Xylanase Production Research Articles

SwrA as global modulator of the two-component system DegSU in Bacillus subtilis

The two-component system DegSU of Bacillus subtilis controls more than one hundred genes involved in several different cellular behaviours. Over the last four decades, the degU32Hy allele, supposedly encoding a constitutively active mutant of the response regulator DegU, was exploited to define the impact of this system on cell physiology. Those studies concluded that phosphorylated DegU (DegU∼P) induced degradative enzyme expression while repressing flagellar motility and competence.Recent experiments, however, demonstrated that flagella expression is enhanced by DegU∼P if SwrA, a protein only encoded by wild strains, is present. Yet, to promote motility, SwrA must interact with DegU∼P produced by a wild-type degU allele, as it cannot correctly cooperate with the mutant DegU32Hy protein.In this work, the impact of DegSU was reanalysed in the presence or absence of SwrA employing a DegS kinase mutant, degS200Hy, to force the activation of the TCS. Our results demonstrate that the role of SwrA in B. subtilis physiology is wider than expected and affects several other DegSU targets. SwrA reduces subtilisin, cellulases and xylanases production while, besides motility, it also positively modulates competence for DNA uptake, remarkably relieving the inhibition caused by DegU∼P alone and restoring transformability in degS200Hy strains.

Production of multienzyme by Bacillus aestuarii UE25 using ionic liquid pretreated sugarcane bagasse.

The utilization of sugarcane bagasse (SB) in fermentation requires pretreatment processes to render fermentable components available to microorganisms. Pretreatment by using ionic liquids (ILs) is considered promising but the high cost is an impediment in its adoption, therefore, a mixture of IL pretreated and untreated SB was utilized to obtain bacterial multienzyme under solid-state fermentation (SSF). Bacillus aestuarii UE25, a thermophilic strain was utilized for that purpose. Fermentation conditions were optimized by adopting a central composite design. The model showed a good correlation between the predicted and the experimental values for amylase, xylanase, endoglucanase, and β-glucosidase. Volumetric and specific productivity of xylanase (4580 IU ml-1 h-1 , 244.25 IU mg-1 substrate, and 50 IU mg-1 protein) were higher than the other enzymes. Changes in lignin content and reduced cellulose crystallinity due to IL pretreatment, followed by fermentation, were visualized by scanning electron microscopy, Fourier transform infrared spectroscopy, and Nuclear magnetic resonance. The strategy adopted by utilizing a mixture of IL pretreated and untreated SB under SSF proved promising to obtain high titers of different enzymes simultaneously. Since the bacterial strain used is thermophilic, therefore, the multienzyme can find its application in commercial processes which are carried out at high temperatures.

Use of Wheat Straw for Value-Added Product Xylanase by Penicillium chrysogenum Strain A3 DSM105774.

The present work highlights the valorization of the bulky recalcitrant lignocellulose byproduct wheat straw (WS) for the enhanced production of value-added xylanase by the locally sourced novel Penicillium chrysogenum strain A3 DSM105774 for the first time. The optimized production of xylanase by submerged state of fermentation of WS was achieved using a three-step statistical and sequential approach: one factor at a time (OFAT), Plackett–Burman design (PBD), and Box Behnken design (BBD). Incubation temperature (30 °C), WS, and ammonium sulphate were the key determinants prompting xylanase production; inferred from OFAT. The WS concentration (%(w/v)), yeast extract concentration (%(w/v)), and initial pH of the production medium imposed significant effects (p ≤ 0.05) on the produced xylanase, realized from PBD. The predicted levels of WS concentration, initial pH of the production medium, and yeast extract concentration provoking the ultimate xylanase levels (53.7 U/mL) with an 8.95-fold enhancement, localized by the estimated ridge of the steepest ascent of the ridge analysis path, were 3.8% (w/v), 5.1, and 0.098% (w/v), respectively; 94.7% lab validation. The current data underpin the up-scaling of xylanase production using this eco-friendly, cheap, and robust methodology for the valorization of WS into the value-added product xylanase.

