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Journal articles on the topic 'Xylanase production'

Author: Grafiati
Published: 6 September 2023

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1

Zadorozhny, Andrey Valentinovich, Viktor Sergeevich Ushakov, Alexei Sergeevich Rozanov, Natalia Vladimirovna Bogacheva, Valeria Nikolayevna Shlyakhtun, Mikhail Evgenyevich Voskoboev, Anton Vladimirovich Korzhuk, et al. "Heterologous Expression of Xylanase xAor from Aspergillus oryzae in Komagataella phaffii T07." International Journal of Molecular Sciences 23, no. 15 (August 5, 2022): 8741. http://dx.doi.org/10.3390/ijms23158741.

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Xylanases (EC 3.2.1.8) hydrolyze the hemicellulose of plant cell walls. Xylanases are used in the food and paper industries and for bioconversion of lignocellulose to biofuel. In this work, the producer-strain with four copies of the xAor xylanase gene was organized in two tandem copies for optimal expression in Komagataella phaffii T07 yeast. The secreted 35 kDa xylanase was purified from culture medium by gel filtration on Sephadex G-25 and anion exchange chromatography on DEAE-Sepharose 6HF. Tryptic peptides of the recombinant enzyme were analyzed by liquid chromatography-tandem mass spectrometry where the amino acid sequence corresponded to Protein Accession # O94163 for Endo-1,4-beta-xylanase from Aspergillus oryzae RIB40. The recombinant xylanase was produced in a bioreactor where the secreted enzyme hydrolyzed oat xylane with an activity of 258240 IU/mL. High activity in the culture medium suggested xylanase could be used for industrial applications without being purified or concentrated. The pH optimum for xylanase xAor was 7.5, though the enzyme was active from pH 2.5 to pH 10. Xylanase was active at temperatures from 35 °C to 85 °C with a maximum at 60 °C. In conclusion, this protocol yields soluble, secreted xylanase suitable for industrial scale production.
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Anand, Gautam, Meirav Leibman-Markus, Dorin Elkabetz, and Maya Bar. "Method for the Production and Purification of Plant Immuno-Active Xylanase from Trichoderma." International Journal of Molecular Sciences 22, no. 8 (April 19, 2021): 4214. http://dx.doi.org/10.3390/ijms22084214.

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Plants lack a circulating adaptive immune system to protect themselves against pathogens. Therefore, they have evolved an innate immune system based upon complicated and efficient defense mechanisms, either constitutive or inducible. Plant defense responses are triggered by elicitors such as microbe-associated molecular patterns (MAMPs). These components are recognized by pattern recognition receptors (PRRs) which include plant cell surface receptors. Upon recognition, PRRs trigger pattern-triggered immunity (PTI). Ethylene Inducing Xylanase (EIX) is a fungal MAMP protein from the plant-growth-promoting fungi (PGPF)–Trichoderma. It elicits plant defense responses in tobacco (Nicotiana tabacum) and tomato (Solanum lycopersicum), making it an excellent tool in the studies of plant immunity. Xylanases such as EIX are hydrolytic enzymes that act on xylan in hemicellulose. There are two types of xylanases: the endo-1, 4-β-xylanases that hydrolyze within the xylan structure, and the β-d-xylosidases that hydrolyze the ends of the xylan chain. Xylanases are mainly synthesized by fungi and bacteria. Filamentous fungi produce xylanases in high amounts and secrete them in liquid cultures, making them an ideal system for xylanase purification. Here, we describe a method for cost- and yield-effective xylanase production from Trichoderma using wheat bran as a growth substrate. Xylanase produced by this method possessed xylanase activity and immunogenic activity, effectively inducing a hypersensitive response, ethylene biosynthesis, and ROS burst.
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Mardawati, Efri, Surya Martha Pratiwi, Robi Andoyo, Tita Rialita, Mochamad Djali, Yana Cahyana, Een Sukarminah, In-In Hanidah, and Imas Siti Setiasih. "Ozonation Pretreatment Evaluation for Xylanase Crude Extract Production from Corncob under Solid-State Fermentation." Journal of Industrial and Information Technology in Agriculture 1, no. 2 (December 29, 2017): 27. http://dx.doi.org/10.24198/jiita.v1i2.14664.

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Xylanases are highly exploited enzyme in industries, including food and chemical industry. Xylanases can be utilized in catalyzing the endohydrolysis of 1,4-β-xylosidic linkages in xylan, lignocellulosic component to produce xylose-monomer. This research aims to optimize xylanase production from alternative substrate, corncob. Corncob contains 41.17% of hemicellulose, polymer of xylan. Xylanases are produced through solid state fermentation by Trichoderma viride. Ratio between substrate and moistening solution was 0.63 g/mL with fermentation temperature 32,8OC. Variables varied include incubation time and pretreatment (using autoclave, ozonation, combination of ozonation and autoclave, also without pretreatment). Xylanase activity was measured by DNS method using 1% of xylan as substrate standard. The result showed that the best incubation time is 36 h with 14403.8707 U/mg protein for specific xylanase activity by using autoclave as pretreatment. Ozonation pretreatment process can increase the enzyme activity of xylanase.
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ARABI, MOHAMMED IMAD EDDIN, YASSER BAKRI, and MOHAMMED JAWHAR. "Extracellular Xylanase Production by Fusarium Species in Solid State Fermentation." Polish Journal of Microbiology 60, no. 3 (2011): 209–12. http://dx.doi.org/10.33073/pjm-2011-029.

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Fusarium sp. has been shown to be a promising organism for enhanced production of xylanases. In the present study, xylanase production by 21 Fusarium sp. isolates (8 Fusarium culmorum, 4 Fusarium solani, 6 Fusarium verticillioides and 3 Fusarium equiseti) was evaluated under solid state fermentation (SSF). The fungal isolate Fusarium solani SYRN7 was the best xylanase producer among the tested isolates. The effects of some agriculture wastes (like wheat straw, wheat bran, beet pulp and cotton seed cake) and incubation period on xylanase production by F. solani were optimized. High xylanase production (1465.8 U/g) was observed in wheat bran after 96 h of incubation. Optimum pH and temperature for xylanase activity were found to be 5 and 50 degrees C, respectively.
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5

Tan, C. Z., W. T. Chang, M. Tarrsini, Y. P. Teoh, K. C. Lee, B. Kunasundari, Q. H. Ng, Z. X. Ooi, and C. Y. Low. "Xylanase Production via Aspergillus niger: Effect of Carbon Source and Composition." Journal of Physics: Conference Series 2080, no. 1 (November 1, 2021): 012001. http://dx.doi.org/10.1088/1742-6596/2080/1/012001.

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Abstract Xylanases are secondary metabolite product of variety organisms from various agriculture wastes. Xylanases’ demands in industrial level are increasing. Precisely, the necessity of enzyme such as xylanase to breaks down the xylan into reducing sugar for biofuel production is inevitable. However, the production of xylanases is insufficient to support the market demand. Hence, Aspergillus niger is used as the xylanase producer in this research. In this study, effect of carbon sources (corn cob-based xylan (CCX) and empty fruit bunches (EFB)) and concentrations of carbon source (2.5g/L to 4.0g/L) on xylanase production through One-factor-at-time (OFAT) experimental technique were investigated. The optimum fermentation period of 5 days determined by using mycelial dry cell mass and Bradford protein concentration growth profile is 5 days was set as the incubation period. Among these data, both carbon sources shown the maximum value at concentration of 3.5g/L. CCX showed a higher xylanase concentration (0.882±0.005μg/mL) compared to EFB (0.533 ± 0.006μg/mL). Hence, among these data analysis CCX has a better performance compared to EFB. Hence, among these data analysis CCX has a better performance compared to EFB.
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6

J, Jonathan, Veren Tania, Jessica C. Tanjaya, and Katherine K. "Recent Advancements of Fungal Xylanase Upstream Production and Downstream Processing." Indonesian Journal of Life Sciences | ISSN: 2656-0682 (online) 3, no. 1 (September 30, 2021): 37–58. http://dx.doi.org/10.54250/ijls.v3i1.122.

