Showing papers on "Xylanase published in 2020"

Bioethanol Production from Food Waste Applying the Multienzyme System Produced On-Site by Fusarium oxysporum F3 and Mixed Microbial Cultures

Abstract: Waste management and production of clean and affordable energy are two main challenges that our societies face. Food waste (FW), in particular, can be used as a feedstock for the production of ethanol because of its composition which is rich in cellulose, hemicellulose and starch. However, the cost of the necessary enzymes used to convert FW to ethanol remains an obstacle. The on-site production of the necessary enzymes could be a possible solution. In the present study, the multienzyme production by the fungus Fusarium oxysporum F3 under solid state cultivation using different agroindustrial residues was explored. Maximum amylase, glucoamylase, endoglucanase, b-glucosidase, cellobiohydrolase, xylanase, b-xylosidase and total cellulase titers on wheat bran (WB) were 17.8, 0.1, 65.2, 27.4, 3.5, 221.5, 0.7, 0.052 and 1.5 U/g WB respectively. F. oxysporum was used for the hydrolysis of FW and the subsequent ethanol production. To boost ethanol production, mixed F. oxysporum and S. cerevisiae cultures were also used. Bioethanol production by F. oxysporum monoculture reached 16.3 g/L (productivity 0.17 g/L/h), while that of the mixed culture was 20.6 g/L (productivity 1.0 g/L/h). Supplementation of the mixed culture with glucoamylase resulted in 30.3 g/L ethanol with a volumetric productivity of 1.4 g/L/h.

Greener approach for pulp and paper industry by Xylanase and Laccase

Abstract: Pulp and paper manufacturing units effectuate large amounts of waste water, causing water pollution. As the generated waste water consists perilous organo-chlorine compounds exuded during various stages of paper manufacturing, thereby meticulously impacting life. Biotechnology recommends some economical and non-polluting practices such as use of enzymes for the significant reduction in the pollution load on the water bodies. Enzymes such as Xylanase and Laccase alone or in cocktail have tremendous potential to be administered as bio-bleaching agents for they are active, renewable, non-polluting, mild, highly specific and affordable and significant for improving the grade of paper. Xylanase, the hydrolytic enzymes act on the dislocated, re-precipitated xylan onto the surface of cellulose fibres, thereby improving bleaching of paper pulp whereas Laccase, the multi-copper oxidoreductases revamp bleaching by accomplishing one electron oxidation. Sterling bio-bleaching outcome of Xylanase and Laccase alone has gained grounds for bio-bleaching via “Xylanase and Laccase” cocktail with the exception of being more economical and offering more stability. This review article throws light on biological systems (bio-bleaching enzymes) to reduce or replace the usage of harmful bleaching chemicals for a cleaner and greener environment.

Xylanase and xylo- oligosaccharide prebiotic improve the growth performance and concentration of potentially prebiotic oligosaccharides in the ileum of broiler chickens.

Abstract: 1. The objective of this study was to investigate the effect of supplementing broiler diets with xylanase or xylo- oligosaccharide (XOS) on growth performance, the concentration of non-starch polys...

Banana Peels: A Promising Substrate for the Coproduction of Pectinase and Xylanase from Aspergillus fumigatus MS16.