Improved Production of Xylanase in Pichia pastoris and Its Application in Xylose Production From Xylan

Xylanases with high specific activity has been focused with great interest as a useful enzyme in biomass utilization. The production of recombinant GH11 xylanase (MYCTH_56237) from Myceliophthora thermophila has been improved through N-terminal signal peptide engineering in P. pastoris. The production of newly recombinant xylanase (termed Mtxyn11C) was improved from 442.53 to 490.7 U/mL, through a replacement of α-factor signal peptide with the native xylanase signal peptide segment (MVSVKAVLLLGAAGTTLA) in P. pastoris. Scaling up of Mtxyn11C production in a 7.5 L fermentor was improved to the maximal production rate of 2503 U/mL. In this study, the degradation efficiency of Mtxyn11C was further examined. Analysis of the hydrolytic mode of action towards the birchwood xylan (BWX) revealed that Mtxyn11C was clearly more effective than commercial xylanase and degrades xylan into xylooligosaccharides (xylobiose, xylotriose, xylotetraose). More importantly, Mtxyn11C in combination with a single multifunctional xylanolytic enzyme, improved the hydrolysis of BWX into single xylose by 40%. Altogether, this study provided strategies for improved production of xylanase together with rapid conversion of xylose from BWX, which provides sustainable, cost-effective and environmental friendly approaches to produce xylose/XOSs for biomass energy or biofuels production.

Paecilomyces variotii xylanase production, purification and characterization with antioxidant xylo-oligosaccharides production

Paecilomyces variotii xylanase was, produced in stirred tank bioreactor with yield of 760 U/mL and purified using 70% ammonium sulfate precipitation and ultra-filtration causing 3.29-fold purification with 34.47% activity recovery. The enzyme purity was analyzed on sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) confirming its monomeric nature as single band at 32 KDa. Zymography showed xylan hydrolysis activity at the same band. The purified enzyme had optimum activity at 60 °C and pH 5.0. The pH stability range was 5–9 and the temperature stability was up 70 °C. Fe2+and Fe3+ exhibited inhibition of xylanase enzyme while Cu2+, Ca2+, Mg2+ and Mn2+ stimulated its activity. Mercaptoethanol stimulated its activity; however, Na2-EDTA and SDS inhibited its activity. The purified xylanase could hydrolyze beechwood xylan but not carboxymethyl cellulose (CMC), avicel or soluble starch. Paecilomyces variotii xylanase Km and Vmax for beechwood were determined to be 3.33 mg/mL and 5555 U/mg, respectively. The produced xylanase enzyme applied on beech xylan resulted in different types of XOS. The antioxidant activity of xylo-oligosaccharides increased from 15.22 to 70.57% when the extract concentration was increased from 0.1 to 1.5 mg/mL. The enzyme characteristics and kinetic parameters indicated its high efficiency in the hydrolysis of xylan and its potential effectiveness in lignocellulosic hydrolysis and other industrial application. It also suggests the potential of xylanase enzyme for production of XOS from biomass which are useful in food and pharmaceutical industries.

Optimization of cellulase and xylanase production by Aspergillus niger CECT 2700 using brewery spent grain based on Taguchi design

Optimization of cellulase and xylanase production by Aspergillus niger CECT 2700 using brewery spent grain based on Taguchi design

Screening of Fungal Strains for Cellulolytic and Xylanolytic Activities Production and Evaluation of Brewers’ Spent Grain as Substrate for Enzyme Production by Selected Fungi

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.

Production, Purification and Characterization of Xylanase Enzyme from <i>Bacillus sp</i> in Solid State Fermentation

Xylanases are extensively applied in paper and pulp industries as well as during preparation of baked products to improve their quality. Additionally, it is also used in coffee, oil and starch industries in order to increase their nutritional values. Soil samples were collected near saw mills in various localities of Bangalore urban to isolate organisms for the production of xylanase using solid state fermentation. Six organisms were isolated using selective media based on their morphological characters. Among them one organism showed maximum production of xylanase enzyme identified as Bacillus sp based on their biochemical test and 16s RNA sequencing. Solid substrate fermentation was carried out using various agro wastes such as sugar cane bagasse, saw dust, paddy husk, wheat straw and orange peel powder. Sugarcane bagasse showed maximum production of enzyme compared to other substrates with different physical parameters such as pH 8, temperature at 35 °C after 72 hrs of incubation. Trace element such as Mg++ enhances the production of enzyme more than 22 % compared with other metal ions like Ca++, Mn++ and Fe++. After production, enzyme purified by using three step methods such ammonium sulphate precipitation, dialysis, ion exchange and gel filtration. Fold purification was increased up to 12 fold, yield 36 % and molecular weight of enzyme was 62 KDa determined using SDS PAGE.