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Xylanase is a hydrolytic enzyme produced by fungi and bacteria utilized in various industrial applications such as food, biobleaching, animal feed, and pharmaceuticals. Due to its wide variety of applications, xylanase's large-scale industrial production has gained researchers' interest. Many factors and methods affect fungal xylanase's production in both upstream and downstream processing stages. The upstream production methods used are submerged fermentation (SmF) and solid-state fermentation (SSF), where SmF involves the usage of liquid substrates, while the SSF applies solid substrates to inoculate the microbes. The downstream processing of fungal xylanase includes extraction, purification, and formulation. The extraction methods used to extract fungal xylanase are filtration and solvent extraction. Meanwhile, the purification methods include ultrafiltration, precipitation, chromatography, Aqueous Two-Phase System (ATPS), and Aqueous Two-Phase Affinity Partitioning (ATPAP). The formulation of xylanase product is obtained in either liquid from the extraction-purification results, which can be converted to powder form using technologies such as spray drying to increase storage life. Moreover, immobilization of xylanase with nanoparticles of SiO2 could produce reusable xylanase enzymes. Several future studies have also been suggested. This review aims to explain the upstream and downstream processes of fungal xylanase production as well as the factors that affect those processes.
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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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8

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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Bakri, Y., Y. Akeed, M. Jawhar, and M. I. E. Arabi. "EVALUATION OF XYLANASE PRODUCTION FROM FILAMENTOUS FUNGI WITH DIFFERENT LIFESTYLES." Acta Alimentaria 49, no. 2 (June 2020): 197–203. http://dx.doi.org/10.1556/066.2020.49.2.9.

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Xylanase plays an important role in the food, feed, and pulp/paper industry. Filamentous fungi have been considered as useful producers of this enzyme from an industrial point of view, due to the fact that they excrete xylanases into the medium. In this study, four fungal species belonging to different genera, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium were isolated from different sources and compared for their ability to produce xylanase in submerged culture. The fungal species showed enzyme activity as determined by dinitrosalicylic acid (DNS) method. It was found that the two saprophytic Aspergillus strains, i.e A. terreus (Fss 129) and A. niger (SS7) had the highest xylanase activity of 474 and 294 U ml–1 at pH 7 and 8, respectively, in the presence of corn cob hulls after 120 h of incubation. The production of xylanase seemed to be strongly influenced by the interactive effect of initial pH on the fungi. Interestingly, xylanase was better produced by the saprophytic fungi of Aspergillus and Penicillium than by the plant pathogenic ones of Cochliobolus and Pyrenophora. This work provides additional information to support future research on fungi with different lifestyles for food industrial production of xylanase.
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Krisnawati, Ririn, Sardjono, Jaka Widada, Dian Anggraini Suroto, and Muhammad Nur Cahyanto. "Effect of Glucose on Endo-xylanase and β-xylosidase Production by Fungi Isolated in Indonesia." Journal of Pure and Applied Microbiology 16, no. 1 (January 10, 2022): 226–34. http://dx.doi.org/10.22207/jpam.16.1.12.

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Xylanases are widely produced by fungi, and the production of polysaccharide-degrading enzymes, in general, are usually subjected to carbon catabolite repression. In this work, the ability of several Indonesian indigenous fungi to produce endo-xylanase and β-xylosidase and their responses to glucose as a repressor were determined. Ten fungi were grown in a liquid medium supplemented with glucose as the repressor (0, 1%, 3%, and 5%), and the endo-xylanase and β-xylosidase productions were assayed. Aspergillus aculeatus FIG1 and A. oryzae KKB4 produced 3.85 and 0.70 U/mL of endo-xylanase, respectively, compared with other strains (0.22 U/mL or less). Trichoderma asperellum PK1J2, T. virens MLT2J2, A. aculeatus FIG1, T. asperellum MLT5J1, A. oryzae KKB4, and T. asperellum MLT3J2 produced 0.021–0.065 U/mL of β-xylosidase, whereas the other strains produced 0.013 U/mL or less of β-xylosidase. Adding 1% glucose to the growth medium can partially repress endo-xylanase production in A. aculeatus FIG1, T. asperellum PK1J2, and T. virens MLT4J1 and completely repress other strains. By adding 1% glucose, strains FIG1, PK1J2, and MLT4J1 suffered almost complete repression of β-xylosidase production, although such strains exhibited partial repression of endo-xylanase production. β-Xylosidase produced by the other strains showed complete repression by adding 1% glucose, except for A. aculeatus FIG1, A. tamarii FNCC 6151, and T. asperellum MLT1J1, which showed partial repression. Therefore, adding 3% glucose to the growth medium can result in complete repression of endo-xylanase and β-xylosidase productions in all strains examined.
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Knob, Adriana, Susan Michelz Beitel, Diana Fortkamp, César Rafael Fanchini Terrasan, and Alex Fernando de Almeida. "Production, Purification, and Characterization of a MajorPenicillium glabrumXylanase Using Brewer's Spent Grain as Substrate." BioMed Research International 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/728735.

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In recent decades, xylanases have been used in many processing industries. This study describes the xylanase production byPenicillium glabrumusing brewer's spent grain as substrate. Additionally, this is the first work that reports the purification and characterization of a xylanase using this agroindustrial waste. Optimal production was obtained whenP. glabrumwas grown in liquid medium in pH 5.5, at 25 °C, under stationary condition for six days. The xylanase fromP. glabrumwas purified to homogeneity by a rapid and inexpensive procedure, using ammonium sulfate fractionation and molecular exclusion chromatography. SDS-PAGE analysis revealed one band with estimated molecular mass of 18.36 kDa. The optimum activity was observed at 60 °C, in pH 3.0. The enzyme was very stable at 50 °C, and high pH stability was verified from pH 2.5 to 5.0. The ion Mn2+and the reducing agentsβ-mercaptoethanol and DTT enhanced xylanase activity, while the ions Hg2+, Zn2+, and Cu2+as well as the detergent SDS were strong inhibitors of the enzyme. The use of brewer's spent grain as substrate for xylanase production cannot only add value and decrease the amount of this waste but also reduce the xylanase production cost.
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Meilany, Diah, Dewinka Anugeraheni, Abdul Aziz, Made Tri Ari Penia Kresnowati, and Tjandra Setiadi. "The Effects of Operational Conditions in Scaling Up of Xylanase Enzyme Production for Xylitol Production." Reaktor 20, no. 1 (March 13, 2020): 32–37. http://dx.doi.org/10.14710/reaktor.20.1.32-37.

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The biological route to produce xylitol from Oil Palm Empty Fruit Bunches (EFBs) comprises of EFBs pretreatment, enzymatic hydrolysis, fermentation, and downstream separation of the produced xylitol. Due to the specificity in the hemicellulose composition of EFBs, a xylanase enzyme that has a high affinity to EFBs is required to hydrolyze the EFBs into xylose. In this research, the influences of aeration, humidity, and mixing in xylanase production were mapped. The xylanase production was performed by Aspergillus fumigatus ITBCCL170 in a solid-state fermentation using a tray fermenter with EFBs as the substrate. The optimal configuration was further scaled up into xylanase production using 1000 g of EFBs as the substrate. The results showed that the highest enzyme activity was 236.3 U/g EFB, obtained from the use of humid air airflow of 0.1 LPM, and mixing was performed once a day. The scaling up resulted in a lower xylanase activity and call for a better design of the fermenter.Keywords: aeration, humidity, mixing, OPEFBs, tray fermenter, xylanase, xylitol
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13

Raj, Abhay, Sharad Kumar, and Sudheer Kumar Singh. "A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization." Enzyme Research 2013 (December 14, 2013): 1–8. http://dx.doi.org/10.1155/2013/429305.

