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Tryptic Mapping Based Structural Insights of Endo-1, 4-β-Xylanase from Thermomyces lanuginosus VAPS-24.

ABSTRACT: An endo-1,4-β-xylanase, XynA, from Thermomyces lanuginosus VAPS-24, was purified to homogeneity and exhibited a molecular mass of approximately 20 kDa. The protein sequence of XynA was found to be similar to those of other Thermomyces lanuginosus derived xylanases and, as a result, could be used as a model enzyme for understanding the protein structure-activity relationship and facilitating protein engineering to design enzyme variants with desirable properties. Therefore, this xylanase will be an attractive candidate for applications in the biofuel and fine chemical industries for the degradation of xylans in steam pre-treated biomass.

SUBMITTER: Mathibe BN

PROVIDER: S-EPMC7329953 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Lignocellulosic pretreatment-mediated phenolic by-products generation and their effect on the inhibition of an endo-1,4-β-xylanase from <i>Thermomyces lanuginosus</i> VAPS-24.

Project description:The inhibitory effect of eight model lignin derivatives (ferulic acid, guaiacol, kraft lignin (alkali, low sulfonate content), p-coumaric acid, gallic acid, syringic acid, vanillin and vanillic acid) on XynA activity was evaluated. The model lignin derivatives viz. gallic acid, vanillic acid and vanillin were inhibitory to XynA activity, with an over 50% reduction in activity at concentrations as low as 0.5 mg/ml. However, enzyme deactivation studies in the absence of substrate showed that these pretreatment by-products do not interact with the enzyme except when in the presence of its substrate. The effect of the main structural properties of the pretreatment-derived phenolics, for example their hydroxyl and carbonyl group types, on XynA enzyme inhibition was investigated. The presence of carbonyl groups in phenolics appeared to confer stronger inhibitory effects than hydroxyl groups on XynA activity. The hydrolytic potential of XynA was not inhibited by a mixture of phenolics derived after steam pretreatment of woody biomass (Douglas fir and Black wattle). It appears as if the liquors from steam-pretreated woody biomass did not possess high enough phenolic content to confer XynA inhibition. The xylanase (XynA from Thermomyces lanuginosus) is, therefore, a striking choice for application in biofuel and fine chemical industries for the xylan degradation in steam-pretreated biomass.

| S-EPMC7377001 | biostudies-literature

Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris.

Project description:Highly efficient production of a Thermomyces lanuginosus IOC-4145 beta-1,4-xylanase was achieved in Pichia pastoris under the control of the AOX1 promoter. P. pastoris colonies expressing recombinant xylanase were selected by enzymatic activity plate assay, and their ability to secrete high levels of the enzyme was evaluated in small-scale cultures. Furthermore, an optimization of enzyme production was carried out with a 2(3) factorial design. The influence of initial cell density, methanol, and yeast nitrogen base concentration was evaluated, and initial cell density was found to be the most important parameter. A time course profile of recombinant xylanase production in 1-liter flasks with the optimized conditions was performed and 148 mg of xylanase per liter was achieved. Native and recombinant xylanases were purified by gel filtration and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, circular dichroism spectroscopy, matrix-assisted laser desorption ionization-time of flight-mass spectrometry and physicochemical behavior. Three recombinant protein species of 21.9, 22.1, and 22.3 kDa were detected in the mass spectrum due to variability in the amino terminus. The optimum temperature, thermostability, and circular dichroic spectra of the recombinant and native xylanases were identical. For both enzymes, the optimum temperature was 75 degrees C, and they retained 60% of their original activity after 80 min at 70 degrees C or 40 min at 80 degrees C. The high level of fully active recombinant xylanase obtained in P. pastoris makes this expression system attractive for fermentor growth and industrial applications.

| S-EPMC201252 | biostudies-literature

Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8.

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Thermomyces lanuginosus

Project description:Transcriptome Analysis of Avicel Utilization by Thermomyces lanuginosus

| PRJNA286684 | ENA

Thermomyces lanuginosus

Project description:Non-cellulolytic thermophilic fungus

| PRJNA88653 | ENA

Magnetic responsive Thermomyces lanuginosus lipase for biodiesel synthesis.