Optimization of Conditions for Xylanase Production Using Aspergillus tubingensis Under Different Carbon Sources

Xylanases are hydrolytic enzymes with wide range of applications in food processing, bleaching of pulp in paper manufacturing industry, bio-conversion of biomass wastes to fermentable sugars and enhancing nutrient digestibility in animal feeds. The optimization of growth conditions and evaluation of an appropriate substrate as carbon source among cassava peels, corn cobs, wheat bran and rice husk on xylanase production by novel strain of Aspergillus tubingensis under Solid State Fermentation (SSF) was investigated. The fungal isolate was identified based on ribosomal RNA gene and ITS gene sequencing analysis as Aspergillus tubingensis. Results showed that Corn cobs had the highest xylanase production among the four substrates. Corn cobs recorded the highest value of xylanase production at pH of 6.0 (107.97 U/g), after incubation period of 72 hour (111.23 U/g), at temperature of 30oC (44.26 U/g) and at ratio 1:3 (45.68 U/g). The optimum growth conditions for xylanase production by Aspergillus tubingensis were: pH 6.0, incubation period of 72 hours, temperature of 30oC and substrate concentration of 1:3 (4g of substrate per 12ml of fermentation medium). Corn cobs showed the highest yield of xylanase activity (111.23±0.31 U/g), followed by Rice husk (101.91±0.72 U/g), Wheat bran (89.30±1.16 U/g) and Cassava peel (87.03±0.57 U/g). In conclusion, among the various agro residues that were used as carbon sources, Corn cobs had maximum xylanase activity. Various culture conditions were optimized by using one factor at a time method and the maximum xylanase production was obtained at pH of 6.0, incubation period of 72 hour, temperature of 30oC and substrate concentration of 1:3 under solid state fermentation. It is therefore suggested that some other notable environmental and fermentation factors that influence metabolism-mediated production yields of xylanase like aeration, agitation, carbon and nitrogen sources, metal ion requirement, inoculum size etc. should be optimized for maximum production of enzyme. Keywords: Solid State Fermentation, Cassava peels, Corn cobs, Wheat bran, Rice husk

Optimization of hydrolases production from cassava peels by Trametes polyzona BKW001

The saccharification of biomass with hydrolases from fungi is considered as an efficient and sustainable approach to obtain fermentable sugars. The expression of these hydrolytic enzymes by fungi is mainly by a substrate-induced mechanism, which depends on prevailing environmental conditions. Trametes polyzona, a white rot fungus, is regarded as one of the most efficient producers of hydrolases for the hydrolysis of biomass. This study sought to examine and optimize cultivation conditions for the efficient production of hydrolases by Trametes polyzona (T. polyzona). Hydrolase production by T. polyzona was examined using parametric optimization. Crude enzyme extracts obtained under varying cultivation conditions were profiled for endoglucanase, betaglucosidase, exoglucanase, xylanase and amylase activities to determine the optimal conditions for hydrolase production. Significantly (p ≤ 0.05) higher endoglucanase (1.97 ± 0.04 U/mL), xylanase (0.87 ± 0.05 U/mL) and amylase (1.16 ± 0.27 U/mL) activities were achieved by the solid-state cultivation in comparison to the submerged cultivation of T. polyzona. Maximum production of endoglucanase, betaglucosidase, exoglucanase, xylanase and amylase were recorded at 14 days of cultivation on cassava peels, 60% moisture level, temperature 30°C, pH 6, and supplementation with 0.3% w/w urea and 0.03% w/w Mg2+. A solid to liquid ratio of 1:2 was found to be ideal for the solid-liquid extraction of hydrolases. This study has proven that optimization of cultivation conditions is an efficient approach to enhance hydrolases production by T. polyzona BKW001. The hydrolase profile of the enzyme cocktail suggests a potential suitability and adoption for ethanol biorefinery from lignocellulosic biomass.

