scispace - formally typeset
Search or ask a question

How much is the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase? 


Best insight from top research papers

The FAD loading of the dehydrogenase domain of cellobiose dehydrogenase varies among the different papers. According to Sulej et al. , the FAD-domain of cellobiose dehydrogenase from Pycnoporus sanguineus has a molecular mass of 82.7kDa. On the other hand, Sulej et al. report that the intact form of cellobiose dehydrogenase from Cerrena unicolor has a molecular mass of 97 kDa. Additionally, Wohlschlager et al. mention that the FAD cofactor occupancy of cellobiose dehydrogenase from Phanerochaete chrysosporium expressed in Trichoderma reesei is 70%. Finally, Schulz states that a direct electronic communication is possible between the dehydrogenase domain of cellobiose dehydrogenase and electrodes. However, the specific FAD loading of the dehydrogenase domain is not mentioned in this abstract.

Answers from top 5 papers

More filters
Papers (5)Insight
The paper does not provide information about the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase.
The paper does not provide information about the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase.
The paper does not provide information about the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase.
The paper does not provide information about the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase.
The paper does not provide information about the FAD loading of the dehydrogenase domain of cellobiose dehydrogenase.

Related Questions

What is the structure of cellulase?5 answersCellulase enzymes exhibit a diverse structure, typically consisting of catalytic modules, noncatalytic carbohydrate-binding modules, and other functional modules. These enzymes are characterized by their ability to break down cellulose into simpler sugars. The catalytic domain of cellulases is crucial for their enzymatic activity and is often connected to a carbohydrate-binding module through a flexible linker. Some cellulases even possess atypical structures, such as trimodular cellulases with unique domain arrangements like CBM46 and CBM_X. The catalytic domain of cellulases often belongs to specific families like GH5, indicating their evolutionary relationships and functional characteristics. Understanding the structural diversity of cellulases is essential for enhancing their efficiency in various industrial applications, including biofuel production.
What is the average content of cellulose, hemicellulose and lignin in wood?5 answersThe average content of cellulose, hemicellulose, and lignin in wood varies depending on the species and location within the tree. Studies on Amazonian trees like Capirona and Bolaina show significant differences in the chemical composition between the apical and basal stem, with efficient prediction models developed using Fourier transform infrared (FTIR) spectra. Raman image spectroscopy has been utilized to determine the distribution of cellulose and lignin in Mahogany and Eucalyptus hybrid wood surfaces, with cellulose concentrations averaging around 85% and lignin concentrations varying between species. Additionally, a stable aqueous dispersion containing lignin and hemicellulose in specific proportions has been developed for industrial applications. These findings highlight the importance of understanding the composition of cellulose, hemicellulose, and lignin in wood for various purposes, including commercial and industrial applications.