Abstract: Banana peels (BP), an under-utilized waste material, was studied for the production of xylanase and pectinase by Aspergillus fumigates MS16. The factors affecting the co-production of both the enzymes were separately studied for their influence under submerged (Smf) and solid-state fermentation (SSF) of BP. The strain was cultivated in the presence of mineral salt (MS) solution containing BP powder as a sole source of carbon and physical and nutritional factors varied to observe the change in the enzyme titers. The data revealed that the MS-based medium was appropriate for the production of both the enzymes; therefore, in subsequent experiments, the same medium was used. A temperature of 30-35°C was found better for the production of the two enzymes under Smf; however, the titers of pectinase dropped significantly at 40°C. Contrarily, xylanase production was inhibited at 40°C under SSF but not under Smf. Whereas, supplementation of xylan or pectin to BP induced the production of xylanase and pectinase, respectively. Lowering the pH value favored the production of both the enzymes under Smf; however, the production of pectinase improved significantly when a higher concentration of BP (1%) was used compared to the concentration (0.25%) required for the production of xylanase. Interestingly, the enzyme preparation obtained under SSF exhibited optimal activities of both the enzymes at higher temperatures when compared to those obtained under Smf. The data indicated that the physiology of the fungus differed greatly when the cultivation pattern varied from Smf to SSF and, hence, the enzymes produced were characteristically distinct. Banana peels (BP), an under-utilized waste material, was studied for the production of xylanase and pectinase by Aspergillus fumigates MS16. The factors affecting the co-production of both the enzymes were separately studied for their influence under submerged (Smf) and solid-state fermentation (SSF) of BP. The strain was cultivated in the presence of mineral salt (MS) solution containing BP powder as a sole source of carbon and physical and nutritional factors varied to observe the change in the enzyme titers. The data revealed that the MS-based medium was appropriate for the production of both the enzymes; therefore, in subsequent experiments, the same medium was used. A temperature of 30–35°C was found better for the production of the two enzymes under Smf; however, the titers of pectinase dropped significantly at 40°C. Contrarily, xylanase production was inhibited at 40°C under SSF but not under Smf. Whereas, supplementation of xylan or pectin to BP induced the production of xylanase and pectinase, respectively. Lowering the pH value favored the production of both the enzymes under Smf; however, the production of pectinase improved significantly when a higher concentration of BP (1%) was used compared to the concentration (0.25%) required for the production of xylanase. Interestingly, the enzyme preparation obtained under SSF exhibited optimal activities of both the enzymes at higher temperatures when compared to those obtained under Smf. The data indicated that the physiology of the fungus differed greatly when the cultivation pattern varied from Smf to SSF and, hence, the enzymes produced were characteristically distinct.

A new synergistic relationship between xylan-active LPMO and xylobiohydrolase to tackle recalcitrant xylan

Abstract: Hemicellulose accounts for a significant part of plant biomass, and still poses a barrier to the efficient saccharification of lignocellulose. The recalcitrant part of hemicellulose is a serious impediment to the action of cellulases, despite the use of xylanases in the cellulolytic cocktail mixtures. However, the complexity and variety of hemicelluloses in different plant materials require the use of highly specific enzymes for a complete breakdown. Over the last few years, new fungal enzymes with novel activities on hemicelluloses have emerged. In the present study, we explored the synergistic relationships of the xylan-active AA14 lytic polysaccharide monooxygenase (LPMO), PcAA14B, with the recently discovered glucuronoxylan-specific xylanase TtXyn30A, of the (sub)family GH30_7, displaying xylobiohydrolase activity, and with commercial cellobiohydrolases, on pretreated natural lignocellulosic substrates. PcAA14B and TtXyn30A showed a strong synergistic interaction on the degradation of the recalcitrant part of xylan. PcAA14B was able to increase the release of xylobiose from TtXyn30A, showing a degree of synergism (DS) of 3.8 on birchwood cellulosic fibers, and up to 5.7 on pretreated beechwood substrates. The increase in activity was dose- and time- dependent. A screening study on beechwood materials pretreated with different methods showed that the effect of the PcAA14B–TtXyn30A synergism was more prominent on substrates with low hemicellulose content, indicating that PcAA14B is mainly active on the recalcitrant part of xylan, which is in close proximity to the underlying cellulose fibers. Simultaneous addition of both enzymes resulted in higher DS than sequential addition. Moreover, PcAA14B was found to enhance cellobiose release from cellobiohydrolases during hydrolysis of pretreated lignocellulosic substrates, as well as microcrystalline cellulose. The results of the present study revealed a new synergistic relationship not only among two recently discovered xylan-active enzymes, the LPMO PcAA14B, and the GH30_7 glucuronoxylan-active xylobiohydrolase TtXyn30A, but also among PcAA14B and cellobiohydrolases. We hypothesize that PcAA14B creates free ends in the xylan polymer, which can be used as targets for the action of TtXyn30A. The results are of special importance for the design of next-generation enzymatic cocktails, able to efficiently remove hemicelluloses, allowing complete saccharification of cellulose in plant biomass.

Characterization of a novel xylanase from an extreme temperature hot spring metagenome for xylooligosaccharide production.