Purification and characterization of a highly-stable fungal xylanase from Aspergillus tubingensis cultivated on palm wastes through combined solid-state and submerged fermentation

Fungal xylanase was produced from lignocellulosic palm wastes through combined solid-state fermentation (SSF) and submerged fermentation (SmF) by Aspergillus tubingensis TSIP9 in a helical-impeller equipped bioreactor. The combined SSF–SmF promoted the xylanase production by 15 and 70% higher than SSF and SmF, respectively. Sequential purification yielded 7.4-fold purified xylanase with 9.07% recovery. The maximum activities of crude and purified xylanase were observed at the same pH of 5.0 and the same temperature of 50 °C while purified xylanase is more active and highly stable at a wider pH range of 3–8 and temperature of 30−60 °C. The half-life of purified xylanase at various temperatures was also much improved by 2−8 folds compared to crude xylanase. Michaelis–Menten constants, V max and K m, for purified xylanase are 2,602.8 U/mg and 32.4 mg/mL, respectively. Purified xylanase activity was most enhanced with Ca2+ followed by Zn2+ and Fe2+ at 10 mM while significantly inhibited by Co2+, Cu2+, Pb2+, and Ag+. This study has shown the effectiveness of combined SSF–SmF for xylanase production and superior properties of purified xylanase for industrial processes.

Xylanase production by halophilic bacterium Gracilibacillus sp. TSCPVG under solid state fermentation

We previously demonstrated the production and purification of novel halo-acid-alkali-thermo-stable xylanase from halophilic bacterium Gracilibacillus sp. TSCPVG using submerged fermentation (SmF). In this work, we further showed the production of halophilic xylanase by solid state fermentation (SSF) from halophilic bacterium Gracilibacillus sp. TSCPVG using cheap solid-substrate wheat bran. High levels of enzyme titers (657 U/g dw) were obtained after varying certain SSF parameters such as incubation period, particle size, moisture ratio, salinity, pH, temperature and by supplementing different carbon and nitrogen sources externally to the fermentation medium. This bacterium could be a novel strain due to its ability to produce high titers of xylanase with extremophilic characters even under the conditions of SSF. Thus, this beneficiary role may lead to a substantial reduction in the overall cost of enzyme production and may have a huge impact on the economics of hemicellulose degradation under high saline conditions.

Multi-efficient thermostable endoxylanase from Bacillus velezensis AG20 and its production of xylooligosaccharides as efficient prebiotics with anticancer activity

In this study, we have unveiled the novel potential of xylanase production by Bacillus velezensis, previously known only for its PGPR traits. According to our investigations, Bacillus velezensis AG20 produced extracellular xylanase with a fold purification of 5.3 and a yield of 21 %. The purified xylanase (45 kDa) aptly cleaved linear β-(1→4)-xylan with a maximum velocity of 21.0 ± 3.0 U/mL, a turnover of 1.75/s, and a catalytic cycle of 0.571 at optimum pH 7. The temperature of 50 °C was found optimum for enzyme activity. Purified endoxylanase was thermostable and retained its significant residual activities at 50 °C and 60 °C. Metal cations such as Ca2+ and Mg2+ enhanced the substrate catalysis up to 1.5 fold. The purified endoxylanase also demonstrated multi-substrate hydrolyzing properties. However, the enzymatic hydrolysis of sugarcane bagasse produced xylooligosaccharides (XOS), including xylobiose, xylotriose, and xylotetrose. The mixture of released XOS has profound stability in gastric juice, intestinal fluid, and α-amylase and facilitates probiotic bacteria Bifidobacterium. The mixed XOS (300 μg/mL) significantly inhibited the HT-29 and Caco-2 cell proliferation by 90 % and 75 %, respectively, at 48 h. The possible mechanism of XOS uptake through the BIAXP receptor of Bifidobacterium has been contemplated and established using the caver analysis, Molecular Dynamics (MD) simulation, and Density Functional Theory (DFT) studies. Thus, here we reveal the utility of this novel bacterial strain in industries as high-temperature catalysts.