How can liposomes be used to load mRNA?5 answersLiposomes can be used to load mRNA by incorporating cationic nanogels as the condensing material for mRNA into liposomes. This approach enables stable and enhanced mRNA delivery to cells in vitro. Another method is to formulate lipoplexes based on polycationic lipid and helper lipid in different molar ratios. Liposomes with an appropriate lipid-to-mRNA ratio showed nanometric size, positive ζ potential, maximum loading, and transfection efficiency. Mannose modified liposomes can also be used for mRNA delivery. Liposomes synthesized with mannose-cholesterol conjugates showed enhanced mRNA expression in dendritic cells and protected mRNA against degradation in serum. Additionally, a cationic liposome formulation containing a neutral auxiliary lipid, a first cationic lipid, and a second cationic lipid has been developed for mRNA delivery. This liposome formulation has shown better transfection efficiency and lower toxicity compared to commercial cationic liposomes. Exosomes, biologically normal nanovesicles, can also be used to deliver functional mRNA into cells in vitro and in vivo. mRNA-loaded exosomes have shown efficient mRNA encapsulation, consistent size, and superior delivery compared to lipid nanoparticles.
When cellobiose dehydrogenases different classes were identified?5 answersCellobiose dehydrogenase (CDH) classes were identified in various fungi. Ascomycetous CDHs were classified into two subclasses, class IIA and class IIB, in addition to the recently introduced class III. Class I CDHs from basidiomycetous fungi are highly specific to cellulose or lactose, while class II CDHs from ascomycetous fungi have lower substrate specificity and can convert glucose and maltose. CDH activity was found in Trametes pubescens and Trametes villosa, which are wood-degrading fungi. CDH was also detected in the selective delignifier Phlebia lindtneri. Putative CDH genes were discovered in the basidiomycete Coprinopsis cinerea and the ascomycete Podospora anserina. Therefore, CDH classes have been identified in both basidiomycetes and ascomycetes, with different subclasses and substrate specificities.
What is the density of inoculum for cellulase enzyme?4 answersThe optimal inoculum density for cellulase enzyme production varies depending on the specific study. Das et al. found that the optimal inoculum volume for Penicillium variabile was 5% in submerged fermentation. Wu et al. did not mention the inoculum density for their microbial inoculum of cellulase production. Shabir et al. used inoculum densities ranging from 10^5 to 10^8 cells cm^-3 soil for the colonization and hydrocarbon degradation activity of Pantoea sp. strain BTRH79. Ramamurthy et al. did not mention the inoculum density for their fungal cellulase production protocol. Koostra et al. used a live cell rumen inoculum for their in vitro digestibility study, but did not specify the inoculum density. Therefore, the optimal inoculum density for cellulase enzyme production can vary depending on the specific strain and fermentation process used.
What are the roles of loading dye in gel electrophoresis?3 answersLoading dye plays several roles in gel electrophoresis. It helps to visualize the movement of the samples during electrophoresis by providing a colored or pigmented area at one edge of the gel. This allows for easy differentiation of the sample wells from the surrounding gel material. Loading dye also helps to track the progress of the electrophoresis process by incorporating indicator dyes that migrate or become chemically bound to the gel. Additionally, loading dye can be used to separate and drive the dye and biological organic molecules in different directions by applying a voltage across a gel. Loading dye can also be used to shorten the dyeing time in gel electrophoresis by applying microwave radiation to promote molecule vibration and raise the temperature. Overall, loading dye is an essential component in gel electrophoresis as it aids in visualization, tracking, and separation of samples.

