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Danielle Julie Carrier - One of the best experts on this subject based on the ideXlab platform.
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statistical approach for the identification of Cellulolytic Enzyme inhibitors using switchgrass dilute acid prehydrolyzates as a model system
ACS Sustainable Chemistry & Engineering, 2018Co-Authors: Angele Djioleu, Danielle Julie CarrierAbstract:The identification of biomass pretreatment-generated compounds that impede cellulose hydrolysis is critical for improving the overall biomass saccharification process. The aim of this study was to correlate the identification and concentrations of switchgrass dilute acid pretreatment-generated compounds to Cellulolytic Enzyme inhibition and to tie this back to processing parameters. Preparation of 24 dilute acid prehydrolyzates was performed with switchgrass at temperatures from 140 to 180 °C, processing times from 10 to 40 min, and sulfuric acid concentrations of 0.5% or 1% (v/v). Results showed that all the switchgrass prehydrolyzates significantly reduced Cellulolytic Enzyme activities when assayed against model substrates. Exoglucanase was the most sensitive with its activity reduction, ranging from 58% to 88%; the inhibitory effect on β-glucosidase and the cellulase cocktail ranged from 32% to 63% and 16% to 41%, respectively. Polyphenolic compounds were the most detrimental pretreatment-generated pr...
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Statistical Approach for the Identification of Cellulolytic Enzyme Inhibitors Using Switchgrass Dilute Acid Prehydrolyzates as a Model System
2018Co-Authors: Angele Djioleu, Danielle Julie CarrierAbstract:The identification of biomass pretreatment-generated compounds that impede cellulose hydrolysis is critical for improving the overall biomass saccharification process. The aim of this study was to correlate the identification and concentrations of switchgrass dilute acid pretreatment-generated compounds to Cellulolytic Enzyme inhibition and to tie this back to processing parameters. Preparation of 24 dilute acid prehydrolyzates was performed with switchgrass at temperatures from 140 to 180 °C, processing times from 10 to 40 min, and sulfuric acid concentrations of 0.5% or 1% (v/v). Results showed that all the switchgrass prehydrolyzates significantly reduced Cellulolytic Enzyme activities when assayed against model substrates. Exoglucanase was the most sensitive with its activity reduction, ranging from 58% to 88%; the inhibitory effect on β-glucosidase and the cellulase cocktail ranged from 32% to 63% and 16% to 41%, respectively. Polyphenolic compounds were the most detrimental pretreatment-generated products to the Cellulolytic Enzymes, especially to exoglucanase. Limited Enzyme inhibition, with acceptable biomass digestibility, was observed with pretreatment conditions corresponding to 160 °C. The statistically based approach used in this study proved to be a valid method to assess the effect of pretreatment-generated compounds on Cellulolytic Enzyme activities, linking their generation to pretreatment processing parameters
Verawat Champreda - One of the best experts on this subject based on the ideXlab platform.
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designing Cellulolytic Enzyme systems for biorefinery from nature to application
Journal of Bioscience and Bioengineering, 2019Co-Authors: Verawat Champreda, Tatsuya Fujii, Hiroyuki Inoue, Benjarat Bunterngsook, Wuttichai Mhuantong, Hataikarn Lekakarn, Pattanop Kanokratana, Xinqing Zhao, Fei Zhang, Lily EurwilaichitrAbstract:Cellulolytic Enzymes play a key role on conversion of lignocellulosic plant biomass to biofuels and biochemicals in sugar platform biorefineries. In this review, we survey composite carbohydrate-active Enzymes (CAZymes) among groups of Cellulolytic fungi and bacteria that exist under aerobic and anaerobic conditions. Recent advances in designing effective cellulase mixtures are described, starting from the most complex microbial consortium-based Enzyme preparations, to single-origin Enzymes derived from intensively studied cellulase producers such as Trichoderma reesei, Talaromyces Cellulolyticus, and Penicellium funiculosum, and the simplest minimal Enzyme systems comprising selected sets of mono-component Enzymes tailor-made for specific lignocellulosic substrates. We provide a comprehensive update on studies in developing high-performance cellulases for biorefineries.