Abstract: In this study, the metagenomic resource generated from an aquatic habitat of extreme temperature was screened for the identification of a novel xylanase, XynM1. Gene sequence analysis designated it as a member of glycoside hydrolase (GH) family 10. The metagenomic DNA fragment was cloned, expressed in Escherichia coli, and the purified protein was biochemically characterized. The optimum temperature and pH for the XynM1 xylanase were found to be at 80 °C and 7, respectively. It exhibited worthwhile pH stability by retaining about 70% activity in the range of pH 6 to 9 after the exposure for 12 h at 25 °C. Thermostability analysis established considerable heat tolerance in XynM1 protein at elevated temperatures, displaying about 50% residual activity after the exposure of 40 °C, 50 °C, 60 °C, and 70 °C for 20 h, 12 h, 6 h, and 1.5 h, respectively. The effects of additives such as metals, surfactants, and organic solvents were evaluated on the activity of XynM1. It was able to retain about 50% of its initial activity in the presence of NaCl concentration of 1 to 5 M. The novel xylanase was capable of hydrolyzing the hemicellulosic polymer, derived from diverse biomass sources, e.g., beechwood xylan, wheat arabinoxylan, corncob xylan, and sweet sorghum xylan. The XynM1-treated beechwood xylan manifested catalytic release of xylooligosaccharides (XOS) of 2–6 DP. The novel GH10 xylanase is a promising biocatalyst that could be ascribed for biomass conversion and production of prebiotic XOS biomolecules.

Optimization of the solid-state fermentation conditions and characterization of xylanase produced by Penicillium roqueforti ATCC 10110 using yellow mombin residue (Spondias mombin L.)

Abstract: Yellow mombin residue was investigated as a substrate for the production of xylanase by Penicillium roqueforti ATCC 10110 in solid-state fermentation. The parameters incubation temperature, initial...

Optimization of concurrent production of xylanolytic and pectinolytic enzymes by Bacillus safensis M35 and Bacillus altitudinis J208 using agro-industrial biomass through Response Surface Methodology

Abstract: Application of crude xylanolytic and pectinolytic enzymes in diverse industrial processes make these enzymes commercially valuable and demand their production process to be cost-effective. Out of four different agrowaste biomass, wheat bran (WB) and citrus peel (CP), when amended as fermentation substrates, respectively induced the highest xylanolytic enzymes and pectinolytic enzymes from both, B. safensis M35 and B. altitudinis J208. Further, the simultaneous amendment of WB and CP yielded concurrent production of these cellulase free xylanolytic and pectinolytic enzymes. Hence, the quadratic model was developed using the Central Composite Design of Response Surface Method (CCD-RSM). The model gave the concentration values for WB and CP substrates to be amended in one single production medium for obtaining two optimized predicted response values of xylanase activity and pectinase activity units, which were further practically validated for the xylanase and pectinase production responses from the optimized production medium (OPM). These practically obtained response values from OPM were found to be in accordance with a range of 95% predicted intervals (PI) values. These observations verified the validity of the predicted quadratic model from RSM and suggested that both xylanase and pectinase enzymes can be induced concurrently from both of the bacterial strains.

Consolidated bioprocessing performance of a two-species microbial consortium for butanol production from lignocellulosic biomass.

Abstract: Consolidated bioprocessing (CBP) by using microbial consortium was considered as a promising approach to achieve direct biofuel production from lignocellulose. In this study, the interaction mechanism of microbial consortium consisting of Thermoanaerobacterium thermosaccharolyticum M5 and Clostridium acetobutylicum NJ4 was analyzed, which could achieve efficient butanol production from xylan through CBP. Strain M5 possesses efficient xylan degradation capability, as 19.73 g/L of xylose was accumulated within 50 hr. The efficient xylose utilization capability of partner strain NJ4 could relieve the substrate inhibition to hydrolytic enzymes of xylanase and xylosidase secreted by strain M5. In addition, the earlier solventogenesis of strain NJ4 was observed due to the existence of butyrate generated by strain M5. The mutual interaction of these two strains finally gave 13.28 g/L of butanol from 70 g/L of xylan after process optimization, representing a relatively high butanol production from hemicellulose. Moreover, 7.61 g/L of butanol was generated from untreated corncob via CBP. This successfully constructed microbial consortium exhibits efficient cooperation performance on butanol production from lignocellulose, which could provide a platform for the emerging butanol production from lignocellulose.

Eco-friendly scouring of ramie fibers using crude xylano-pectinolytic enzymes for textile purpose