Project description:The low cost lipase derived from Thermomyces lanugionous was chosen to conjugate with Fe3O4 nanoparitcles as a magnetic responsive lipase (MRL) biocatalyst. The structure of MRL was observed by atomic force microscopy (AFM). The Fourier transform infrared (FTIR) spectroscopy analysis confirmed the lipase conjugated to Fe3O4 nanoparticles. Optimized conditions for the process of biodiesel production by MRL were investigated by the response surface methodology (RSM) and the Box-Behnken design (BBD). The optimized conditions for biodiesel production by MRL were as follows. The molar ratio of methanol to oil was 4.0, water content was 1.5 % as oil weight, the dosage of MRL to oil was 9.0 % (W/W) under 41?°C for 28?h. Under the optimized conditions, the yield of FAMEs by MRL reached 82.20 %. Further experiments showed that the MRL could be used 10 cycles and the yield of FAMEs decreased slightly by 10.97 %. These results indicated that Fe3O4 nanoparticle carrier could efficiently improve the FAMEs synthesis and enhance the MRL stabilization and reusability in the biodiesel production.

| S-EPMC7245248 | biostudies-literature

Transcriptome Analysis of Avicel Utilization by Thermomyces lanuginosus

Project description:Thermomyces lanuginosus is a thermophilic fungus whose genome encodes many carbohydrate-active enzymes involved in Avicel degradation. This study examined and compared the transcriptomes of T. lanuginosus during cultivation on Avicesl or glucose. We identified approximately 4485 genes that showed expression differences when T. lanuginosus was cultured on Avicel compared to glucose. Functional annotation of up-regulated genes showed enrichment for proteins predicted to be involved in Avicel degradation, but also many genes encoding proteins of unknown function. Our study represents the first analysis of transcriptomes, with biologic replicates, generated by RNA-seq technology. We conclude that RNA-seq based transcriptome characterization would expedite genetic network analyses and permit the dissection of complex biologic functions.

2015-06-17 | GSE69763 | GEO

Thermomyces lanuginosus SSBP

Project description:Thermomyces lanuginosus SSBP Genome sequencing and assembly

| PRJNA88097 | ENA

High levels of ?-xylosidase in Thermomyces lanuginosus: potential use for saccharification.

Project description:A new strain of Thermomyces lanuginosus was isolated from the Atlantic Forest biome, and its ?-xylosidases optimization in response to agro-industrial residues was performed. Using statistical approach as a strategy for optimization, the induction of ?-xylosidases activity was evaluated in residual corn straw, and improved so that the optimum condition achieved high ?-xylosidases activities 1003U/mL. According our known, this study is the first to show so high levels of ?-xylosidases activities induction. In addition, the application of an experimental design with this microorganism to induce ?-xylosidases has not been reported until the present work. The optimal conditions for the crude enzyme extract were pH 5.5 and 60°C showing better thermostability at 55°C. The saccharification ability of ?-xylosidase in the presence of hemicellulose obtained from corn straw raw and xylan from beechwood substrates showed a xylo-oligosaccharide to xylose conversion yield of 80 and 50%, respectively, at 50°C. Our data strongly indicated that the ?-xylosidases activities was not subjected to the effects of potential enzyme inhibitors often produced during fermentation process. These data suggest the application of this enzyme studied for saccharification of hemicellulose, an abundant residue in the American continents, thus providing an interesting alternative for future tests for energy production.

| S-EPMC4927647 | biostudies-literature

Identification of an endo-1,4-beta-xylanase of Ustilago maydis.

Project description:BackgroundThe utilization of raw biomass components such as cellulose or hemicellulose for the production of valuable chemicals has attracted considerable research interest in recent years. One promising approach is the application of microorganisms that naturally convert biomass constituents into value added chemicals. One of these organisms--Ustilago maydis--can grow on xylan, the second most abundant polysaccharide in nature, while at the same time it produces chemicals of biotechnological interest.ResultsIn this study, we present the identification of an endo-1,4-beta xylanase responsible for xylan degradation. Xylanase activity of U. maydis cells was indirectly detected by the quantification of released reducing sugars and could be confirmed by visualizing oligosaccharides as degradation products of xylan by thin layer chromatography. A putative endo-1,4-beta-xylanase, encoded by um06350.1, was identified in the supernatant of xylan-grown cells. To confirm the activity, we displayed the putative xylanase on the surface of the xylanase negative Saccharomyces cerevisiae EBY100. The presented enzyme converted xylan to xylotriose, similar to the source organism U. maydis.ConclusionsThe xylan degradation ability together with its unicellular and yeast-like growth makes U. maydis MB215 a promising candidate for the production of valuable chemicals such as itaconic acid or glycolipids from lignocellulosic biomass. Therefore, the characterization of the endo-1,4-beta-xylanase, encoded by um06350.1, is a further step towards the biotechnological application of U. maydis and its enzymes.

| S-EPMC3737115 | biostudies-literature

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