Relevant bibliographies by topics / Microbial xylanase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'Microbial xylanase'

Author: Grafiati
Published: 18 May 2024

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Journal articles on the topic "Microbial xylanase"

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Tundo, Silvio, Giulia Mandalà, Luca Sella, Francesco Favaron, Renesh Bedre, and Raviraj M. Kalunke. "Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing." International Journal of Molecular Sciences 23, no. 23 (November 30, 2022): 14994. http://dx.doi.org/10.3390/ijms232314994.

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Xylanase inhibitors (XIs) are plant cell wall proteins largely distributed in monocots that inhibit the hemicellulose degrading activity of microbial xylanases. XIs have been classified into three classes with different structures and inhibition specificities, namely Triticum aestivum xylanase inhibitors (TAXI), xylanase inhibitor proteins (XIP), and thaumatin-like xylanase inhibitors (TLXI). Their involvement in plant defense has been established by several reports. Additionally, these inhibitors have considerable economic relevance because they interfere with the activity of xylanases applied in several agro-industrial processes. Previous reviews highlighted the structural and biochemical properties of XIs and hypothesized their role in plant defense. Here, we aimed to update the information on the genomic organization of XI encoding genes, the inhibition properties of XIs against microbial xylanases, and the structural properties of xylanase-XI interaction. We also deepened the knowledge of XI regulation mechanisms in planta and their involvement in plant defense. Finally, we reported the recently studied strategies to reduce the negative impact of XIs in agro-industrial processes and mentioned their allergenicity potential.
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Dhiman, Saurabh Sudha, Jitender Sharma, and Bindu Battan. "Industrial applications and future prospects of microbial xylanases: A review." BioResources 3, no. 4 (October 30, 2008): 1377–402. http://dx.doi.org/10.15376/biores.3.4.1377-1402.

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Microbial enzymes such as xylanases enable new technologies for industrial processes. Xylanases (xylanolytic enzyme) hydrolyze complex polysaccharides like xylan. Research during the past few decades has been dedicated to enhanced production, purification, and characterization of microbial xylanase. But for commercial applications detailed knowledge of regulatory mechanisms governing enzyme production and functioning should be required. Since application of xylanase in the commercial sector is widening, an understanding of its nature and properties for efficient and effective usage becomes crucial. Study of synergistic action of multiple forms and mechanism of action of xylanase makes it possible to use it for bio-bleaching of kraft pulp and for desizing and bio-scouring of fabrics. Results revealed that enzymatic treatment leads to the enhancement in various physical properties of the fabric and paper. This review will be helpful in determining the factors affecting xylanase production and its potential industrial applications in textile, paper, pulp, and other industries.
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Brennan, YaLi, Walter N. Callen, Leif Christoffersen, Paul Dupree, Florence Goubet, Shaun Healey, Myrian Hern�ndez, et al. "Unusual Microbial Xylanases from Insect Guts." Applied and Environmental Microbiology 70, no. 6 (June 2004): 3609–17. http://dx.doi.org/10.1128/aem.70.6.3609-3617.2004.

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ABSTRACT Recombinant DNA technologies enable the direct isolation and expression of novel genes from biotopes containing complex consortia of uncultured microorganisms. In this study, genomic libraries were constructed from microbial DNA isolated from insect intestinal tracts from the orders Isoptera (termites) and Lepidoptera (moths). Using a targeted functional assay, these environmental DNA libraries were screened for genes that encode proteins with xylanase activity. Several novel xylanase enzymes with unusual primary sequences and novel domains of unknown function were discovered. Phylogenetic analysis demonstrated remarkable distance between the sequences of these enzymes and other known xylanases. Biochemical analysis confirmed that these enzymes are true xylanases, which catalyze the hydrolysis of a variety of substituted β-1,4-linked xylose oligomeric and polymeric substrates and produce unique hydrolysis products. From detailed polyacrylamide carbohydrate electrophoresis analysis of substrate cleavage patterns, the xylan polymer binding sites of these enzymes are proposed.
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Liang, Fangfang, Yi Mo, Suleman Shah, Ying Xie, Arshad Mehmood, Hesheng Jiang, and Yafen Guo. "Characterization of Two Wheat-Derived Glycoside Hydrolase Family-10 Xylanases Resistant to Xylanase Inhibitors." Journal of Food Quality 2022 (April 5, 2022): 1–10. http://dx.doi.org/10.1155/2022/9590243.

