species are capable of producing various active metabolites, including monacolin K (MK) and pigments. Studies have shown that the overexpression of the gene from the MK synthesis gene cluster in species can significantly increase MK production; however, the molecular mechanism has not yet been fully elucidated. Therefore, this study focused on the gene of to construct overexpression strains of the gene, resulting in high-yield MK production.
View Article and Find Full Text PDFGlycerol dehydrogenase has been identified and characterized functionally in many species. However, little is known about glycerol dehydrogenase genes and their functions in Aspergillus oryzae. Here, a total of 45 glycerol dehydrogenase genes in Aspergillus oryzae were identified and renamed from AoGld1 to AoGld45 according to their chromosome distribution.
View Article and Find Full Text PDFPreviously, the alpha amylase-encoding gene from was heterologously expressed in CICC41233 to promote starch hydrolysis and increase the production of pigments. The target of this study is to screen the effective alpha-amylases from for starch fast degradation and investigated for pigments production. The 13 types of predicted alpha-amylases in the NRRL1597 genome were divided into four classes based on EC number and into five groups based on the glycoside hydrolase sub-family.
View Article and Find Full Text PDFThe ZRT, IRT-like protein (ZIP) family exists in many species and plays an important role in many biological processes, but little is known about ZIP genes in Aspergillus oryzae. Here, 10 ZIP genes in A. oryzae were identified and these were classified into four groups based on phylogenetic analysis.
View Article and Find Full Text PDFMonacolin K (MK) is the principal active substance in Monascus-fermentation products (e.g. red yeast rice).
View Article and Find Full Text PDFTo investigate the relationship between starch hydrolysis and pigments (MPs) production, the α-amylase gene () from was heterologously expressed in CICC41233, and we obtained a positive transformant named Amy9. In Amy9, the α-amylase activities were 6.65- and 4.
View Article and Find Full Text PDFThe present study verified whether acyl-coenzyme A (acyl-CoA)-binding protein (ACBP) affected the production of pigments (MPs) in CICC41233 (MrACBP). Phylogenetic analysis revealed that the cloned gene, which encoded the MrACBP protein, exhibited the closest match (99% confidence level) to the gene from . The MrACBP and maltose-binding protein (MBP) were simultaneously expressed in Rosetta DE3 in the form of a fusion protein.
View Article and Find Full Text PDFThe goal of this study was to enhance the production of xylooligosaccharides (XOs) and reduce the production of xylose. We investigated β-xylosidases, which were key enzymes in the hydrolysis of xylan into xylose, in EU7-22. The binary vector pUR5750G/:: was constructed to knock out the - gene (encoding β-xylosidases) in EU7-22 by homologous integration, producing the mutant strain Bxyl-1.
View Article and Find Full Text PDFThe role of the transcription factor creA-mediating carbon catabolite repression in Trichoderma orientalis EU7-22 was investigated for cellulase and hemicellulase production. The binary vector pUR5750G/creA::hph was constructed to knock out creA by homologous integration, generating the ΔcreA mutant Trichoderma orientalis CF1D. For strain CF1D, the filter paper activities (FPA), endoglucanase activities (CMC), cellobiohydrolase activity(CBH), β-glucosidase activity (BG), xylanase activity (XYN), and extracellular protein concentration were 1.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
January 2018
Characterization of the changes after various stimuli is crucial to comprehend the adaptation of cells to the changing condition. Aspergillus oryzae is widely used for the industrial production of soy sauce, which always encounter changes within a complex environment, such as salinity stress. However, the protective biochemical mechanisms of A.
View Article and Find Full Text PDFHPLC using pre-column derivatization with 1-phenyl-3-methyl-5-pyrazolone (PMP) was used to analyse mono-saccharides and oligo-saccharides in hydrolysates of lignocellulosic biomass. PMP derivatives, including those of mannose, rhamnose, cellobiose, glucose, xylose and arabinose, were separated within 14 min with detection at 254 nm. The method was also suitable for xylo-oligosaccharides (XOS): PMP derivatives of xylohexaose, xylopentaose, xylotetraose, xylotriose and xylobiose were well separated under the same conditions.
View Article and Find Full Text PDFA high concentration of glucose in the medium could greatly inhibit the expression of cellulase in filamentous fungi. The aspartic protease from fungus Hypocrea orientalis EU7-22 could efficiently express under both induction condition and glucose repression condition. Based on the sequence of structure gene of aspartic protease, the upstream sequence harboring the putative promoter proA for driving the expression of aspartic protease was obtained by genome walking.
View Article and Find Full Text PDFTo produce cellulolytic enzyme efficiently, Penicillium decumbens strain L-06 was used to prepare mutants with ethyl methane sulfonate (EMS) and UV-irradiation. A mutant strain ML-017 is shown to have a higher cellulase activity than others. Box-Behnken's design (BBD) and response surface methodology (RSM) were adopted to optimize the conditions of cellulase (filter paper activity, FPA) production in strain ML-017 by solid-state fermentation (SSF) with rice bran as the substrate.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
June 2008
Cellulases are relatively costly enzymes that are sold in large volumes for use in different industrial applications, and a significant reduction in cost will be important for their commercial use in biorefineries. The production of cellulase is a major factor in the hydrolysis of cellulosic materials. Hence it is essential to make the process economically viable.
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