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Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach. Xylanase production studies by S. maltophilia on different commercial xylans and agro-industrial residues suggested that wheat bran was the best carbon source for xylanase production (26.4 ± 0.6 IU/mL). The studies with inorganic and organic nitrogen sources suggested yeast extract as the best support for xylanase production (25 ± 0.6 IU/mL). Maximum xylanase production was observed at initial medium pH = 8.0 (23.8 ± 0.4 IU/mL) with production at pH = 7.0 and pH = 9.0 being almost comparable. Xylanase produced by S. maltophilia was purified to homogeneity using ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The final purification was 5.43-fold with recovery of 19.18%. The molecular weight of the purified xylanase protein was ~142 kDa. Both crude and purified xylanase had good stability at pH = 9.0 and 80°C with activity retention greater than 90% after 30 min incubation. The enzyme stability at high temperature and alkaline pH make it potentially effective for industrial applications.
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14

Damaso, Mônica C. Triches, Marcius S. Almeida, Eleonora Kurtenbach, Orlando B. Martins, Nei Pereira, Carolina M. M. C. Andrade, and Rodolpho M. Albano. "Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris." Applied and Environmental Microbiology 69, no. 10 (October 2003): 6064–72. http://dx.doi.org/10.1128/aem.69.10.6064-6072.2003.

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ABSTRACT Highly efficient production of a Thermomyces lanuginosus IOC-4145 β-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 23 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°C, and they retained 60% of their original activity after 80 min at 70°C or 40 min at 80°C. The high level of fully active recombinant xylanase obtained in P. pastoris makes this expression system attractive for fermentor growth and industrial applications.
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15

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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Alcobaça, Olinda S. A., Emeline B. Campanini, Iara Ciancaglini, Sâmara V. Rocha, Iran Malavazi, Caio C. M. Freire, Francis M. F. Nunes, Andrea S. C. Fuentes, and Anderson F. Cunha. "Identification of a New Endo-β-1,4-xylanase Prospected from the Microbiota of the Termite Heterotermes tenuis." Microorganisms 10, no. 5 (April 26, 2022): 906. http://dx.doi.org/10.3390/microorganisms10050906.

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Xylanases are hemicellulases that break down xylan to soluble pentoses. They are used for industrial purposes, such as paper whitening, beverage clarification, and biofuel production. The second-generation bioethanol production is hindered by the enzymatic hydrolysis step of the lignocellulosic biomass, due to the complex arrangement established among its constituents. Xylanases can potentially increase the production yield by improving the action of the cellulolytic enzyme complex. We prospected endo-β-1,4-xylanases from meta-transcriptomes of the termite Heterotermes tenuis. In silico structural characterization and functional analysis of an endo-β-1,4-xylanase from a symbiotic protist of H. tenuis indicate two active sites and a substrate-binding groove needed for the catalytic activity. No N-glycosylation sites were found. This endo-β-1,4-xylanase was recombinantly expressed in Pichia pastoris and Escherichia coli cells, presenting a molecular mass of approximately 20 kDa. Enzymatic activity assay using recombinant endo-β-1,4-xylanase was also performed on 1% xylan agar stained with Congo red at 30 °C and 40 °C. The enzyme expressed in both systems was able to hydrolyze the substrate xylan, becoming a promising candidate for further analysis aiming to determine its potential for application in industrial xylan degradation processes.
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Alcobaça, Olinda S. A., Emeline B. Campanini, Iara Ciancaglini, Sâmara V. Rocha, Iran Malavazi, Caio C. M. Freire, Francis M. F. Nunes, Andrea S. C. Fuentes, and Anderson F. Cunha. "Identification of a New Endo-β-1,4-xylanase Prospected from the Microbiota of the Termite Heterotermes tenuis." Microorganisms 10, no. 5 (April 26, 2022): 906. http://dx.doi.org/10.3390/microorganisms10050906.

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Xylanases are hemicellulases that break down xylan to soluble pentoses. They are used for industrial purposes, such as paper whitening, beverage clarification, and biofuel production. The second-generation bioethanol production is hindered by the enzymatic hydrolysis step of the lignocellulosic biomass, due to the complex arrangement established among its constituents. Xylanases can potentially increase the production yield by improving the action of the cellulolytic enzyme complex. We prospected endo-β-1,4-xylanases from meta-transcriptomes of the termite Heterotermes tenuis. In silico structural characterization and functional analysis of an endo-β-1,4-xylanase from a symbiotic protist of H. tenuis indicate two active sites and a substrate-binding groove needed for the catalytic activity. No N-glycosylation sites were found. This endo-β-1,4-xylanase was recombinantly expressed in Pichia pastoris and Escherichia coli cells, presenting a molecular mass of approximately 20 kDa. Enzymatic activity assay using recombinant endo-β-1,4-xylanase was also performed on 1% xylan agar stained with Congo red at 30 °C and 40 °C. The enzyme expressed in both systems was able to hydrolyze the substrate xylan, becoming a promising candidate for further analysis aiming to determine its potential for application in industrial xylan degradation processes.
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Denta Putri, Lupita, Hasnah Natsir, and Seniwati Dali. "Thermophilic Xylanase Production Rom Isolates of Macula’ Hot Springs Bacteria Using Corn Cobs Waste Media." Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta) 10, no. 2 (May 30, 2019): 25. http://dx.doi.org/10.20956/ica.v10i2.6652.

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Xylanases is an extracellular enzyme that has prospects as enzymes that hydrolyze hemicellulose (xylan). In this study, carried out isolatied of bacteria from the hot springs Makula', Tana Toraja and determine the optimum conditions in producing the xylanase enzyme. The steps being taken are the rejuvenation of bacteria, the manufacture medium inoculum and the production medium, the measurement OD (Optical Density) measurements of protein and testing activities xylanase. The results obtained showed that the production time for B. stearothermophilus SL3A is in the 48 hours with a value of 0.1237 activity mU/mL and B. stearothermophilus SL3S at the 60 hours with a value of 0.1593 activity mU/mL. B. stearothermophilus SL3A have a protein content of 9.828 mg/mL and for B. stearothermophilus SL3S have a protein content of 10.07 mg/mL. Characteristics bacterial xylanase from B. stearothermophilus SL3A and B. stearothermophilus SL3S work optimally at pH 7 a temperature of 45 ºC. Crude extract of the isolated xylanase enzyme can hydrolyze substrate is xylan corn cobs. The addition of metal CaCl2, MgCl2, CaCl2 can increase the activities of the enzyme xylanase and CoCl2 decreases the activities of enzymes that are inhibitors.
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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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Liguori, Rossana, Anna Pennacchio, Luciana Porto de Souza Vandenberghe, Addolorata De Chiaro, Leila Birolo, Carlos Ricardo Soccol, and Vincenza Faraco. "Screening of Fungal Strains for Cellulolytic and Xylanolytic Activities Production and Evaluation of Brewers’ Spent Grain as Substrate for Enzyme Production by Selected Fungi." Energies 14, no. 15 (July 23, 2021): 4443. http://dx.doi.org/10.3390/en14154443.