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Xylanase inhibitors inhibit the activities of microbial xylanases and seriously compromise the efficacy of microbial xylanases added to modify cereals. Cereal endogenous xylanases are unaffected by these xylanase inhibitors, but little information is available regarding their effects in improving cereal quality, a neglected potential application. As a strategy for circumventing the negative effects of xylanase inhibitors, the objective of this study was to use genetic engineering to obtain sufficient amounts of active endo-1,4-β-D-xylanase from wheat to analyze the characteristics of its structure. The endo-1,4-β-D-xylanase from wheat was heterologously expressed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blotting, MALDI-TOF/TOF (MS) analyses, and enzyme activity determination confirmed 2 active endo-1,4-β-D-xylanases (EXY3 and EXY4) were successfully obtained. The molecular weights (MW) and isoelectric point (pI) of EXY3 were 36.108 kDa and 5.491, while those of the EXY4 protein were 41.933 kDa and 5.726. They both contained the same catalytic domain of GH10 xylanases from G266 to V276 and have the same catalytic site, Glu273. They shared the same putative N-glycosylation sites (N62-T63-S64 and N280–V281–S282) and 3 putative O-glycosylation sites (Ser8, Ser9, and Thr21), but EXY4 had an additional O-glycosylation site (Thr358). EXY3 was smaller than EXY4 by 51 amino acids because of a nonsense mutation and premature termination. They both had the 8-fold beta/alpha-barrel (TIM-barrel) fold. The specific activities of EXY3 and EXY4 were 152.0891 and 67.2928 U/mg, respectively. This work demonstrates a promising way to obtain wheat xylanases by genetic engineering; the properties of the enzymes indicate their potential application in cereal-based industries.
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Anand, Deepsikha, Jeya Nasim, Sangeeta Yadav, and Dinesh Yadav. "Bioinformatics Insights Into Microbial Xylanase Protein Sequences." Biosciences, Biotechnology Research Asia 15, no. 2 (June 27, 2018): 275–94. http://dx.doi.org/10.13005/bbra/2631.

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Microbial xylanases represents an industrially important group of enzymes associated with hydrolysis of xylan, a major hemicellulosic component of plant cell walls. A total of 122 protein sequences comprising of 58 fungal, 25 bacterial, 19actinomycetes and 20 yeasts xylanaseswere retrieved from NCBI, GenBank databases. These sequences were in-silico characterized for homology,sequence alignment, phylogenetic tree construction, motif assessment and physio-chemical attributes. The amino acid residues ranged from 188 to 362, molecular weights were in the range of 20.3 to 39.7 kDa and pI ranged from 3.93 to 9.69. The aliphatic index revealed comparatively less thermostability and negative GRAVY indicated that xylanasesarehydrophilicirrespective of the source organisms.Several conserved amino acid residues associated with catalytic domain of the enzyme were observed while different microbial sources also revealed few conserved amino acid residues. The comprehensive phylogenetic tree indicatedsevenorganismsspecific,distinct major clusters,designated as A, B, C, D, E, F and G. The MEME based analysis of 10 motifs indicated predominance of motifs specific to GH11 family and one of the motif designated as motif 3 with sequence GTVTSDGGTYDIYTTTRTNAP was found to be present in most of the xylanases irrespective of the sources.Sequence analysis of microbial xylanases provides an opportunity to develop strategies for molecular cloning and expression of xylanase genes and also foridentifying sites for genetic manipulation for developing novel xylanases with desired features as per industrial needs.
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Oyinlola, Ayodeji Adedapo, and Felix Akinsola Akinyosoye. "Isolation, Screening and Optimization of Xylanase Producing Fungi from Rhizosphere Soil of Cassava Tuber." International Journal of Advance Research and Innovation 9, no. 4 (2021): 19–29. http://dx.doi.org/10.51976/ijari.942103.