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characterization of Cellulolytic Enzyme system of schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis
Bioscience Biotechnology and Biochemistry, 2017Co-Authors: Warasirin Sornlake, Lily Eurwilaichitr, Verawat Champreda, Phatcharamon Rattanaphanjak, Suthathip Kittisenachai, Sittiruk Roytrakul, Tatsuya Fujii, Hiroyuki InoueAbstract:Schizophyllum commune is a basidiomycete equipped with an efficient Cellulolytic Enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading Enzymes from S. commune mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and β-glucosidase were obtained on Avicel-PH101 while a wider range of Enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex Enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox Enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an Enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by add...
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Characterization of Cellulolytic Enzyme system of Schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis
2017Co-Authors: Warasirin Sornlake, Lily Eurwilaichitr, Verawat Champreda, Phatcharamon Rattanaphanjak, Suthathip Kittisenachai, Sittiruk Roytrakul, Tatsuya Fujii, Hiroyuki InoueAbstract:Schizophyllum commune is a basidiomycete equipped with an efficient Cellulolytic Enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading Enzymes from S. commune mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and β-glucosidase were obtained on Avicel-PH101 while a wider range of Enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex Enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox Enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an Enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by addition external β-xylosidase. Enzymatic hydrolysis of alkaline-pretreated biomass by Sc-Cel and yield enhancement by external β-xylosidase (BX).
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biochemical characterization and synergism of Cellulolytic Enzyme system from chaetomium globosum on rice straw saccharification
BMC Biotechnology, 2016Co-Authors: Wanwitoo Wanmolee, Warasirin Sornlake, Nakul Rattanaphan, Surisa Suwannarangsee, Navadol Laosiripojana, Verawat ChampredaAbstract:Efficient hydrolysis of lignocellulosic materials to sugars for conversion to biofuels and chemicals is a key step in biorefinery. Designing an active saccharifying Enzyme system with synergy among their components is considered a promising approach. In this study, a lignocellulose-degrading Enzyme system of Chaetomium globosum BCC5776 (CG-Cel) was characterized for its activity and proteomic profiles, and synergism with accessory Enzymes. The highest cellulase productivity of 0.40 FPU/mL was found for CG-Cel under the optimized submerged fermentation conditions on 1% (w/v) EPFB (empty palm fruit bunch), 2% microcrystalline cellulose (Avicel®) and 1% soybean meal (SBM) at 30 °C, pH 5.8 for 6 d. CG-Cel worked optimally at 50–60 °C in an acidic pH range. Proteomics analysis by LC/MS/MS revealed a complex Enzyme system composed of core cellulases and accessory hydrolytic/non-hydrolytic Enzymes attacking plant biopolymers. A synergistic Enzyme system comprising the CG-Cel, a β-glucosidase (Novozyme® 188) and a hemicellulase Accellerase® XY was optimized on saccharification of alkaline-pretreated rice straw by a mixture design approach. Applying a full cubic model, the optimal ratio of ternary Enzyme mixture containing CG-Cel: Novozyme® 188: Accellerase® XY of 44.4:20.6:35.0 showed synergistic enhancement on reducing sugar yield with a glucose releasing efficiency of 256.4 mg/FPU, equivalent to a 2.9 times compared with that from CG-Cel alone. The work showed an approach for developing an active synergistic Enzyme system based on the newly characterized C. globosum for lignocellulose saccharification and modification in bio-industries.
Hiroyuki Inoue - One of the best experts on this subject based on the ideXlab platform.
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designing Cellulolytic Enzyme systems for biorefinery from nature to application
Journal of Bioscience and Bioengineering, 2019Co-Authors: Verawat Champreda, Tatsuya Fujii, Hiroyuki Inoue, Benjarat Bunterngsook, Wuttichai Mhuantong, Hataikarn Lekakarn, Pattanop Kanokratana, Xinqing Zhao, Fei Zhang, Lily EurwilaichitrAbstract:Cellulolytic Enzymes play a key role on conversion of lignocellulosic plant biomass to biofuels and biochemicals in sugar platform biorefineries. In this review, we survey composite carbohydrate-active Enzymes (CAZymes) among groups of Cellulolytic fungi and bacteria that exist under aerobic and anaerobic conditions. Recent advances in designing effective cellulase mixtures are described, starting from the most complex microbial consortium-based Enzyme preparations, to single-origin Enzymes derived from intensively studied cellulase producers such as Trichoderma reesei, Talaromyces Cellulolyticus, and Penicellium funiculosum, and the simplest minimal Enzyme systems comprising selected sets of mono-component Enzymes tailor-made for specific lignocellulosic substrates. We provide a comprehensive update on studies in developing high-performance cellulases for biorefineries.