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Brewer’s spent grain (BSG), the solid residue of beer production, is attracting significant attention as raw material for the production of added value substances, since until recently it was mainly used as animal feed or deposited in landfills, causing serious environmental problems. Therefore, this work aimed at developing a bioprocess using BSG as a substrate for the production of cellulases and xylanases for waste saccharification and bioenergy production. Different fungi were analyzed for their cellulolytic and xylanolytic abilities, through a first screening on solid media by assessment of fungal growth and enzyme production on agar containing carboxylmethylcellulose or xylan as the sole carbon source, respectively. The best cellulase and xylanase producers were subjected to quantitative evaluation of enzyme production in liquid cultures. Aspergillus niger LPB-334 was selected for its ability to produce cellulase and xylanase at high levels and it was cultivated on BSG by solid state fermentation. The cellulase production reached a maximum of 118.04 ± 8.4 U/g of dry substrate after 10 days of fermentation, while a maximum xylanase production of 1315.15 ± 37.5 U/g of dry substrate was reached after 4 days. Preliminary characterization of cellulase and xylanase activities and identification of the enzymes responsible were carried out.
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Sampaio, C. R., C. G. S. Silva, É. C. T. Anjos, R. P. M. Fernandes, and M. F. Fernandes. "Screening of a Soil Bacteria Collection for the Production of Alkali Thermostable Xylanases." Journal of Agricultural Science 10, no. 8 (July 10, 2018): 232. http://dx.doi.org/10.5539/jas.v10n8p232.

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This work aimed to evaluate a collection of common and rare soil bacteria regarding to extracellular xylanases production and to characterize the stability in contrasting conditions of temperature and pH of these enzymes. This collection consists of 120 isolates belonging to six phyla that were subjected to screening for xylanase activity in pure cultures and in the extracellular proteic extract (EPE). The ratio between the halos diameters of xylan hydrolysis and in the colonies on solid medium (ratio H:C) was used for the evaluation of cultures as selection criteria. EPEs of isolates with highest ratios H:C were evaluated for the specific xylanases activity at 50 °C for 1 h. EPE of the three isolates with the highest potential for activity under this condition were evaluated for optimum activity, stability at 60 °C and different pH values. Twenty-two isolates showed xylanase activity under these conditions. Xylanases from TC21 and TC119 showed high relative activity at temperatures up to 70 °C and were less sensitive to changes in pH. Soil bacteria show high potential as a source of extracellular xylanases adapted to extreme pH and temperature conditions, which are required in agroindustrial processes.
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22

SIPRIYADI, SIPRIYADI, ARIS TRI WAHYUDI, MAGGY THENAWIDJAYA SUHARTONO, and ANJA MERYANDINI. "Optimization of Xylanase Production by Streptomyces costaricanus 45I-3 Using Various Substrates through Submerged Fermentation." Microbiology Indonesia 14, no. 1 (September 7, 2020): 5. http://dx.doi.org/10.5454/mi.14.1.5.

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Xylanase is an important hydrolytic enzymes with many application in several industries, but to obtain enzyme derived products is not easy. Thus, the optimization of efficient xylanases production is a great interest for biotechnological application. This study aims to determine the type of substrate, medium composition, and optimum conditions of xylanase production by S. costaricanus 45I-3. Determination of substrate type was done by growing the tested bacteria on birchwood xylan, beechwood xylan, oat spelled xylan, corn cobs xylan, and tobacco xylan substrate, meanwhile the determination of medium composition and enzyme production were done by measuring xylanase activity at various substrate concentration and replacing the carbon, nitrogen, phosphate and surfactants source. The results showed that the highest enzymatic index (EI) produced from corn cob xylan substrate at 3.60 meanwhile the second highest was beechwood xylan substrate at 2.87 EI, however this substrate is purer, thus this substrate was selected and used as xylan sources for further optimization measurement. The best xylanase activity (2.29 U/mL) obtained on eighth day after inoculation on rotary incubator at 120 rpm in 28 ºC. Arabinose as the source of carbon generate the highest activity at 3.161 U/mL meanwhile the most preferred source of phosphate is Na2HPO4 (2.37 U/mL). Both source of nitrogen i.e. nitrogen ammonium sulphate (NH4)2SO4 and yeast extract were able to produce xylanase at 2.57 and 2.36 U/mL. The addition of surfactant in production medium showed addition of SDS surfactant (0.146 U/mL) and Tween 80 (0.438 U/mL) showed a negative response by decreasing the activity. The conclusion showed that the xylanase activity was increased after optimization at various C, N, and P sources, and the use of nitrogen source (NH4)2SO4), become a more economical alternative to replacing a nitrogen source yeast extract so it can lower the production costs of xylanase enzyme.
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23

Lian, Ling-Dan, Ling-Yan Shi, Jing Zhu, Rui Liu, Liang Shi, Ang Ren, Han-Shou Yu, and Ming-Wen Zhao. "GlSwi6 Positively Regulates Cellulase and Xylanase Activities through Intracellular Ca2+ Signaling in Ganoderma lucidum." Journal of Fungi 8, no. 2 (February 14, 2022): 187. http://dx.doi.org/10.3390/jof8020187.

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Ganoderma lucidum is a white-rot fungus that produces a range of lignocellulolytic enzymes to decompose lignin and cellulose. The mitogen-activated protein kinase (MAPK) pathway has been implicated in xylanases and cellulases production. As the downstream transcription factor of Slt2-MAPK, the function of Swi6 in G. lucidum has not been fully studied. In this study, the transcription factor GlSwi6 in G. lucidum was characterized and shown to significantly positively regulate cellulases and xylanases production. Knockdown of the GlSwi6 gene decreased the activities of cellulases and xylanases by approximately 31%~38% and 54%~60% compared with those of the wild-type (WT) strain, respectively. Besides, GlSwi6 can be alternatively spliced into two isoforms, GlSwi6A and GlSwi6B, and overexpression of GlSwi6B increased the activities of cellulase and xylanase by approximately 50% and 60%, respectively. Further study indicates that the existence of GlSwi6B significantly increased the concentration of cytosolic Ca2+. Our study indicated that GlSwi6 promotes the activities of cellulase and xylanase by regulating the Ca2+ signaling. These results connected the GlSwi6 and Ca2+ signaling in the regulation of cellulose degradation, and provide an insight for further improvement of cellulase or xylanase activities in G. lucidum as well as other fungi.
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24

Ha, D. T., A. V. Kanarskiy, Z. A. Kanarskaya, A. V. Scherbakov, E. N. Scherbakova, and A. V. Pranovich. "Impact of cultivation conditions on xylanase production and growth in Paenibacillus mucilaginosus." Proceedings of Universities. Applied Chemistry and Biotechnology 10, no. 3 (October 8, 2020): 459–69. http://dx.doi.org/10.21285/2227-2925-2020-10-3-459-469.

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Xylanase is an enzyme that hydrolyses β-1,4 bonds in plant xylan. This enzyme is applied in the bioconversion of agro-industrial waste for xylooligosaccharide hydrolysate production to improve digestibility and nutrition value of animal feed, food processing, the utilisation and faster decomposition of crop debris in soil, as well as in cellulose bleaching and other industries. The current trend focuses on using renewable resources, such as agricultural waste, as substitutes for expensive purified xylan in producer screening and xylanase synthesis. This work aimed to determine the impact of Paenibacillus mucilaginosus cultivation conditions on the xylanase production yield. Rice bran ferment lysate along with birch and beech timber xylans were used as a carbon source. Temperature, medium pH, pH correction factors, inoculant incubation time, carbon and nitrogen sources and concentrations were the studied criteria of xylanase biosynthesis and growth in bacteria P. ucilaginosus strain 560. We show that the xylanase biosynthesis and cultivation in P. mucilaginosus strain 560 are more practical and cost-effective with the use of a rice bran ferment lysate-based nutrient medium. Inductors contained in the rice bran ferment lysate improve the xylanase biosynthesis. Calcium ions also facilitate biosynthesis in the studied strain. Cultivation recommendations are: carbon source concentration in medium 0.5% of total reducing substances content; 0.2% carbamide as optimal nitrogen source; calcium hydroxide as an agent for medium pH correction to 6.0±0.2; cultivation temperature 30±1 °С. Under the specified conditions, cultivation of P. mucilaginosus does not require inoculate preprocessing, and a maximal xylanase activity in stationary culture reaches 20 U/mL.
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Metreveli, Eka, Tamar Khardziani, and Vladimir Elisashvili. "The Carbon Source Controls the Secretion and Yield of Polysaccharide-Hydrolyzing Enzymes of Basidiomycetes." Biomolecules 11, no. 9 (September 10, 2021): 1341. http://dx.doi.org/10.3390/biom11091341.