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Microbial xylanases have attracted a great deal of attention, due to their biotechnological potential in various industrial processes. In this study, the isolation, screening and optimization of xlanase-producing fungi from rhizosphere soil of cassava tuber under submerged fermentation were carried out. Altogether, eight fungal strains were isolated from the rhizosphere soil of cassava. All the fungal isolates were screened positive for xylanase activity on mineral salt medium supplemented with araboxylan as sole carbon source. The process parameters were optimized using one factor at a time technique. The identities of the isolates authenticated as Debaryomyces nepalensis and Penicillium polonicum by molecular techniques were regarded as good xylanase producers and they were selected for optimization studies. In order to maximize enzyme synthesis from fungi, the effect of nutritional and environmental conditions on xylanase production was investigated. The optimal incubation periods for maximal xylanase production by Penicillium polonicum and Debaryomyces nepalensis were 120 and 144 hours respectively while the optimal pH and temperature for xylanase production were 5.0 and 50oC respectively by Penicillium polonicum and Debaryomyces nepalensis. The best carbon sources for xylanase production from both fungi were found to be xylan. As a result of this, both fungal species have significant potential as sources of xylanases for industrial and biotechnological applications.
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Moscetti, Ilaria, Silvio Tundo, Michela Janni, Luca Sella, Katia Gazzetti, Alexandra Tauzin, Thierry Giardina, Stefania Masci, Francesco Favaron, and Renato D'Ovidio. "Constitutive Expression of the Xylanase Inhibitor TAXI-III Delays Fusarium Head Blight Symptoms in Durum Wheat Transgenic Plants." Molecular Plant-Microbe Interactions® 26, no. 12 (December 2013): 1464–72. http://dx.doi.org/10.1094/mpmi-04-13-0121-r.

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Cereals contain xylanase inhibitor (XI) proteins which inhibit microbial xylanases and are considered part of the defense mechanisms to counteract microbial pathogens. Nevertheless, in planta evidence for this role has not been reported yet. Therefore, we produced a number of transgenic plants constitutively overexpressing TAXI-III, a member of the TAXI type XI that is induced by pathogen infection. Results showed that TAXI-III endows the transgenic wheat with new inhibition capacities. We also showed that TAXI-III is correctly secreted into the apoplast and possesses the expected inhibition parameters against microbial xylanases. The new inhibition properties of the transgenic plants correlate with a significant delay of Fusarium head blight disease symptoms caused by Fusarium graminearum but do not significantly influence leaf spot symptoms caused by Bipolaris sorokiniana. We showed that this contrasting result can be due to the different capacity of TAXI-III to inhibit the xylanase activity of these two fungal pathogens. These results provide, for the first time, clear evidence in planta that XI are involved in plant defense against fungal pathogens and show the potential to manipulate TAXI-III accumulation to improve wheat resistance against F. graminearum.
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Tremblay, L., and F. Archibald. "Production of a cloned xylanase in Bacillus cereus and its performance in kraft pulp prebleaching." Canadian Journal of Microbiology 39, no. 9 (September 1, 1993): 853–60. http://dx.doi.org/10.1139/m93-127.

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Xylanase production from a Bacillus subtilis gene cloned into a strain of Escherichia coli was monitored. Although this gene was expressed in E. coli at several temperatures, efficient xylanase secretion did not occur; the observed protein release apparently depended on cell leakage or lysis. Screening for a better microbial protein secretor free of cellulase selected Bacillus cereus No. 518. A bidirectional vector plasmid (pMK3) was employed to carry the cloned gene into this B. cereus strain. Transformation was carried out by electroporation. Total xylanase production by the new pMK3-borne gene in B. cereus was similar to that from E. coli but the xylanase was shown to be normally secreted. The xylanase gene products from the E. coli and B. cereus hosts were shown to function identically. Both xylanases improved the delignification of unbleached softwood and hardwood kraft pulps, thus reducing the Cl2 required to achieve a given degree of bleaching, without altering the physical properties of the fibers. Using a target kappa number (lignin content) of 5, xylanase pretreatment of aspen kraft (chemical) pulp led to a 22% savings of chlorine. Adsorbable organic halogens in the bleachery effluent were also lowered by more than 50%.Key words: Bacillus subtilis, endoxylanase gene, bleaching, kraft pulp properties.
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Vandeplas, S., R. D. Dauphin, P. Thonart, A. Théwis, and Y. Beckers. "Effect of the bacterial or fungal origin of exogenous xylanases supplemented to a wheat-based diet on performance of broiler chickens and nutrient digestibility of the diet." Canadian Journal of Animal Science 90, no. 2 (June 1, 2010): 221–28. http://dx.doi.org/10.4141/cjas09067.