Improvement of cellulase and xylanase production in Penicillium oxalicum under solid-state fermentation by flippase recombination enzyme/ recognition target-mediated genetic engineering of transcription repressors

Penicillium oxalicum has received increasing attention as a potential cellulase-producer. In this study, a copper-controlled flippase recombination enzyme/recognition target (FLP/FRT)-mediated recombination system was constructed in P. oxalicum, to overcome limited availability of antibiotic resistance markers. Using this system, two crucial transcription repressor genes atf1 and cxrC for the production of cellulase and xylanase under solid-state fermentation (SSF) were simultaneously deleted, thereby leading to 2.4- to 29.1-fold higher cellulase and 78.9% to 130.8% higher xylanase production than the parental strain under SSF, respectively. Glucose and xylose released from hydrolysis of pretreated sugarcane bagasse achieved 10.6%–13.5% improvement by using the crude enzymes from the engineered strain Δatf1ΔcxrC::flp under SSF in comparison with that of the parental strain. Consequently, these results provide a feasible strategy for improved cellulase and xylanase production by filamentous fungi.

Cellulase and Xylanase Production by Sugarcane Bagasse Mycobiota

Cellulase and Xylanase Production by Sugarcane Bagasse Mycobiota

Cellulolytic enzymes production guided by morphology engineering

Endoglucanase and xylanase are critical enzymes for liquefaction and enzyme hydrolysis of high solids lignocellulosic biomass to facilitate its transport and production of desired derived products. Here is reported how combinations of different spore concentrations and pH influence microbial morphology, and how this may be used to direct expression and secretion of enzymes by Aspergillus niger. While xylanase production is not affected by A. niger morphology changes, endoglucanase production is enhanced under conditions of lower stress and by morphology that results in pellets. β-glucosidase production is enhanced under dispersed morphology, which results in up to fourfold increase of this enzyme production under the tested experimental conditions. A morphologic scale (Y) is proposed based on a form factor that considers the size and frequency of each morphology class, and that points to conditions that result in high selectivity for either endoglucanase or β-glucosidase production. An equation proposed to relate enzyme activity to morphology provides a useful tool for tuning enzyme production of A. niger, where morphology is a first indication of relative enzyme activities in a fermentation broth.

Optimisation of xylanases production by two Cellulomonas strains and their use for biomass deconstruction

One of the main distinguishing features of bacteria belonging to the Cellulomonas genus is their ability to secrete multiple polysaccharide degrading enzymes. However, their application in biomass deconstruction still constitutes a challenge. We addressed the optimisation of the xylanolytic activities in extracellular enzymatic extracts of Cellulomonas sp. B6 and Cellulomonas fimi B-402 for their subsequent application in lignocellulosic biomass hydrolysis by culture in several substrates. As demonstrated by secretomic profiling, wheat bran and waste paper resulted to be suitable inducers for the secretion of xylanases of Cellulomonas sp. B6 and C. fimi B-402, respectively. Both strains showed high xylanolytic activity in culture supernatant although Cellulomonas sp. B6 was the most efficient xylanolytic strain. Upscaling from flasks to fermentation in a bench scale bioreactor resulted in equivalent production of extracellular xylanolytic enzymatic extracts and freeze drying was a successful method for concentration and conservation of the extracellular enzymes, retaining 80% activity. Moreover, enzymatic cocktails composed of combined extra and intracellular extracts effectively hydrolysed the hemicellulose fraction of extruded barley straw into xylose and xylooligosaccharides.Key points• Secreted xylanase activity of Cellulomonas sp. B6 and C. fimi was maximised.• Biomass-induced extracellular enzymes were identified by proteomic profiling.• Combinations of extra and intracellular extracts were used for barley straw hydrolysis.