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In the present study, the polysaccharide-hydrolyzing secretomes of Irpex lacteus (Fr.) Fr. (1828) BCC104, Pycnoporus coccineus (Fr.) Bondartsev and Singer (1941) BCC310, and Schizophyllum commune Fr. (1815) BCC632 were analyzed in submerged fermentation conditions to elucidate the effect of chemically and structurally different carbon sources on the expression of cellulases and xylanase. Among polymeric substrates, crystalline cellulose appeared to be the best carbon source providing the highest endoglucanase, total cellulase, and xylanase activities. Mandarin pomace as a growth substrate for S. commune allowed to achieve comparatively high volumetric activities of all target enzymes while wheat straw induced a significant secretion of cellulase and xylanase activities of I. lacteus and P. coccineus. An additive effect on the secretion of cellulases and xylanases by the tested fungi was observed when crystalline cellulose was combined with mandarin pomace. In I. lacteus the cellulase and xylanase production is inducible in the presence of cellulose-rich substrates but is suppressed in the presence of an excess of easily metabolizable carbon source. These enzymes are expressed in a coordinated manner under all conditions studied. It was shown that the substitution of glucose in the inoculum medium with Avicel provides accelerated enzyme production by I. lacteus and higher cellulase and xylanase activities of the fungus. These results add new knowledge to the physiology of basidiomycetes to improve cellulase production.
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26

Richana, Nur, Tun T. Irawadi, Anwar Nur, and Khaswar Syamsu. "Isolasi Identifikasi Bakteri Penghasil Xilanase serta Karakterisasi Enzimnya." Jurnal AgroBiogen 4, no. 1 (August 9, 2016): 24. http://dx.doi.org/10.21082/jbio.v4n1.2008.p24-34.

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<p>Xylanase is an extracellular enzyme produced by<br />microorganisms. This enzyme is able to hydrolise xylane<br />(hemicellulose) to produce xylooligosaccharide and xylose.<br />Thermoalkaliphilic xylanase is an agent that can be used as<br />a substitute in the pulp whitening process instead of chlorine.<br />A study was done to isolate, identificate of bacteria and<br />characterize xylanase. The isolation of xylanase producing<br />bacteria has been done from soil and waste of starch industry.<br />Colonies which produced clearing zone were presumed<br />as xylanolytic bacteria and chosen for further screening.<br />Identification of potential isolate in xylanase production was<br />done using 16S ribosomal RNA sequencing. Isolate Bacillus<br />pumilus RXA-III5 originated from lime or alkaline soil was<br />more potential isolate in xylanase production than other 24<br />isolates. Precipitation of xylanase, that was done using<br />ammonium sulphate followed by dialyzes produced xylanase<br />of a higher specific activity (267.1 U.mg-1) than that using<br />acetone (131.1 U.mg-1) and ethanol (186.65 U.mg-1). Xylanase<br />was done at purification produced three fractions of xylanase.<br />Xylanase characteristics consist of pH and temperature<br />(9 and 50oC), Km and Vmaks value 6 mg.ml-1 and 0.2<br />mol.minute-1, respectively. The Fe2+ was the strongest activetor<br />and Mg2+ was the strongest inhibitor activity. This enzyme<br />was detected as a cellulose-free xylanase. Xylanase is a<br />prospective agent for bio-bleaching of paper.</p>
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Hanim, Chusnul, Muhamad Nur Cahyanto, Lies Mira Yusiati, and Ali Wibowo. "Partial Purifi cation, Stability Analysis, and Preservation of Xylanase from Xylanolytic Alkalophylic Bacteria." Indonesian Journal of Biotechnology 18, no. 1 (November 9, 2015): 1. http://dx.doi.org/10.22146/ijbiotech.7861.

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A xylanase, which produces xylose from oat spelt xylans, was isolated from the culture medium of xylanolytic alkalophylic bacteria mutant. The enzyme was purifi ed by ammonium sulphate with level 30, 40, 50, 60, 70, 80, and 90%. The purify of the fi nal preparation was demonstrated by sodium dodecyl sulphatepolyacrylamide gel electrophoresis. The molecular masses of the purifi ed xylanase were 137.61 and 165.34 kDa. Result of ammonium sulphate saturation with the highest activity was used as standart for saturation for enzyme production and preservation, using corn, tapioca, soy bean meal and gaplek fl our as carriers. Addition of 60% ammonium sulphate showed the highest xylanase activity (62.03 U/g), and produced 89.40% enzyme recovery. Tapioca, as a carrier, produced the highest xylanase activity. Key words: preservation, purifi cation, stability analysis, xylanase.
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28

Elegbede, Joseph Adetunji, and Agbaje Lateef. "Optimization of the production of xylanases in corncob-based media by Aspergillus niger and Trichoderma longibrachiatum using Taguchi approach." Acta Biologica Szegediensis 63, no. 1 (July 25, 2019): 51–58. http://dx.doi.org/10.14232/abs.2019.1.51-58.

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Xylanases are important in producing several commercially valued bioproducts. In this study, xylanases were produced by Aspergillus niger L3 and Trichoderma longibrachiatum L2 using corncob, an agricultural waste, as sole carbon source. The impact of important fermentation parameters at individual and interactive levels were studied using Taguchi L9 orthogonal array. Substantial variation in enzyme synthesis was observed among designated factor levels. The optimal conditions to produce xylanases were 20% inoculum size, 24 h fermentation time, substrate concentration of 15 g/l at pH 5.5 for A. niger L3; and inoculum size 12.5%, 72 h fermentation time, substrate concentration of 15 g/l at pH 5.5 for T. longibrachiatum L2. Validation of outcomes of the optimal combination of parameters resulted in a significant improvement of approximately 208.09 and 192.59% in the yield of xylanase by A. niger L3 (28.69 to 88.39 U/ml) and T. longibrachiatum L2 (22.13 to 64.75 U/ml), respectively. The study therefore established the optimal valorization of corncob to produce xylanase by the fungal isolates.
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29

Andrade, Gislaine da Cunha de, Elis Regina de Moraes Garcia, Charles Kiefer, Fabiana Fonseca Zanoelo, Giovana Cristina Giannesi, Patrícia Gomes Santana, and Danilo Souza Sanches. "Xylanases in diets with alternative feeds and energy reduction in commercial layers." Semina: Ciências Agrárias 42, no. 5 (July 2, 2021): 3007–28. http://dx.doi.org/10.5433/1679-0359.2021v42n5p3007.