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Two identical experiments were carried out to study the effects of four xylanases from bacterial or fungal origin supplemented to a wheat-based diet, on growth performance of broiler chickens and nutrient digestibilities. Experimental treatments consisted of a control basal diet containing 600 g kg-1 wheat (C), and the basal diet supplemented with 0.1 g kg-1 Grindazyme G from Aspergillus niger (G), 0.1 g kg-1 Belfeed B1100MP from Bacillus subtilis (B), 0.1 g kg-1 Roxazyme G from Trichoderma viride (R), or 0.0125 g kg-1 of a xylanase from Aspergillus aculeatus (A). Each experimental diet was given to four groups of six chickens each. Growth performance and feed conversion ratio (FCR) were recorded weekly, from 7 to 21 d of age. In the second experiment, a digestion balance trial was performed from 27 to 31 d of age to evaluate the nitrogen-corrected apparent metabolizable energy (AMEn) and the digestibilities of nitrogen, crude fat, starch and crude fibre. From 7 to 21 d of age, xylanase supplementation led to increased final body weight and daily weight gain, by 3.7 and 4.5 % (P < 0.05), respectively, without significant difference according to the xylanase origin. Xylanase supplementation significantly increased the AMEn (+2.6 %), and the digestibilities of crude fibre (+58.9 %) and nitrogen (+1.6 %). Increase in AMEn as well as in crude fat and starch digestibilities were significantly different according to the xylanase, but were not dependent on fungal or bacterial origin. In conclusion, the microbial origin of xylanases supplemented to wheat-based diets influenced neither the performance of broiler chickens nor the improvement in nutrient digestibilities.Key words: Broiler, growth performance, nutrient digestibility, wheat, xylanase
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Cui, Shixiu, Tianwen Wang, Hong Hu, Liangwei Liu, Andong Song, and Hongge Chen. "Investigating the expression of F10 and G11 xylanases in Aspergillus niger A09 with qPCR." Canadian Journal of Microbiology 62, no. 9 (September 2016): 744–52. http://dx.doi.org/10.1139/cjm-2015-0394.

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There exist significant differences between the 2 main types of xylanases, family F10 and G11. A clear understanding of the expression pattern of microbial F10 and G11 under different culture conditions would facilitate better production and industrial application of xylanase. In this study, the fungal xylanase producer Aspergillus niger A09 was systematically investigated in terms of induced expression of xylanase F10 and G11. Results showed that carbon and nitrogen sources could influence xylanase F10 and G11 transcript abundance, with G11 more susceptible to changes in culture media composition. The most favorable carbon and nitrogen sources for high G11 and low F10 production by A. niger A09 were xylan (2%) and (NH4)2C2O4 (0.3%), respectively. Following cultivation at 33 °C for 60 h, the highest xylanase activity (1132 IU per gram of wet mycelia) was observed. On the basis of differential gene expression of F10 and G11, as well as their different properties, we deduced that the F10 protein initially targeted xylan and hydrolyzed it into fragments including xylose, after which xylose acted as the inducer of F10 and G11 gene expression. These speculations also accounted for our failure to identify conditions favoring the high production of F10 but a low production of G11.
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Dissertations / Theses on the topic "Microbial xylanase"

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Balakrishnan, H. "Studies on microbial xylanase." Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 1993. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/3057.

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Andrade, Fontes Carlos Mendes Godinho de. "Characterization of a microbial xylanase and its expression in mammalian cells." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294720.

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Saha, Shyama Prasad. "Production of microbial xylanase under submerged fermentation of agro-residues and its application in xylitol production." Thesis, University of North Bengal, 2018. http://ir.nbu.ac.in/hdl.handle.net/123456789/2682.

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Mosina, Leticia Ntsoaki. "Partial purification and characterisation of Phialophora alba xylanases and its application to pretreated sugarcane bagasse." Thesis, 2013. http://hdl.handle.net/10413/11197.