Production of cellulases and xylanases in solid-state fermentation by different strains of Aspergillus niger using sugarcane bagasse and brewery spent grain

The objective of this study was to evaluate the effect of sugarcane bagasse (SCB) and brewery spent grain (BSG) on xylanase and cellulase enzymes production using different strains: Aspergillus niger CECT 2700, A. niger CECT 2915 and A. niger ITV-01 growing up in solid-state fermentation (SSF). Both lignocellulosic residues were previously subjected to three pretreatments: alkaline, boiling water, and autoclave. The maximum cellulase activity was 6.23 U/g of a dry substrate (gds) using A. niger CECT 2700 and BSG pretreated with boiling water. Further, the highest xylanase activity (1400.80 U/gds) was obtained using BSG pretreated in autoclave with A. niger CECT 2700 strain. Also, the highest cellulases and xylanases production was recorded on day 5 with a microbial load of 5 × 106 spores/gds. Finally, the enzymatic extract from A. niger CECT 2700 reached maximum saccharification in alkaline pretreated SCB of 68.52 and 78.66 % of glucan and xylan, respectively. This investigation showed the feasibility to obtain an enzymatic extract with xylanase and cellulase activity using low-cost substrates such as SCB and BSG.

Cloning and Heterologous Expression of a Novel Xylanase Gene TAX1 from Trichoderma atroviride and Its Application in the Deconstruction of Corn Stover.

Xylanase plays a vital role in the efficient utilization of xylan, which accounts for up to 30% of plant dry matter. However, the production cost of xylanase remains high, and the enzymatic characteristics of xylanases of most microorganisms are not suitable for industrial production. Therefore, it is of great significance to discover and develop new and efficient xylanases. In this study, the xylanase gene TAX1 (672 bp cDNA) was cloned from Trichoderma atroviride 3.3013 and expressed in Pichia pastoris. The TAX1 gene encoded a 223-amino acid protein (TAX1) with a molecular weight of 24.2 kDa which showed high similarity to glycoside hydrolase family 11. Enzyme activity assay verified that the recombinant xylanase TAX1 had optimal activity (215.3 IU/mL) at 50°C and pH 6.0. Stable working conditions were measured as pH 4.0-7.0 and 40-60°C. By adding Zn2+, the relative enzymatic activity of recombinant TAX1 was enhanced by 26%. The recombinant xylanase showed high activity toward birchwood xylan and corn stover. The Km and Kcat for xylan and corn stover were 0.36 mg/mL and 0.204 S-1 and 0.48 mg/mL and 0.149 S-1, respectively. The enzymatic activity of the TAX1 produced by P. pastoris was about 2.4-4 times higher that directly isolated from T. atroviride, so engineered P. pastoris for xylanase production could be an ideal candidate for industrial enzyme production.

Efficient utilization of waste paper as an inductive feedstock for simultaneous production of cellulase and xylanase by Trichoderma longiflorum

Waste paper, one of the major components of municipal and industrial wastes, has considerable potential as a low-cost inductive feedstock for enzyme production. In this study, four kinds of waste papers were used for simultaneous production of cellulase and xylanase by Trichoderma longiflorum. The highest FPase activities (3.21 IU/mL and 2.97 IU/mL) were achieved using waste office paper (WOP) and corrugated board (CB), respectively, followed by magazine paper (MP, 2.51 IU/mL) and tissue paper (TP, 2.34 IU/mL). The maximum β-glucosidase activities (0.51 IU/mL) and xylanase activities (382.59 IU/mL) were obtained from CB substrates, which were higher than that in the reported literature using waste paper. Correspondingly, the soluble protein concentrations and SDS-PAGE profiles from CB fermentation revealed that more enzymes were secreted during fermentation compared with other waste paper. Moreover, the structural features of different waste paper were characterized by using SEM and XRD technique and revealed that the structural variations were mainly caused by the raw wood sources and papermaking processes, and further affected the fermentation capacity. In addition, a higher β-glucosidase activity of 0.80 IU/mL were obtained from the mixed carbon source of CB and wheat bran (WB), which were significantly improved and increased by 56.86% when compared with the CB as single carbon source. This study confirmed that the waste paper without pretreatment could be efficiently utilized as an inductive feedstock for simultaneous production of cellulase and xylanase by T. longiflorum. Therefore, these findings obtained from this study will provide a more widely insight into investigating the low-cost inductive feedstock for enzyme production, which were of great benefit both for the economy and environment.