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The use of alternative ingredients has been increasing in a continuing attempt to reduce production costs, along with the use of additives, such as carbohydrases, for their possible positive effects on nutrient metabolization by layers. Thus, this study aimed to evaluate the effects of different xylanases in diets with reduced metabolizable energy (ME) and the inclusion of alternative ingredients on the metabolizability of nutrients in diets for commercial laying hens, by conducting two metabolism tests. In the first trial,100 layers hens were distributed in a fully randomized 2 × 2 + 1 factorial design (two metabolizable energy reductions × two xylanases, plus one control diet). In the second assay,140 layer hens were distributed in a fully randomized 2 × 3 + 2 factor design (two xylanases× three ingredients, plus two control diets, positive and negative). It was concluded that supplementation with pantanal xylanase improved the metabolizability of nutrients in corn-based diets and soybean meal for light commercial layers, allowing for a reduction of up to 200 kcal/kg of ME in the diets. Xylanases are more effective on wheat bran enabling a decrease of 150 kcal/kg of ME in commercial laying diets without affecting nutrient metabolizability. The action of pantanal xylanase in diets containing fibrous ingredients was similar to that of commercial xylanase.
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30

Paccanaro, Maria Chiara, Luca Sella, Carla Castiglioni, Francesca Giacomello, Ana Lilia Martínez-Rocha, Renato D’Ovidio, Wilhelm Schäfer, and Francesco Favaron. "Synergistic Effect of Different Plant Cell Wall–Degrading Enzymes Is Important for Virulence of Fusarium graminearum." Molecular Plant-Microbe Interactions® 30, no. 11 (November 2017): 886–95. http://dx.doi.org/10.1094/mpmi-07-17-0179-r.

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Endo-polygalacturonases (PGs) and xylanases have been shown to play an important role during pathogenesis of some fungal pathogens of dicot plants, while their role in monocot pathogens is less defined. Pg1 and xyr1 genes of the wheat pathogen Fusarium graminearum encode the main PG and the major regulator of xylanase production, respectively. Single- and double-disrupted mutants for these genes were obtained to assess their contribution to fungal infection. Compared with wild-type strain, the ∆pg mutant showed a nearly abolished PG activity, slight reduced virulence on soybean seedlings, but no significant difference in disease symptoms on wheat spikes; the ∆xyr mutant was strongly reduced in xylanase activity and moderately reduced in cellulase activity but was as virulent as wild type on both soybean and wheat plants. Consequently, the ΔpgΔxyr double mutant was impaired in xylanase, PG, and cellulase activities but, differently from single mutants, was significantly reduced in virulence on both plants. These findings demonstrate that the concurrent presence of PG, xylanase, and cellulase activities is necessary for full virulence. The observation that the uronides released from wheat cell wall after a F. graminearum PG treatment were largely increased by the fungal xylanases suggests that these enzymes act synergistically in deconstructing the plant cell wall.
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31

Bibra, Mohit, Venkat Kunreddy, and Rajesh Sani. "Thermostable Xylanase Production by Geobacillus sp. Strain DUSELR13, and Its Application in Ethanol Production with Lignocellulosic Biomass." Microorganisms 6, no. 3 (September 5, 2018): 93. http://dx.doi.org/10.3390/microorganisms6030093.

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The aim of the current study was to optimize the production of xylanase, and its application for ethanol production using the lignocellulosic biomass. A highly thermostable crude xylanase was obtained from the Geobacillus sp. strain DUSELR13 isolated from the deep biosphere of Homestake gold mine, Lead, SD. Geobacillus sp. strain DUSELR13 produced 6 U/mL of the xylanase with the beechwood xylan. The xylanase production was improved following the optimization studies, with one factor at a time approach, from 6 U/mL to 19.8 U/mL with xylan. The statistical optimization with response surface methodology further increased the production to 31 U/mL. The characterization studies revealed that the crude xylanase complex had an optimum pH of 7.0, with a broad pH range of 5.0–9.0, and an optimum temperature of 75 °C. The ~45 kDa xylanase protein was highly thermostable with t1/2 of 48, 38, and 13 days at 50, 60, and 70 °C, respectively. The xylanase activity increased with the addition of Cu+2, Zn+2, K+, and Fe+2 at 1 mM concentration, and Ca+2, Zn+2, Mg+2, and Na+ at 10 mM concentration. The comparative analysis of the crude xylanase against its commercial counterpart Novozymes Cellic HTec and Dupont, Accellerase XY, showed that it performed better at higher temperature, hydrolyzing 65.4% of the beechwood at 75 °C. The DUSEL R13 showed the mettle to hydrolyze, and utilize the pretreated, and untreated lignocellulosic biomass: prairie cord grass (PCG), and corn stover (CS) as the substrate, and gave a maximum yield of 20.5 U/mL with the untreated PCG. When grown in co-culture with Geobacillus thermoglucosidasius, it produced 3.53 and 3.72 g/L ethanol, respectively with PCG, and CS. With these characteristics the xylanase under study could be an industrial success for the high temperature bioprocesses.
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32

Stutzenberger, F. J., and A. B. Bodine. "Xylanase production byThermomonospora curvata." Journal of Applied Bacteriology 72, no. 6 (June 1992): 504–11. http://dx.doi.org/10.1111/j.1365-2672.1992.tb01867.x.

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33

Fernández-Espinar, María T., Daniel Ramón, Francisco Piñaga, and Salvador Vallés. "Xylanase production byAspergillus nidulans." FEMS Microbiology Letters 91, no. 2 (March 1992): 91–96. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05190.x.

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34

Kadowaki, Marina K., Cristina G. M. Souza, Rita C. G. Simão, and Rosane M. Peralta. "Xylanase production byAspergillus tamarii." Applied Biochemistry and Biotechnology 66, no. 2 (May 1997): 97–106. http://dx.doi.org/10.1007/bf02788755.

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35

Carmona, Eleonora Cano, Aline A. Pizzirani-Kleiner, Regina T. Rosim Monteiro, and João Atilio Jorge. "Xylanase production byAspergillus versicolor." Journal of Basic Microbiology 37, no. 6 (1997): 387–93. http://dx.doi.org/10.1002/jobm.3620370602.

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36

Sharma, SCD, MS Shovon, AKM Asaduzzaman, MG Sarowar Jahan, T. Yeasmin, and N. Roy. "Optimization of alkali-thermostable and cellulase-free eylanase production from Bacillus Sp." Journal of Bio-Science 19 (December 19, 2012): 7–14. http://dx.doi.org/10.3329/jbs.v19i0.12994.

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Context: To analyze the nutritional and physicochemical parameters for the production of alkali-thermostable and cellulase free xylanase from bacteria. Objectives: The aim of this study was to isolation and identification and of alkali-thermostable and cellulase free xylanase producing bacteria from soil as well as optimization of process parameters for xylanase production. Materials and Methods: The bacterium Bacillus sp. was isolated from soil by serial dilution technique on xylan agar medium and identified by morphological and biochemical studies. The production of xylanase was carried out on xylan broth medium and xylanase activity was assayed by dinitrosalicylic acid (DNS) method. The effect of cultural parameters on the production of xylanase was determined by measuring the activity of xylanase. The effect of temperature and pH on the activity of partially purified xylanase as well as substrate specificity of xylanase were examined. Results: The maximum xylanase production (4000 U/L) by a Bacillus sp. was attained when the medium containing 0.5% wheat bran xylan and peptone at pH 8.0 and 50-55°C within 48-60 h. The partially purified xylanase was optimally active at pH 9.0 and 55°C. The xylanase showed high substrate activity towards wheat bran xylan but no activity towards cellulose, carboxymethyl cellulose and starch. Thus the enzyme was alkali-thermostable and cellulase free xylanase. Conclusion: The results obtained in this study suggest that the Bacillus sp. used is highly potential and useful for the production of cellulase free xylanase. DOI: http://dx.doi.org/10.3329/jbs.v19i0.12994 J. bio-sci. 19: 7-14, 2011
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37

Belorkar, SA, and H. Kausar. "Prelimnary Screening of Molds for Production of Xylanase." Journal of Pure and Applied Microbiology 12, no. 1 (March 30, 2018): 161–64. http://dx.doi.org/10.22207/jpam.12.1.20.

