Xylanase-Producing Microbes and Their Real-World Application

Phuyal, Milan; Budhathoki, Uttam; Bista, Durga; Shakya, Shailendra; Shrestha, Rajan; Shrestha, Ashwinee Kumar

doi:https://doi.org/10.1155/2023/3593035

International Journal of Chemical Engineering

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Abstract Introduction Methods Conclusion Conflicts of Interest Acknowledgments References Copyright Related Articles

Review Article | Open Access

Volume 2023 | Article ID 3593035 | https://doi.org/10.1155/2023/3593035

Xylanase-Producing Microbes and Their Real-World Application

Milan Phuyal,¹Uttam Budhathoki,¹Durga Bista,¹Shailendra Shakya,¹Rajan Shrestha,¹and Ashwinee Kumar Shrestha¹

Academic Editor: Fernanda Casciatori

Received01 Nov 2022

Revised04 Jun 2023

Accepted13 Oct 2023

Published01 Nov 2023

Abstract

The present study is focused on the availability of microbial sources capable of producing xylanase, a hemicelluloses-degrading enzyme with multiple modes of action along with specificity, and their real-world applications. For the accumulation of suitable data, article surfing was carried out using multiple search engines viz. Hinari and PubMed; irrelevant and duplicate articles were discarded and articles were summarized in a narrative way herein. This review article was written aiming to bridge the recent research activities with the commercial activities of xylanase going on around the globe. The readers would be able to acknowledge themselves with the basic idea of the hydrolytic enzyme xylanase, their classification representing their different families, presenting the affinity of different families at the structural level, the sources, and the commercial implications that have been going on alone and in combination. The major hemicellulose, Xylan is digested with the help of combination other enzymes such as alpha-amylase, subtilisin, protease, and endo-1,3(4)-β-glucanase along with xylanase. Xylanase has a diverse applications such as pharmaceutical, food and feed, bakery, paper and pulp, textile, and bio-refinery industries. The objective of this review article is to compile microbial sources of this enzyme and its application for betterment of human kind.

1. Introduction

Xylan is one of the most plentiful polysaccharides on Earth [1]. Xylan is the major hemicellulosic constituent found in soft and hard wood and is the next most abundant renewable polysaccharide after cellulose. Xylanases are hydrolytic enzymes that catalyze the cleavage of the β-1,4 backbone of xylan [2] randomly which results in the production of diverse products which include xylobiose, xylotriose, xylotetraose, and longer and/or branched xylo-oligomers (XOS) [3, 4].

Scientifically, xylanase is known as endo-1,4-β-xylanase (EC 3.2.1.8). Xylanases (endo-1,4-β-xylanases; EC 3.2.1.8) catalyze the hydrolysis of β-1,4-xylosidic bonds of xylan, constituting a class of enzymes that are critical for the degradation of hemicellulosic polysaccharides in biomass [5]. Due to the complex nature and diversity of xylan, enzymatic degradation must be carried out by multiple hydrolytic enzymes with multiple modes of action and specificities [6]. Xylanase is preferred due to its involvement in cleaving glycosidic bonds and endo-xylanase [7].

Bacteria, fungi, actinomycetes, and yeasts which include cellulomonas, bacillus, micrococcus, aspergillus, penicillium, streptomyces, chytridiomycetes, trichoderma, and ruminococcus have also been reported for xylanase production [6–8].

Abundant use of bacteria for enzyme production is because they are capable of growing rapidly, are capable of genetic modification easily, and have ease of growth and regulation of production [9], though fungi are considered as the most potent xylanase producers [6]. Industrial processes are carried out at a higher temperature and extreme pH which is a supporting fact for the suitability of thermostable xylanases obtained from the thermophilic microorganisms and those obtained from their mesophilic counterparts [10]. This is the main reason for the increasing demand for the isolation and screening of thermophilic microorganisms for the production of novel thermostable xylanases for industrial applications, and it is preferred to adapt genomic strategies and various molecular approaches conducted via bioinformatics tool. Hence, produced xylanase has been reported to have stable, higher enzyme activity [6].