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development of tailor made synergistic Cellulolytic Enzyme system for saccharification of steam exploded sugarcane bagasse
Journal of Bioscience and Bioengineering, 2017Co-Authors: Benjarat Bunterngsook, Tatsuya Fujii, Hiroyuki Inoue, Thanaporn Laothanachareon, Chayanon Chotirotsukon, Tamotsu Hoshino, Niran Roongsawang, Sanchai Kuboon, Wasawat Kraithong, Wikanda TechananAbstract:Designing a tailor-made synergistic system is a promising strategy for developing an effective Enzyme for saccharification of lignocellulosic materials. In this study, a Cellulolytic Enzyme mixture comprising selected core recombinant Enzymes for hydrolysis of sugarcane bagasse pretreated by alkaline-catalyzed steam explosion was optimized using a mixture design approach. The optimized Enzyme system comprised a cellobiohydrolase (Cel7A) from Talaromyces Cellulolyticus, an endo-glucanase (Cel7B) from Thielavia terrestris, a β-glucosidase (BGL) and an endo-β1,4-xylanase (XYN) from Aspergillus aculeatus at the ratio of 0.34:0.27:0.14:0.25. The maximum reducing sugar yield of 797 mg/g biomass, comprising 543 and 96.8 mg/g glucose and xylose, respectively were achieved, equivalent to 92.44% and 47.50% recoveries, respectively from the pretreated substrate at the Enzyme dosage of 20 mg/g biomass. The sugar yield from the quaternary Enzyme mixture was 17.37% higher than that obtained with Accellerase 1500.
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characterization of Cellulolytic Enzyme system of schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis
Bioscience Biotechnology and Biochemistry, 2017Co-Authors: Warasirin Sornlake, Lily Eurwilaichitr, Verawat Champreda, Phatcharamon Rattanaphanjak, Suthathip Kittisenachai, Sittiruk Roytrakul, Tatsuya Fujii, Hiroyuki InoueAbstract:Schizophyllum commune is a basidiomycete equipped with an efficient Cellulolytic Enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading Enzymes from S. commune mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and β-glucosidase were obtained on Avicel-PH101 while a wider range of Enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex Enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox Enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an Enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by add...
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Characterization of Cellulolytic Enzyme system of Schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis
2017Co-Authors: Warasirin Sornlake, Lily Eurwilaichitr, Verawat Champreda, Phatcharamon Rattanaphanjak, Suthathip Kittisenachai, Sittiruk Roytrakul, Tatsuya Fujii, Hiroyuki InoueAbstract:Schizophyllum commune is a basidiomycete equipped with an efficient Cellulolytic Enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading Enzymes from S. commune mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and β-glucosidase were obtained on Avicel-PH101 while a wider range of Enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex Enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox Enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an Enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by addition external β-xylosidase. Enzymatic hydrolysis of alkaline-pretreated biomass by Sc-Cel and yield enhancement by external β-xylosidase (BX).
Angele Djioleu - One of the best experts on this subject based on the ideXlab platform.
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statistical approach for the identification of Cellulolytic Enzyme inhibitors using switchgrass dilute acid prehydrolyzates as a model system
ACS Sustainable Chemistry & Engineering, 2018Co-Authors: Angele Djioleu, Danielle Julie CarrierAbstract:The identification of biomass pretreatment-generated compounds that impede cellulose hydrolysis is critical for improving the overall biomass saccharification process. The aim of this study was to correlate the identification and concentrations of switchgrass dilute acid pretreatment-generated compounds to Cellulolytic Enzyme inhibition and to tie this back to processing parameters. Preparation of 24 dilute acid prehydrolyzates was performed with switchgrass at temperatures from 140 to 180 °C, processing times from 10 to 40 min, and sulfuric acid concentrations of 0.5% or 1% (v/v). Results showed that all the switchgrass prehydrolyzates significantly reduced Cellulolytic Enzyme activities when assayed against model substrates. Exoglucanase was the most sensitive with its activity reduction, ranging from 58% to 88%; the inhibitory effect on β-glucosidase and the cellulase cocktail ranged from 32% to 63% and 16% to 41%, respectively. Polyphenolic compounds were the most detrimental pretreatment-generated pr...
