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41 results for “cellulase”
Data from: Comprehensive cDNA cloning and putative feature analysis of endogenous cellulases possessed by the Pacific oyster, Crassostrea gigas
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Modeled cellulase structure
<p>Cellulase structure based on PDB code 7CEL, used for Galaxy molecular dynamics tutorial.</p>
Fig. 3 in First comprehensive multi-tissue transcriptome of Cherax quadricarinatus (Decapoda: Parastacidae) reveals unexpected diversity of endogenous cellulase
Fig. 3 Expression of 65 transcripts categorized into 16 GH families measured in log2 of (TPM + 1) values. The descriptions of GH families were assigned based on InterPro annotations of transcripts in each family (Online Resource 3), providing higher confidence of its putative function. In contrast, GH30, GH31, and GH39 do not have descriptions as their corre- sponding transcripts do not pos- sess detectable domains or signatures that point to any enzymatic functions
Fig. 2 in First comprehensive multi-tissue transcriptome of Cherax quadricarinatus (Decapoda: Parastacidae) reveals unexpected diversity of endogenous cellulase
Fig. 2 Annotation and information on the Cherax quadricarinatus transcriptome. a Distribution of transcript lengths with blue bars representing the lengths of all transcripts and red bars showing the length distribution only for transcripts with at least one annotation. b Venn diagram showing the number of shared and unique transcripts in different tissue types expressed at a TPM threshold of 100. c Transcript
Fig. 1 in First comprehensive multi-tissue transcriptome of Cherax quadricarinatus (Decapoda: Parastacidae) reveals unexpected diversity of endogenous cellulase
Fig. 1 Workflow diagram for the analysis of the Cherax quadricarinatus transcriptome. Analyses included the de novo assembly of the transcriptome, annotation of transcripts, expression analysis in multiple tissues, and the identification of putative cellulases
Data Availability for "Function of four tryptophan residues on Cel7A catalytic efficiency: insight into cellulase screening strategy based on natural cellulose or cellulose analogs"
<p><strong>The data support for this article "Function of four tryptophan residues on Cel7A catalytic efficiency: insight into cellulase screening strategy based on natural cellulose or cellulose analogs"</strong></p>
All data support published article "Function of four tryptophan residues on Cel7A catalytic efficiency: insight into cellulase screening strategy based on natural cellulose or cellulose analogs"
<p>There is a high level of conservation of tryptophans within the active site architecture of the cellulase family, whereas the function of the four tryptophans in the catalytic domain of Cel7A is unclear. By mutating four tryptophan residues in the catalytic domain of Cel7A from <em>Penicillium piceum</em> (PpCel7A), the binding affinity between PpCel7A and <em>p-</em>nitrophenol-D-cellobioside (<em>p</em>NPC) was reduced as determined by Michaelis–Menten constants, molecular dynamics simulations, and fluorescence spectroscopy. Furthermore, PpCel7A variants showed a reduced level of cellobiohydrolase activity against cellulose analogs or natural cellulose. Therefore, it could be concluded four tryptophan residues in Cel7A played a critical role in substrate binding. Mutagenesis results indicated that the W390 stacking interactions at the -2 site played an essential role in facilitating substrate distortion to the -1 site. As soon as the function was altered, the mutation would inevitably affect the catalytic activity against the natural substrate. Interestingly, no clear relationship was found between the cellobiohydrolase activity of PpCel7A variants against <em>p</em>NPC and Avicel. <em>p</em>NP contains many electrophilic groups that may result in overestimation of the binding constant between tryptophan residues and <em>p</em>NPC in comparison to the natural substrate. Consequently, screening improved cellulase using cellulose analogs would divert attention from the target direction for lignocellulose biorefinery. Clarifying mechanism of catalytic diversity on the natural cellulose or cellulose analogs may give better insight into cellulase screening and selecting strategy.</p>
Data from: Effect of cellulases and xylanases on refining process and kraft pulp properties
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Comparative genomic analysis reveals cellulase plays an important role in the pathogenicity of Setosphaeria turcica f. sp. Zeae