Abstract: This study was carried out to demonstrate the biotechnological potential of xylano-pectinolytic enzymes on scouring of ramie fibers. Optimization of bioscouring process showed a maximum effect of enzymes with 50-mM strength of buffer, pH 8.5, fibers to liquid ratio of 1 : 20 (g:ml). Xylanase and pectinase dosage of 7.5 and 3.0 IU, respectively, was found to be best for removal of xylan and pectin impurities, after treatment time of 1.5 h, at 50 °C temperature and 55 rpm agitation rate. EDTA and Tween 80 at concentration of 1.5 mM and 1.25 %, respectively, were found to be the best for effective removal of impurities, in order to improve hydrophilicity of the fibers. After bioscouring, brightness and whiteness values of bioscoured fibers were increased by 9.72 and 7.10% in comparison with control fibers. After enzymatic scouring, a reduction of 14.45 % in yellowness was also seen in ramie fibers. Enzymatic treatment resulted in 6.97% increased brightness, 10.64% increased whiteness, and 4.11% decreased yellowness as compared with scoured ramie fibers. The results indicated that scouring using xylanase and pectinase enzymes could be a substitute for chemical scouring technique. Enzymatic scouring is, therefore, environmentally sustainable and saves energy, also decreases the consumption of harmful chemicals used in alkaline scouring. This is the first report showing the effect of xylanase and pectinase enzymes, produced by a bacterial isolate, on physico-chemical and various optical properties of ramie fibers.

Potential applications of extracellular enzymes from Streptomyces spp. in various industries

Abstract: Extracellular enzymes produced from Streptomyces have the potential to replace toxic chemicals that are being used in various industries. The endorsement of this replacement has not received a better platform in developing countries. In this review, we have discussed the impact of chemicals and conventional practices on environmental health, and the role of extracellular enzymes to replace these practices. Burning of fossil fuels and agriculture residue is a global issue, but the production of biofuel using extracellular enzymes may be the single key to solve all these issues. We have discussed the replacement of hazardous chemicals with the use of xylanase, cellulase, and pectinase in food industries. In paper industries, delignification was done by the chemical treatment, but xylanase and laccase have the efficient potential to remove the lignin from pulp. In textile industries, the conventional method includes the chemicals which affect the nervous system and other organs. The use of xylanase, cellulase, and pectinase in different processes can give a safe and environment-friendly option to textile industries. Hazardous chemical pesticides can be replaced by the use of chitinase as an insecticide and fungicide in agricultural practices.

Exploration of low-cost agro-industrial waste substrate for cellulase and xylanase production using Aspergillus heteromorphus

Abstract: The current study was executed to explore the nutritive potential of low-cost agro-industrial waste substrates including anaerobically treated distillery spent wash (ADSW) and rice straw (RS) for enzyme production (cellulase and xylanase). The statistical model, Box–Behnken Design (BBD), was utilized to optimize the enzyme production through Aspergillus heteromorphus under liquid state bioconversion on examining the interactive interaction between substrate (ADSW), co-substrate (RS), temperature and initial pH. The BBD results revealed that the optimum levels of different factors for enzymes production were 6% ADSW, 3% RS, pH 5 and temperature 32.5 °C. The highest exoglucanase, xylanase and endoglucanase enzyme activities under optimum conditions were 6.3 IU/mL, 11.6 IU/mL and 8.1 IU/mL, respectively. The results confined that the agro-industrial waste substrate could be a cost-effective and eco-friendly alternative to produce value-added products like enzymes.

Optimization of Cellulase and Xylanase Productions by Streptomyces thermocoprophilus TC13W Using Low Cost Pretreated Oil Palm Empty Fruit Bunch

Abstract: The cellulase and xylanase productions from the pretreated empty fruit bunch as the low-cost substrate in a submerged fermentation were investigated. The objectives of this study were selected the local strain that produced high cellulase and xylanase and enhanced the enzymes production by the selected strain. Ten Streptomyces strains were cultivated in the complex medium [(g/l); CaCl2·2H2O 0.1, MgSO4·7H2O 0.1, KH2PO4 0.5, K2HPO4 1.0, NaCl 0.2, NH4NO3 1.0, yeast extract 5.0 and Tween 80 0.5 with alkaline peroxide pretreated empty fruit bunch (APEFB) 20 in distilled water, pH 7.0] in an incubator shaker at 150 rpm and 45 °C for 120 h. The strain TC13W gave the highest cellulase and xylanase activities (280 and 878 U/g APEFB, respectively). This strain was identified by 16S rDNA method as Streptomyces thermocoprophilus (96% similarity). Cellulase and xylanase productions by S. thermocoprophilus TC13W in the optimized medium with 1% (w/v) APEFB and 0.5% (w/v) yeast extract, pH 6.5 at 150 rpm and 40 °C for 120 h gave the maximum cellulase and xylanase activities of 925 and 1796 U/g APEFB, respectively. The increasing of cellulase and xylanase activities in the optimized medium was 3.30 and 2.04 folds, respectively in comparison to the original medium. These in-house enzymes could be used as the promising candidate enzyme for produce various value-added products via an enzymatic hydrolysis of the lignocellulosic waste.