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Xylan is the major component of hemicellulose and its degradation can be achieved through the hydrolytic action of microbial xylanases. Xylanases have an array of applications one being bioethanol production. The lack of thermophilic xylanases has prompted the search for new enzymes with increased thermostability. Previous work on the crude enzyme of Phialophora alba has demonstrated optimal activity (39 U/μg) at a pH of 4 and two temperature optima of 50°C and 90°C. These desirable properties highlighted the need for further research on the purified enzyme. In the present study P. alba was identified as a thermophilc Ascomycete that forms conidia and chlamydospores during the asexual and sexual stages of its life cycle, respectively. The various isozymes present in the crude enzyme extract were subsequently detected by zymogram analysis. Up to six xylanase isozymes ranging from 90-210 kDa in size were detected. The crude enzyme was subsequently purified by precipitation and ion exchange chromatography (IEX). Protein precipitation methods, desalting methods, IEX resins, elution buffers and NaCl gradients were optimized. The 31-70% ammonium sulphate precipitate had the highest levels of xylanase activity. Separation of proteins with the anion exchanger, HiTrap Q sepharose fast flow column and a linear gradient of 0-2.5 M NaCl in phosphate buffer (50 mM, pH 7) yielded a partially pure xylanase isozyme with molecular weight of 210 kDa. A final yield of 1.4% and purification fold 10.6 was obtained after ion exchange chromatography. The specific activity of the xylanase was 21 IU/μg. At optimum pH (pH 4) and temperature (50°C) a combined xylanase activity of 32 IU.ml⁻¹ was detected. The partially pure xylanase was stable from pH 4-6 with 86% of xylanase activity retained for 90 minutes. Thermostability was observed from 40-70°C with 95% of activity retained for 90 minutes at optimum temperature. The ability of the partially pure xylanase and crude enzyme to hydrolyze untreated and pretreated (alkali and temperature/pressure) sugarcane bagasse was tested at a constant enzyme loading rate of 15 IU/g. Overall, maximum hydrolysis was achieved with the alkali pretreatment and saccharification with the crude enzyme: approximately, 2.4 g/ml of reducing sugars were liberated over a 48 hours. The partially pure xylanase liberated a maximum amount of 2.3 g/ml reducing sugars after 48 hours. The results obtained highlight the desirable characteristics of the partially pure enzyme and its applicability to bioethanol production.
Thesis (M.Sc.)-University of KwaZulu-Natal, Durban, 2013.
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Book chapters on the topic "Microbial xylanase"

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Ramanjaneyulu, G., A. Ramya, and B. Rajasekhar Reddy. "Microbial Population Dynamics of Eastern Ghats of Andhra Pradesh for Xylanase Production." In Microbial Biotechnology, 355–72. Toronto ; New Jersey : Apple Academic Press, 2015.: Apple Academic Press, 2017. http://dx.doi.org/10.1201/b19978-23.

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Gautério, Gabrielle Victoria, Luiz Claudio Simões Corrêa, Taiele Blumberg Machado, Mariana Vilar Castro da Veiga de Mattos, Janaina Fernandes de Medeiros Burkert, and Susana Juliano Kalil. "Industrial Xylanase Production Using Agri-Food Wastes Through Microbial Applications." In Microbial Bioprocessing of Agri-food Wastes, 83–116. Boca Raton: CRC Press, 2023. http://dx.doi.org/10.1201/9781003341017-4.

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Menon, Gopalakrishnan, and Sumitra Datta. "Xylanases: From Paper to Fuel." In Microbial Applications Vol.1, 153–64. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-52666-9_7.

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Selvarajan, E., S. Swathi, and V. Sindhu. "Xylanases: For Sustainable Bioproduct Production." In Microbial Bioprospecting for Sustainable Development, 223–36. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0053-0_11.

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El Enshasy, Hesham Ali, Subeesh Kunhi Kandiyil, Roslinda Malek, and Nor Zalina Othman. "Microbial Xylanases: Sources, Types, and Their Applications." In Biofuel and Biorefinery Technologies, 151–213. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43679-1_7.