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Statistical Approach for the Identification of Cellulolytic Enzyme Inhibitors Using Switchgrass Dilute Acid Prehydrolyzates as a Model System
2018Co-Authors: Angele Djioleu, Danielle Julie CarrierAbstract:The identification of biomass pretreatment-generated compounds that impede cellulose hydrolysis is critical for improving the overall biomass saccharification process. The aim of this study was to correlate the identification and concentrations of switchgrass dilute acid pretreatment-generated compounds to Cellulolytic Enzyme inhibition and to tie this back to processing parameters. Preparation of 24 dilute acid prehydrolyzates was performed with switchgrass at temperatures from 140 to 180 °C, processing times from 10 to 40 min, and sulfuric acid concentrations of 0.5% or 1% (v/v). Results showed that all the switchgrass prehydrolyzates significantly reduced Cellulolytic Enzyme activities when assayed against model substrates. Exoglucanase was the most sensitive with its activity reduction, ranging from 58% to 88%; the inhibitory effect on β-glucosidase and the cellulase cocktail ranged from 32% to 63% and 16% to 41%, respectively. Polyphenolic compounds were the most detrimental pretreatment-generated products to the Cellulolytic Enzymes, especially to exoglucanase. Limited Enzyme inhibition, with acceptable biomass digestibility, was observed with pretreatment conditions corresponding to 160 °C. The statistically based approach used in this study proved to be a valid method to assess the effect of pretreatment-generated compounds on Cellulolytic Enzyme activities, linking their generation to pretreatment processing parameters
Yuqi Qin - One of the best experts on this subject based on the ideXlab platform.
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normal transcription of Cellulolytic Enzyme genes relies on the balance between the methylation of h3k36 and h3k4 in penicillium oxalicum
Biotechnology for Biofuels, 2019Co-Authors: Zhu Zhu, Jian Zhao, Kaili Zhao, Guodong Liu, Lushan Wang, Yuqi QinAbstract:Enzymatic hydrolysis of lignocellulose by fungi is a key step in global carbon cycle and biomass utilization. Cellulolytic Enzyme production is tightly controlled at a transcriptional level. Here, we investigated the roles of different histone lysine methylation modifications in regulating Cellulolytic Enzyme gene expression, as histone lysine methylation is an important process of chromatin regulation associated with gene transcription. PoSet1 and PoSet2 in Penicillium oxalicum, orthologs of Set1 and Set2 in budding yeast, were associated with the methylation of histone H3 lysine 4 (H3K4) and lysine 36 (H3K36). Cellulolytic Enzyme production was extensively upregulated by the disruption of PoSet2, but was significantly downregulated by the disruption of PoSet1. We revealed that the activation of Cellulolytic Enzyme genes was accompanied by the increase of H3K4me3 signal, as well as the decrease of H3K36me1 and H3K36me3 signal on specific gene loci. The repression of Cellulolytic Enzyme genes was accompanied by the absence of global H3K4me1 and H3K4me2. An increase in the H3K4me3 signal by Poset2 disruption was eliminated by the further disruption of Poset1 and accompanied by the repressed Cellulolytic Enzyme genes. The active or repressed genes were not always associated with transcription factors. H3K4 methylation is an active marker of Cellulolytic Enzyme production, whereas H3K36 methylation is a marker of repression. A crosstalk occurs between H3K36 and H3K4 methylation, and PoSet2 negatively regulates Cellulolytic Enzyme production by antagonizing the PoSet1-H3K4me3 pathway. The balance of H3K4 and H3K36 methylation is required for the normal transcription of Cellulolytic Enzyme genes. These results extend our previous understanding that Cellulolytic Enzyme gene transcription is primarily controlled by transcription factors.