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38

Bérenger, Jean-François, Chantal Frixon, Jacqueline Bigliardi, and Nicole Creuzet. "Production, purification, and properties of thermostable xylanase from Clostridium stercorarium." Canadian Journal of Microbiology 31, no. 7 (July 1, 1985): 635–43. http://dx.doi.org/10.1139/m85-120.

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The production of xylanase and endoglucanase in Clostridium stercorarium has been studied in different conditions. Activities were higher when the organism was grown on xylan and cellulose than on soluble substrates. Catabolite repression of xylanase synthesis occurred when glucose and other readily metabolizable substrates were added during growth on cellulose. Three endoxylanases, A, B, and C, from culture filtrate were purified to homogeneity. Most of the properties of xylanases A, B, and C were similar (optimum pH in the range of 5.5–7.0 at 65 °C; isoelectric pH, 4.4–4.5; Km values of 2.9–3.7 mg/mL). The enzymes were inactivated by Hg2+ and p-chloromercuribenzoate but slight inhibition was obtained with more specific thiol reagents such as 5,5′-dithiobis(2-nitrobenzoic acid) and N-ethylmaleimide. Carbohydrate content (3–19%) and half-life (2 min 30 s to 90 min) varied. Patterns of hydrolysis demonstrate that the three enzymes are endo-splitting enzymes able to break down xylan at random giving xylobiose and xylotriose as the main end products. The three enzymes exhibited immunological cross-reactivity.
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Maestrello, Chadia Chahud, and Luis Henrique Souza Guimarães. "Potential of the Aspergillus labruscus ITAL 22.223 as a producer of cellulolytic enzymes and xylanase under solid-state fermentation." International Journal of Scientific Reports 4, no. 6 (May 22, 2018): 147. http://dx.doi.org/10.18203/issn.2454-2156.intjscirep20182203.

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<p class="abstract"><strong>Background:</strong> The enzymatic hydrolysis of the lignocellulosic biomass to obtain saccharides that can be used for the production of bioethanol is an important field in the renewable energy area. For this purpose, fungal cellulases and xylanases can be applied.</p><p class="abstract"><strong>Methods:</strong> <em>Aspergillus labruscus</em> ITAL 22.223 was cultured under SSF with agroindustrial residues and by-products as substrates, humidified with different moistening agents, at different proportions (1:0.5, 1:1, 1:1.5 and 1:2; m/v), for different periods (24-216 h) at 25ºC. The extract obtained was used for determination of the cellulase and xylanase activities. The influence of temperature, pH and different compounds on xylanase activity was analyzed. </p><p class="abstract"><strong>Results:</strong> <em>A. labruscus</em> produced cellulases and xylanase under solid-state fermentation (SSF) using agroindustrial by products and residues as carbon source/substrates. The best production of β-glucosidase (6.3 U/g of substrate) was obtained in the presence of rye bran, whereas for the CMCase it was in the presence of crushed soybean (5.1 U/g of substrate) and xylanase using oat bran (74.8 U/g of substrate) as substrates, for 168 h of cultivation at 25ºC. Considering the high xylanase production, the best moistening agent and its proportion (tap water, 1:2 m/v) were determined. Optimum of temperature and pH for xylanase activity was determined as 55ºC and pH 5.5. The xylanase activity was inhibited by different salts, with exception of MnSO<sub>4</sub>. It was also inhibited by organic solvents, detergents, EDTA, urea and β-mercaptoethanol.</p><p class="abstract"><strong>Conclusions:</strong> The fungus <em>A. labruscus</em> presented potential to produce enzymes from the cellulolytic complex and xylanase using low cost substrates.</p>
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Herold, Silvia, Robert Bischof, Benjamin Metz, Bernhard Seiboth, and Christian P. Kubicek. "Xylanase Gene Transcription in Trichoderma reesei Is Triggered by Different Inducers Representing Different Hemicellulosic Pentose Polymers." Eukaryotic Cell 12, no. 3 (January 4, 2013): 390–98. http://dx.doi.org/10.1128/ec.00182-12.

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ABSTRACTThe ascomyceteTrichoderma reeseiis a paradigm for the regulation and production of plant cell wall-degrading enzymes, including xylanases. Four xylanases, including XYN1 and XYN2 of glycosyl hydrolase family 11 (GH11), the GH10 XYN3, and the GH30 XYN4, were already described. By genome mining, we identified a fifth xylanase, XYN5, belonging to GH11. Transcriptional analysis reveals that the expression of all xylanases butxyn3is induced byd-xylose, dependent on the cellulase and xylanase regulator XYR1 and negatively regulated by the carbon catabolite repressor CRE1. Impairment ofd-xylose catabolism at thed-xylose reductase and xylitol dehydrogenase step strongly enhanced induction byd-xylose. Knockout of thel-xylulose reductase-encoding genelxr3, which connects thed-xylose andl-arabinose catabolic pathways, had no effect on xylanase induction. Besides the induction byd-xylose, theT. reeseixylanases were also induced byl-arabinose, and this induction was also enhanced in knockout mutants inl-arabinose reductase (xyl1),l-arabitol dehydrogenase (lad1), andl-xylulose reductase (lxr3). Induction byl-arabinose was also XYR1 dependent. Analysis of intracellular polyols revealed accumulation of xylitol in all strains only during incubation withd-xylose and accumulation ofl-arabitol only during incubation withl-arabinose. Induction byl-arabinose could be further stimulated by addition ofd-xylose. We conclude that the expression of theT. reeseixylanases can be induced by bothd-xylose andl-arabinose, but independently of each other and by using different inducing metabolites.
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41

Haniyya, Haniyya, Lina Mulyawati, Is Helianti, Phitsanu Pinmanee, Kanokarn Kocharin, Duriya Cantasingh, and Thidarat Nimchua. "Characterization of recombinant Bacillus halodurans CM1 xylanase produced by Pichia pastoris KM71 and its potential application in bleaching process of bagasse pulp." Indonesian Journal of Biotechnology 26, no. 1 (March 30, 2021): 15. http://dx.doi.org/10.22146/ijbiotech.57701.

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Thermoalkalophilic xylanases promise potential application in pulp biobleaching to reduce the use of toxic chlorinated chemical agents, which are harmful to the environment. In this study, a thermoalkalophilic endoxylanase gene (bhxyn3) originating from Indonesian indigenous Bacillus halodurans CM1 was cloned into yeast expression vector pPICZα A and expressed in Pichia pastoris KM71 under the control of AOX1 promoter. Recombinant P. pastoris expressed the highest final level of xylanase (146 U/mL) on BMGY medium after five days of cultivation. Optimization of xylanase production on a small scale was carried out by varying the methanol concentrations and the optimal xylanase production by the recombinant P. pastoris was observed in the culture with 2% (v/v) methanol after four days of the induction phase. The recombinant xylanase (BHxyn3E) was thermotolerant and alkalophilic, with an optimal temperature at around 55‐65 °C and under pH 8.0. The enzyme activity was slightly induced by K+, Fe2+, and MoO42‐. Enzymatic bleaching of bagasse pulp with no prior pH adjustment (pH 9) using BHxyn3E at 200 U/g oven dried pulp increased the lightness index (L*) and changed substantially the color a index (a*); however, the treatments did not change the whiteness index in a significant way. Therefore, further optimization and assessment such as adjustment of incubation temperature and pH in biobleaching were needed to reduce the use of harmful chemical agents in industrial applications.
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42

Aro, Nina, Marja Ilmén, Anu Saloheimo, and Merja Penttilä. "ACEI of Trichoderma reesei Is a Repressor of Cellulase and Xylanase Expression." Applied and Environmental Microbiology 69, no. 1 (January 2003): 56–65. http://dx.doi.org/10.1128/aem.69.1.56-65.2003.