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Biely, Peter. "Diversity of Microbial Endo-β-l,4-Xylanases." In ACS Symposium Series, 361–80. Washington, DC: American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0855.ch021.

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Dhiman, Sunny, and Gunjan Mukherjee. "Recent Advances and Industrial Applications of Microbial Xylanases: A Review." In Fungi and their Role in Sustainable Development: Current Perspectives, 329–48. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0393-7_19.

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Ho, Hooi Ling. "Biotechnology of Microbial Xylanase." In Biotechnology, 1424–55. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-8903-7.ch059.

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Xylanases are inducible enzymes responsible for the complete hydrolysis of xylan into xylose. Both solid state fermentation (SsF) and submerged fermentation (SmF) are used in the production of xylanase. SsF has become a popular approach due to its economic value. In fact, higher biomass and lower protein breakdown are among the factors involved in determining the production of xylanases in SsF. Agricultural extracts which are abundantly available in the environment such as rice bran and wheat bran are commonly used as the potential carbon source in xylanases production. Xylanase is indeed one of the valuable enzymes which show immense potential in vast industrial applications. The demand for xylanase is increasing because of its prodigious utilization in pulp and paper, bakery, food and beverage, detergents, textile, and animal feed. Xylanase has therefore become one of the important commercial enzymes in recent years.
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Ho, Hooi Ling. "Biotechnology of Microbial Xylanase." In Research Advancements in Pharmaceutical, Nutritional, and Industrial Enzymology, 294–325. IGI Global, 2018. http://dx.doi.org/10.4018/978-1-5225-5237-6.ch013.

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Xylanases are inducible enzymes responsible for the complete hydrolysis of xylan into xylose. Both solid state fermentation (SsF) and submerged fermentation (SmF) are used in the production of xylanase. SsF has become a popular approach due to its economic value. In fact, higher biomass and lower protein breakdown are among the factors involved in determining the production of xylanases in SsF. Agricultural extracts which are abundantly available in the environment such as rice bran and wheat bran are commonly used as the potential carbon source in xylanases production. Xylanase is indeed one of the valuable enzymes which show immense potential in vast industrial applications. The demand for xylanase is increasing because of its prodigious utilization in pulp and paper, bakery, food and beverage, detergents, textile, and animal feed. Xylanase has therefore become one of the important commercial enzymes in recent years.
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Jha, Harit, and Ragini Arora. "Application of Fungal Xylanase Enzymes." In Mushrooms: A Wealth of Nutraceuticals and An Agent of Bioremediation, 142–66. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815080568123010013.

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The enzyme xylanase breaks down the linear polysaccharide β-1,4-xylan into xylose, therefore breaking down hemicellulose, one of the primary components of plant cell walls. It is essential for the breakdown of plant materials into usable nutrients by microorganisms that thrive on plant sources. Fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insects, seeds, and other organisms generate xylanases. However, the amount of xylanase produced by fungal cultures is generally significantly larger than that produced by yeasts or bacteria. There is a growing demand for low-cost microbial xylanolytic enzymes that have industrial uses and are commercially manufactured. The chlorine-free whitening of wood pulp preparatory to the papermaking process and the enhanced digestibility of silage are two commercial applications for xylanase. Aside from the pulp and paper industry, xylanases are used in wheat flour for ethanol production, improving dough handling and quality of baked products, as food additives in poultry, clarification of fruit juices, biofuel production, textiles, pharmaceuticals, and chemical industries. Improved knowledge of the biological characteristics and genetics of fungal xylanase will allow these enzymes to be used in a variety of novel biotechnological and commercial applications.
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Conference papers on the topic "Microbial xylanase"

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Sultana, Sharmin, Md Sad Salabi Sawrav, Md Bokhtiar Rahma, Md Shohorab Hossain, and Md Azizul Haque. "Isolation and Biochemical Characterization of Xylanase Enzyme Producing Bacteria from Goat Rumen." In International Conference on Emerging Trends in Engineering and Advanced Science. AIJR Publisher, 2022. http://dx.doi.org/10.21467/proceedings.123.1.