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the different roles of penicillium oxalicum laea in the production of extracellular cellulase and β xylosidase
Frontiers in Microbiology, 2016Co-Authors: Xiaoju Zheng, Xiujun Zhang, Longfei Bao, Yingying Zhu, Jian Zhao, Yuqi QinAbstract:Cellulolytic Enzyme hydrolysis of lignocellulose biomass to release fermentable sugars is one of the key steps in biofuel refining. Gene expression of fungal Cellulolytic Enzymes is tightly controlled at the transcriptional level. Key transcription factors such as activator ClrB/CLR2 and XlnR/XYR1, as well as repressor CreA/CRE1 play crucial roles in this process. The putative protein methyltransferase LaeA/LAE1 has also been reported to regulate the gene expression of the Cellulolytic Enzyme. The formation and gene expression of the Cellulolytic Enzyme was compared among Penicillium oxalicum wild type (WT) and seven mutants, including ΔlaeA (deletion of laeA), OEclrB (clrB overexpression), OEclrBΔlaeA (clrB overexpression with deletion of laeA), OExlnR (xlnR overexpression), OExlnRΔlaeA (xlnR overexpression with deletion of laeA), ΔcreA (deletion of creA), and ΔcreAΔlaeA (double deletion of creA and laeA). Results revealed that LaeA extensively affected the expression of glycoside hydrolase genes. The expression of genes that encoded the top 10 glycoside hydrolases assayed in secretome was remarkably downregulated especially in later phases of prolonged batch cultures by the deletion of laeA. Cellulase synthesis of four mutants ΔlaeA, OEclrBΔlaeA, OExlnRΔlaeA, and ΔcreAΔlaeA was repressed remarkably compared with their parent strains WT, OEclrB, OExlnR, and ΔcreA, respectively. The overexpression of clrB or xlnR could not rescue the impairment of Cellulolytic Enzyme gene expression and cellulase synthesis when LaeA was absent, suggesting that LaeA was necessary for the expression of Cellulolytic Enzyme gene activated by ClrB or XlnR. In contrast to LaeA positive roles in regulating prominent cellulase and hemicellulase, the extracellular β-xylosidase formation was negatively regulated by LaeA. The extracellular β-xylosidase activities improved over 5-fold in the OExlnRΔlaeA mutant compared with that of WT, and the expression of prominent β-xylosidase gene xyl3A was activated remarkably. The cumulative effect of LaeA and transcription factor XlnR has potential applications in the production of more β-xylosidase.
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expression and chromatin structures of Cellulolytic Enzyme gene regulated by heterochromatin protein 1
Biotechnology for Biofuels, 2016Co-Authors: Xiujun Zhang, Yuqi QinAbstract:Heterochromatin protein 1 (HP1, homologue HepA in Penicillium oxalicum) binding is associated with a highly compact chromatin state accompanied by gene silencing or repression. HP1 loss leads to the derepression of gene expression. We investigated HepA roles in regulating Cellulolytic Enzyme gene expression, as an increasingly number of studies have suggested that Cellulolytic Enzyme gene expression is not only regulated by transcription factors, but is also affected by the chromatin status. Among the genes that exhibited significant differences between the hepA deletion strain (ΔhepA) and the wild type (WT), most (95.0 %) were upregulated in ΔhepA compared with WT. The expression of the key transcription factor for Cellulolytic Enzyme gene (e.g., repressor CreA and activator ClrB) increased significantly. However, the deletion of hepA led to downregulation of prominent extracellular Cellulolytic Enzyme genes. Among the top 10 extracellular glycoside hydrolases (Amy15A, Amy13A, Cel7A/CBHI, Cel61A, Chi18A, Cel3A/BGLI, Xyn10A, Cel7B/EGI, Cel5B/EGII, and Cel6A/CBHII), in which secretion amount is from the highest to the tenth in P. oxalicum secretome, eight genes, including two amylase genes (amy15A and amy13A), all five cellulase genes (cel7A/cbh1, cel6A/cbh2, cel7B/eg1, cel5B/eg2, and cel3A/bgl1), and the cellulose-active LPMO gene (cel61A) expression were downregulated. Results of chromatin accessibility real-time PCR (CHART-PCR) showed that the chromatin of all three tested upstream regions opened specifically because of the deletion of hepA in the case of two prominent cellulase genes cel7A/cbh1 and cel7B/eg1. However, the open chromatin status did not occur along with the activation of Cellulolytic Enzyme gene expression. The overexpression of hepA upregulated the Cellulolytic Enzyme gene expression without chromatin modification. The overexpression of hepA remarkably activated the Cellulolytic Enzyme synthesis, not only in WT (~150 % filter paper activity (FPA) increase), but also in the industry strain RE-10 (~20–30 % FPA increase). HepA is required for chromatin condensation of prominent cellulase genes. However, the opening of chromatin mediated by the deletion of hepA was not positively correlated with Cellulolytic Enzyme gene activation. HepA is actually a positive regulator for Cellulolytic Enzyme gene expression and could be a promising target for genetic modification to improve Cellulolytic Enzyme synthesis.