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ABSTRACT We characterized the effect of deletion of the Trichoderma reesei (Hypocrea jecorina) ace1 gene encoding the novel cellulase regulator ACEI that was isolated based on its ability to bind to and activate in vivo in Saccharomyces cerevisiae the promoter of the main cellulase gene, cbh1. Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression. Growth of the strain with a deletion of the ace1 gene on different carbon sources was analyzed. On cellulose-based medium, on which cellulases are needed for growth, the Δace1 strain grew better than the host strain due to the increased cellulase production. On culture media containing sorbitol as the sole carbon source, the growth of the strain with a deletion of the ace1 gene was severely impaired, suggesting that ACEI regulates expression of other genes in addition to cellulase and xylanase genes. A strain with a deletion of the ace1 gene and with a deletion of the ace2 gene coding for the cellulase and xylanase activator ACEII expressed cellulases and xylanases similar to the Δace1 strain, indicating that yet another activator regulating cellulase and xylanase promoters was present.
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43

Li, Shi Chang, Dong Dong Wang, Zhao Yang Zhu, and Hong Xia Liu. "Breeding of Xylanase-Producing Strains by Ion Implantation and Studying of Fermentation Conditions." Advanced Materials Research 233-235 (May 2011): 1442–46. http://dx.doi.org/10.4028/www.scientific.net/amr.233-235.1442.

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With ion implantation, a high xylanase-producing strainAspergillus nigerBU99 was selected. Different late acting carbon sources (wheat bran, wheat straw, corncob and bagasse) had an effect on enzymatic production. Additionally, it was found that fast acting carbon sources (lactose, galactose, sucrose, glucose and maltose) put into the media affected on xylanase production too. Severe catabolic repression was observed in the media with lactose, but other sugars (galactose, sucrose, glucose and maltose) could increase the production of xylanase compared with the control. The production of xylanase was improved too when corncob flour was hydrolyzed by α-amylase, cellulase or/and glucoamylase. Additionally, it was found that the production of xylanase would be almost higher at 60h when the media contained glucose or were hydrolyzed by enzymes.
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44

Cunha, Luana, Raquel Martarello, Paula Monteiro de Souza, Marcela Medeiros de Freitas, Kleber Vanio Gomes Barros, Edivaldo Ximenes Ferreira Filho, Mauricio Homem-de-Mello, and Pérola Oliveira Magalhães. "Optimization of Xylanase Production from Aspergillus foetidus in Soybean Residue." Enzyme Research 2018 (April 11, 2018): 1–7. http://dx.doi.org/10.1155/2018/6597017.

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Enzymatic hydrolysis is an important but expensive step in the process to obtain enzyme derived products. Thus, the production of efficient enzymes is of great interest for this biotechnological application. The production of xylanase by Aspergillus foetidus in soybean residues was optimized using 2×23 factorial designs. The experimental data was fitted into a polynomial model for xylanase activity. Statistical analyses of the results showed that variables pH and the interaction of pH and temperature had influenced the production of xylanase, with the best xylanase production level (13.98 U/mL) occurring at fermentation for 168 hours, pH 7.0, 28°C, and 120 rpm.
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45

Garg, Sarika. "Xylanase: Applications in Biofuel Production." Current Metabolomics 4, no. 1 (March 2, 2016): 23–37. http://dx.doi.org/10.2174/2213235x03666150915211224.

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46

Royer, J. C., and J. P. Nakas. "Xylanase production by Trichoderma longibrachiatum." Enzyme and Microbial Technology 11, no. 7 (July 1989): 405–10. http://dx.doi.org/10.1016/0141-0229(89)90134-8.

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47

FERNANDEZESPINAR, M. "Xylanase production by Aspergillus nidulans." FEMS Microbiology Letters 91, no. 2 (March 1992): 91–96. http://dx.doi.org/10.1016/0378-1097(92)90665-b.

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48

Piñaga, F., J. L. Peña, and S. Vallés. "Xylanase production by Bacillus polymyxa." Journal of Chemical Technology & Biotechnology 57, no. 4 (April 24, 2007): 327–33. http://dx.doi.org/10.1002/jctb.280570406.

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49

Chaves, Bruno Las-Casas, Ana Paula Martinazzo, Brisabella Coca, Adriane Nunes De Souza, and Carlos Eduardo Teodoro. "Optimization of production and partial characterization of xylanase from a newly isolated Bacillus amyloliquefaciens." Ciência e Natura 42 (May 11, 2020): e9. http://dx.doi.org/10.5902/2179460x42741.

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This paper reports the process of production optimization and partial characterization of xylanase from a newly isolated Bacillus amyloliquefacies VR002, isolated from local soil. The microorganism exhibited maximum xylanase production when 1.0% (v/v) of inoculum size was added to culture medium with initial pH 6, 1.0% (w/v) birchwood xylan, at 35 °C after 48h of incubation. Xylanase production in different carbon sources apart from birchwood xylan and xylose did not show high production levels. Optimum pH for xylanase activity was 6.0. The enzyme was alkali-stable and retained 100% of residual activity over the pH range from 6.0 to 10.0 for 24 h at 25°C. Optimum temperature for enzyme activity was 55°C. Xylanase was 100% stable at 4°C and 25°C even after 24h of incubation, a desirable characteristic for enzyme storage. Moreover, best crude extract volume and time reaction were found to be 10 µL and 5 min, respectively. After optimization of production and activity parameters, an increase of nearly 60-fold in xylanase activity (44.12 ± 4.36 U/mL) was achieved. Characteristics of B. amyloliquefaciens VR002 xylanase are particularly desirable for biotechnological applications
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50

Al Mousa, Amal A., Nageh F. Abo-Dahab, Abdallah M. A. Hassane, Abd El-Rahman F. Gomaa, Jana A. Aljuriss, and Noura D. Dahmash. "Harnessing Mucor spp. for Xylanase Production: Statistical Optimization in Submerged Fermentation Using Agro-Industrial Wastes." BioMed Research International 2022 (April 20, 2022): 1–17. http://dx.doi.org/10.1155/2022/3816010.

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Xylan is the primary hemicellulosic polymer found in lignocellulosic agricultural wastes and can be degraded by xylanase. In the current research, Mucor circinelloides and M. hiemalis were tested for their ability to produce xylanase from tangerine peel by submerged fermentation. Experiments on five variables were designed with Box–Behnken design and response surface methodology. Analysis of variance was exercised, the xylanase output was demonstrated with a mathematical equation as a function of the five factors, and the quixotic states for xylanase biosynthesis was secured. In addition, xylanase was partially purified, characterized, and immobilized on calcium alginate beads. The optimum parameters for xylanase production by M. circinelloides and M. hiemalis were consisted of incubation temperature (30 and 20°C), pH value (9 and 7) incubation period (9 and 9 days), inoculum size (3 and 3 mL), and substrate concentration (3 and 3 g/100 mL), respectively. M. circinelloides and M. hiemalis demonstrated the highest xylanase activities after RSM optimization, with 42.23 and 35.88 U/mL, respectively. The influence of single, interchange, and quadratic factors on xylanase output was investigated using nonlinear regression equations with significant R 2 and p values. The partial purification of M. circinelloides and M. hiemalis xylanase yielded 1.69- and 1.97-fold purification, and 30.74 and 31.34% recovery with 292.08 and 240.15 U/mg specific activity, respectively. Partially purified xylanase from M. circinelloides and M. hiemalis demonstrated the highest activity at neutral pH and 60 and 50°C, respectively. The immobilized M. circinelloides and M. hiemalis xylanase retained 84.02 and 79.43% activity, respectively. The production of xylanase from M. circinelloides and M. hiemalis utilizing RSM is deemed profitable for the decomposition of the agro-industrial wastes.
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