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The rumen microbial communities of ruminants are thought to be the most promising biochemical source of inordinately diversified and multi-functional cellulolytic enzymes with unique functional adaptations to improve biotechnological processes. The exploitation of rumen microbial genetic variety has been limited due to a lack of effective screening culture techniques and a lack of understanding of the rumen microbial genetic diversity. This study is conducted to isolate and characterize rumen bacteria from goat rumen that have capability to produce xylanase enzyme. Serial dilutions technique is applied to isolate bacteria from goat rumen and repeated tubing of the selectively enriched microbial cultures by using the specific media for rumen bacteria. Following that, all of the isolates were underwent Methyl Red (MR) test & Voges-Proskauer (VP) test to identify organisms metabolic pathway, Triple Sugar Iron Agar (TSI) Test to determine bacterial ability to utilize sugar, Motility Indole and Urease activity test (MIU) to determine motility, Urease utilization and can produce Indole or not, Citrate utilization test to utilize citrate as carbon and energy source, Oxidase test, Catalase test to check the presence of catalytic enzyme where all isolates found promising which indicates that all five isolates are superior and capable to produce xylanase.
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Reports on the topic "Microbial xylanase"

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Avni, Adi, and Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7600030.bard.

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Maximizing food production with minimal negative effects on the environment remains a long-term challenge for sustainable food production. Microbial pathogens cause devastating diseases, minimizing crop losses by controlling plant diseases can contribute significantly to this goal. All plants possess an innate immune system that is activated after recognition of microbial-derived molecules. The fungal protein Eix induces defense responses in tomato and tobacco. Plants recognize Eix through a leucine-rich-repeat receptor- like-protein (LRR-RLP) termed LeEix. Despite the knowledge obtained from studies on tomato, relatively little is known about signaling initiated by RLP-type immune receptors. The focus of this grant proposal is to generate a foundational understanding of how the tomato xylanase receptor LeEix2 signals to confer defense responses. LeEix2 recognition results in pattern triggered immunity (PTI). The grant has two main aims: (1) Isolate the LeEix2 protein complex in an active and resting state; (2) Examine the biological function of the identified proteins in relation to LeEix2 signaling upon perception of the xylanase elicitor Eix. We used two separate approaches to isolate receptor interacting proteins. Transgenic tomato plants expressing LeEix2 fused to the GFP tag were used to identify complex components at a resting and activated state. LeEix2 complexes were purified by mass spectrometry and associated proteins identified by mass spectrometry. We identified novel proteins that interact with LeEix receptor by proteomics analysis. We identified two dynamin related proteins (DRPs), a coiled coil – nucleotide binding site leucine rich repeat (SlNRC4a) protein. In the second approach we used the split ubiquitin yeast two hybrid (Y2H) screen system to identified receptor-like protein kinase At5g24010-like (SlRLK-like) (Solyc01g094920.2.1) as an interactor of LeEIX2. We examined the role of SlNRC4a in plant immunity. Co-immunoprecipitation demonstrates that SlNRC4a is able to associate with different PRRs. Physiological assays with specific elicitors revealed that SlNRC4a generally alters PRR-mediated responses. SlNRC4a overexpression enhances defense responses while silencing SlNRC4 reduces plant immunity. We propose that SlNRC4a acts as a non-canonical positive regulator of immunity mediated by diverse PRRs. Thus, SlNRC4a could link both intracellular and extracellular immune perception. SlDRP2A localizes at the plasma membrane. Overexpression of SlDRP2A increases the sub-population of LeEIX2 inVHAa1 endosomes, and enhances LeEIX2- and FLS2-mediated defense. The effect of SlDRP2A on induction of plant immunity highlights the importance of endomembrane components and endocytosis in signal propagation during plant immune . The interaction of LeEIX2 with SlRLK-like was verified using co- immunoprecipitation and a bimolecular fluorescence complementation assay. The defence responses induced by EIX were markedly reduced when SlRLK-like was over-expressed, and mutation of slrlk-likeusing CRISPR/Cas9 increased EIX- induced ethylene production and SlACSgene expression in tomato. Co-expression of SlRLK-like with different RLPs and RLKs led to their degradation, apparently through an endoplasmic reticulum-associated degradation process. We provided new knowledge and expertise relevant to expression of specific be exploited to enhance immunity in crops enabling the development of novel environmentally friendly disease control strategies.
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