasing the soluble dietary fiber (SDF) yield by 1.52 and 1.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Faculty of Petroleum and Chemical Engineering, Razi University, Kermanshah, Iran. Electronic address:
Cellulase is extensively used in the biorefinery of cellulosic materials to fermentable sugars in bioethanol production. Application of cellulase in the free form has disadvantages in enzyme wastage and low stability. The results of the present work showed these drawbacks can be solved by cellulase immobilization on functionalized FeO magnetic nanoparticles (MNPs) with reactive red 120 (RR120) as the affinity ligands.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Forestry, Northwest A&F University, No.3 Taicheng Road, Yangling, Shaanxi 712100, China; Shaanxi Key Laboratory of Economic Plant Resources Development and Utilization, Yangling, Shaanxi 712100, China. Electronic address:
Crosslinked Enzyme Aggregates (CLEAs) are favored for their operational stability and recyclability. However, the traditional CLEAs preparation may distort the enzyme's active site and reduce activity. Therefore, we developed a universally applicable crosslinked SpyCatcher scaffold system designed for the facile preparation of CLEAs.
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