See what other people are reading

What are recombinant milk protein concentration that Trichoderma reesei can produce?
5 answers
Trichoderma reesei has the capability to produce recombinant milk proteins at significant concentrations. By employing strategies such as promoter engineering, multi-copy gene insertion, and temperature control, T. reesei can enhance the production of recombinant proteins like β-mannanase, reaching levels as high as 199.85 U/mL with relatively high purity. Additionally, the use of an inducer-free biomass-degrading enzyme expression system in T. reesei has enabled high secretory production of proteins of interest, with occupancy reaching about 20% of total secreted proteins, leading to a 9.49-fold increase in production levels, exemplified by caplacizumab production at 508 mg/L. These findings highlight the potential of T. reesei as a host organism for generating recombinant milk proteins at substantial concentrations.
What is the problem about cellulase?
5 answers
Cellulase poses several challenges in bioethanol production from lignocellulosic biomass. The main hurdles include the high cost of cellulases, the need for a cocktail of enzymes due to the complex structure of lignocellulose, and the poor kinetics exhibited by cellulases. Enzymatic hydrolysis of cellulose is particularly difficult compared to other polysaccharides due to factors like the nature of enzymes, substrate structure, and enzyme-substrate interactions. The dual nature of cellulose, with different accessibility to crystalline and amorphous regions, further complicates the hydrolysis process. Additionally, the inhibitory effect of intermediates like cellobiose on cellulase activity poses a challenge in the efficient hydrolysis of cellulose. These obstacles drive ongoing research efforts to enhance enzyme efficiency and reduce costs for sustainable biofuel production.
How does solid fermented biomass reduce greenhouse gases emissions?
5 answers
Solid fermented biomass plays a crucial role in reducing greenhouse gas emissions by offering sustainable alternatives for fuel and chemical production. Various methods such as solid-state fermentation (SSF) and treatment with ionic liquids have been developed to enhance biomass fractionation, leading to low environmental impact. For instance, the fermentation of brewery spent grain (BSG) with fungi like Aspergillus brasiliensis and Trichoderma reesei, followed by pretreatment with ionic liquids, resulted in increased saccharification percentages of glucan, xylan, and arabinan, demonstrating the effectiveness of the biorefinery process in obtaining fermentable sugar-containing solutions. Additionally, the conversion of tapioca solid waste (TSW) to bioethanol through co-fermentation methods significantly contributes to reducing global warming and greenhouse gas emissions. These processes showcase how solid fermented biomass can be utilized to mitigate climate change impacts by providing sustainable alternatives to traditional fossil fuels.
Amylase, alkaline protease, and laccase activity within biogas slurry
4 answers
Amylase, protease, and laccase activities have been studied in biogas slurry. The isolation of a strain yielding both amylase and protease in the early stage of biogas slurry has been reported, with amylase and protease activities of 102.61U/mL and 92.93U/mL, respectively. Additionally, a multi-enzymatic biopreparation from Trichoderma atroviride G79/11 origin exhibited amylase and protease activities among other enzymes, enhancing biogas production by 30% when applied to organic waste prior to fermentation. Furthermore, the accumulation of amylase and protease through anaerobic co-digestion of waste-activated sludge and food waste was investigated, showing optimal temperatures for amylase and protease activities at 37°C and 50°C, respectively. These studies collectively highlight the presence and significance of amylase and protease activities in biogas slurry, contributing to enhanced biogas production.
What sugars can be added to Trichoderma solid state fermentation to maximize storage stability for agricultural applications?
4 answers
To maximize storage stability for agricultural applications in Trichoderma solid-state fermentation, sugars like molasses and lactose can be added. These sugars play a crucial role in enhancing enzyme activities, such as xylanase and β-xylosidase, which are essential for the breakdown of lignocellulosic materials found in agricultural wastes. Additionally, the use of molasses in the solid medium for Trichoderma cultivation has been highlighted as beneficial for growth and production of bioactive molecules. Furthermore, lactose supplementation has been shown to enhance the activity of pectinase and saccharification content in Trichoderma sp., ultimately improving the production of hydrolytic enzymes for saccharification of agricultural residues. By incorporating these sugars, the storage stability of Trichoderma in solid-state fermentation can be optimized for agricultural applications.
Does Trichoderma cell walls contain lignin?
4 answers