<p><i><span>Setosphaeria turcica</span></i><span> f. sp. <i>sorghi</i> and <i>S. turcica</i> f. sp. <i>zeae</i>, the two formae speciales of <i>S. turcica</i>, cause northern leaf blight disease of sorghum and corn, respectively, and often cause serious economic losses. They show obvious host specialization and have a close evolutionary relationship. Genomic sequencing can provide more information for understanding the virulence mechanisms of pathogens. However, the complete genomic sequence of <i>S. turcica</i> f. sp. <i>sorghi</i> has not yet been reported, and no comparative genomic information is available for the two formae speciales. In this study, based on the analysis of genomic structure, there were more protein-coding genes in <i>S. turcica</i> f. sp. <i>sorghi</i> than <i>S. turcica</i> f. sp. <i>zeae</i></span><span>, </span><span>showing positive selection in the evolution of <i>S. turcica</i>. The results of genomic functional analysis showed that the two formae speciales had a large number of identical protein-coding genes, while there were also specific protein families, including metabolic pathway proteins, transport proteins, </span><span>CAZy</span><span>s, pathogen and host interaction proteins. We also investigated the expression of specific effector-coding genes in <i>S. turcica</i> f. sp. <i>zeae</i>, and found that the endo-1, 4-β-D-glucanase coding gene </span><i><span>CEL</span><span>2</span></i><span>, an important component of cellulase, was significantly up-regulated during the interaction process. Finally, gluconolactone inhibited cellulase activity and decreased infection rate and pathogenicity, which indicates that cellulase is essential for maintaining virulence. These findings demonstrate that cellulase plays an important role in the pathogenicity of <i>S. turcica</i> f. sp. <i>zeae</i>. </span></p>
Data from: The optimization of fermentation conditions for producing cellulase of Bacillus amyloliquefaciens and its application to goose feed
The proper culture conditions for producing cellulase of Bacillus amyloliquefaciens S1, isolated from the cecum of goose was optimized by single-factor experiment combined with orthogonal test. The properties of the cellulase were investigated by DNS method. The appropriate doses of B. amyloliquefaciens S1 were obtained by adding them to goose feed. It indicated that the suitable culture conditions of producing cellulase were the culture temperature of 37°C, the initial pH of 7.0, the incubation time of 72 h and the loaded liquid volume of 75 ml per 250 ml. The effects of each factor on producing cellulase by B. amyloliquefaciens S1 were as follows: initial pH > incubation time = culture temperature > loaded liquid volume. The optimum reaction temperature and pH were 50°C and 7.0, respectively. This enzyme is a kind of neutral cellulase that possesses resistance to heat and acidity. It showed high activity to absorbent cotton, soya bean meal and filter paper. By adding different doses of B. amyloliquefaciens S1 to the goose feed, it was found that the egg production, average egg weight, fertilization rate and the hatching rate were promoted both in experiment 1 (1.5 g kg−1) and experiment 2 (3 g kg−1). Also the difference of egg production, fertilization rate and hatching rate between experiment 1 and control group was obvious (p < 0.05), and the average egg weight was significantly increased in experiment 2 (p < 0.05).
Data from: The optimization of fermentation conditions for producing cellulase of Bacillus amyloliquefaciens and its application to goose feed
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Comparative genomic analysis reveals cellulase plays an important role in the pathogenicity of Setosphaeria turcica f. sp. Zeae
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Decoding the black box of cellulase formation in Hypocrea jecorina by RNA-Seq analysis
GEO Series GSE53629. Trichoderma reesei. 9 samples. Type: Expression profiling by high throughput sequencing.
The Protein Non-anchored cell wall protein NCW-1 promotes cellulase production through effects on cellobiose uptake in Neurospora crassa
GEO Series GSE73838. Neurospora crassa. 2 samples. Type: Expression profiling by high throughput sequencing.
Kinetic transcriptome study reveals an essentially intact cellulase induction system in a cellulase hyper-producer Trichoderma reesei strain
GEO Series GSE60908. Trichoderma reesei. 32 samples. Type: Expression profiling by array.
Growing Trichoderma reseei on a mix of carbon sources reveals links between development and cellulase production
GEO Series GSE82287. Trichoderma reesei. 36 samples. Type: Expression profiling by high throughput sequencing.
Systemic analysis of lactose metabolism in Trichoderma reesei identifies a lactose permease that is essential for cellulase induction
GEO Series GSE39276. Trichoderma reesei. 6 samples. Type: Expression profiling by array.
The putative cellodextrin transporter-like protein CLP1 is involved in cellulase induction in Neurospora crassa
GEO Series GSE60004. Neurospora crassa OR74A. 3 samples. Type: Expression profiling by high throughput sequencing.
Large-scale transcriptomic analyses reveal a global co-expression network of cellulase and xylanase genes in filamentous fungi
GEO Series GSE133258. Penicillium oxalicum. 72 samples. Type: Expression profiling by high throughput sequencing.
Genome sequencing and transcriptome analysis of Trichoderma reesei QM9978 reveals vib1 to be essential for cellulase induction
GEO Series GSE89199. Trichoderma reesei. 12 samples. Type: Expression profiling by high throughput sequencing.
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