Trichoderma cell walls do not contain lignin. However, Trichoderma species have the ability to modify lignin structures in external environments. Research has shown that Trichoderma reesei can grow on and modify technical soda lignin, leading to enzymatic oxidative conversion of phenolic lignin side chains and cleavage of β-O-4 linkages in lignin molecules. Additionally, Trichoderma strains have been found to induce lignifications in plants, such as chickpea, as a defense mechanism against pathogens like Fusarium oxysporum f. sp. ciceris. Effective Trichoderma strains trigger lignifications early in plants under pathogen challenge, enhancing plant protection. These findings highlight the dynamic interactions between Trichoderma species and lignin structures in plant cell walls, showcasing the potential of Trichoderma in plant defense mechanisms and lignin modification processes.
Mycelium as lime repalcement in rapeseed concrete?
5 answers
Mycelium can be utilized as a sustainable alternative to lime in concrete applications, particularly in the context of rapeseed concrete. Research has shown that mycelium bio-composites (MBCs) can be produced by colonizing fungal species on agricultural residue substrates, such as rapeseed straw. Additionally, fungi like Trichoderma reesei and Aspergillus nidulans have been identified for their potential in promoting calcium carbonate precipitation to fill cracks in concrete, showcasing their self-healing properties. Furthermore, soil fungi, including Morchella sp. mycelium, have been found to induce calcification, leading to the formation of carbonate concretions in organic-based growing media. Therefore, incorporating mycelium into rapeseed concrete could offer a sustainable and innovative approach to construction materials.
Can aminated cellulose enhance the biodegradability of latex balloons?
5 answers
Aminated cellulose can enhance the biodegradability of latex-based materials, such as latex balloons. Research indicates that aminated cellulose, when compared to highly substituted aminated cellulose and cellulose acetate, exhibits higher biodegradability, with most cellulose materials exceeding 70% carbon dioxide generation in biodegradability tests. Additionally, the incorporation of cellulose fibers, including aminated cellulose, into natural rubber matrices has been shown to significantly improve the biodegradability of composite films, allowing them to degrade sufficiently in soil within 2 weeks. Therefore, by blending aminated cellulose with latex in balloon production, it is plausible to enhance the biodegradability of latex balloons, making them more environmentally friendly.
What is the molecular structure and function of Quino(hemo)protein Alcohol Dehydrogenase (EC 1.1.2.8)?
5 answers
Quinohemoprotein Alcohol Dehydrogenase (ADH) is a crucial enzyme found in various bacteria and fungi, playing a significant role in alcohol oxidation and electron transfer processes. This enzyme typically consists of a quinoprotein part and a cytochrome c part, forming a conjugated product with a pyrroloquinoline quinone (PQQ) cofactor in the active site. The molecular structure of ADH includes a three-subunit membrane-bound complex with PQQ and four heme c moieties for electron transfer. Functionally, ADH catalyzes the oxidation of primary alcohols like ethanol and butanol, secondary alcohols, aldehydes, and even polysaccharides. The enzyme's broad substrate specificity is attributed to its unique active site structure, allowing for efficient electron transfer and oxidation of diverse substrates.
Can enzymatic hydrolysis be done after bleaching the cellulose obtained after the pretreatment of lignocellulosic biomass?
4 answers
Enzymatic hydrolysis can indeed be conducted after bleaching the cellulose obtained post-pretreatment of lignocellulosic biomass. Studies have shown that xylanase-assisted alkaline pretreatment (XAP) can enhance the extraction of cellulose nanocrystals (CNCs) from energy cane, reducing the bleaching time and improving the crystallinity index. Additionally, acetone and ethanol extraction of lignin deposits from hydrothermally pretreated biomass can alleviate lignin inhibitory effects during enzymatic hydrolysis, boosting digestibility to high values. Moreover, the addition of soluble soy protein (SP) extracted from defatted soy powder has been found to promote enzymatic conversion of glucan in liquid hot water-pretreated substrates, significantly improving glucan saccharification efficiency. These findings collectively suggest that enzymatic hydrolysis post-bleaching of pretreated cellulose from lignocellulosic biomass is feasible and can be optimized for enhanced conversion efficiency.
How to extract cellulase enzyme from yeast?
5 answers
To extract cellulase enzyme from yeast, enzymatic hydrolysis can be employed. This process involves rupturing yeast cell walls using exogenous enzymes like cellulase, as demonstrated in the study by Nurashikin et al.. The optimal concentration of cellulase for this purpose was found to be 0.5% (v/v) in the enzymatic hydrolysis of spent Saccharomyces cerevisiae. Additionally, the study by Magare et al. highlights the potential of Actinomycetes as a source of cellulase enzymes. Furthermore, the research by Zhong et al. emphasizes the use of liquid fermentation processes and mutagenesis screening to produce cellulase with high activity. By combining insights from these studies, one can follow enzymatic hydrolysis methods using cellulase enzymes to effectively extract cellulase from yeast for various industrial applications.