The xylan processing arena makes the use of xylanase as it is eco-friendly and can reduce the processing cost. The enzymatic action of xylanase in the paper industry can improve the efficiency of bleaching agents (hydrogen peroxide, ozone, and chlorine) in a bakery; it can aid in the improvement of the bread texture; and in the juice and wine industry, it can aid in the clarification steps and hence improve the quality. Along with these applications, xylanase has been reported in animal feed additive formulations as well. Besides all these beneficial applications, few limitations hindering its commercialization are present. The complex and diverse nature of xylan, the cost of the enzyme along with thermal instability, and the pH-dependent nature of xylanase are limiting factors hindering further commercialization [11]. With the aid of various engineering procedures, limiting factors hindering commercialization are diminished, increasing its demand in the diverse industrial arena that includes the paper and pulp industry, pharmaceuticals, and food and feed. [10].

The synergistic action of xylanase has been observed when used in combination with pectinase, cellulase, phytase, glucanases, glucose oxidase, α-amylase, and malting amylase. A combination of xylanase along with pectinases and cellulases has been reported for yield increment when used for clarification and extraction of vegetable and fruit juices. The similar, combinational benefits of xylanase, when used in combination with cellulase and phytase, have been reported for showing improvements in the performance and feed value of animals. A combination of xylanases and glucanases improves the absorption and digestion of feed materials like barley-based feed and high-fiber rye for poultry and pig. Xylanase along with glucose oxidase, α-amylase, and malting amylase breaks down hemicelluloses in wheat flour, leavening the dough, increasing bread volume, making the bread softer, etc., aids in the bakery industry [7].

This review focuses on the real-world application of xylanase along with xylanase-producing microbes. The main aim of this review is to incorporate almost all the xylanase sources along with their significance into a single sheet.

2. Methods

Article screening was carried out using different search engines viz. Hinari and PubMed. A six-year time frame was used for the accumulation of suitable articles. {(Xylanase) and (Microorganism)}, {(Xylanase producing microbes) and (enzyme activity)}, (Xylanolytic microbes), {(Xylanolytic microorganism) and (xylanase)}, are different keywords that have been used for article accumulation. While using keywords: ((xylanase) and (microorganism)), one hundred and eighty-eight search results had been shown in PubMed and five hundred and sixty-four search results had been shown in Hinari. Similarly, while using keywords: {(Xylanase producing microbe) and (enzyme activity)}, thirteen results had been shown in Hinari, and six results had been shown in PubMed; while using keywords: (xylanolytic microbes), twenty results had been shown in Hinari and thirteen results had been shown in PubMed; while using keywords: {(xylanolytic microorganism) and (xylanase)}, forty-three search results appeared in the Hinari search engine and twenty-one results in PubMed. Out of eight hundred and sixty-eight search results, one hundred and twenty-seven articles were selected for writing this review article.

The screening was carried out; duplicate articles along with irrelevant articles were discarded, and the available relevant contents were incorporated into this review paper. Microbial sources and real-world application of the xylanase were collected from screened primary, secondary, and tertiary sources data, i.e., original work data, review work data, e-books, etc. Articles containing the sources and application of xylanase were selected, collected, analyzed, and summarized in this review. Relevant data were summarized in a narrative way herein.

2.1. Classification of Xylanase

Within this classification system, xylanases are normally reported as being confined to families 10 (formerly) and 11 (formerly G). However, it is revealed that enzymes with xylanase activity are also found in families 5, 7, 8, 16, 26, 43, 52, and 62 [4].

Higher molecular weight and peptide-linked catalytic domain with a cellulose-binding domain falls under Family 10 while the enzyme with a lower molecular weight falls under Family 11. Based upon iso-electric points, Family 11 enzymes are subdivided into the alkaline and acidic groups. enzyme structure, mode of action, physiochemical properties, and substrate specificity are some of the differential factors in other families 5, 7, 8, and 43 [12]. Glyoside hydrolase (GH) families 5, 7, 8, 10, 11, 16, 43, 51, 52, and 62 have been reported to contain xylanase [4, 13].

Maximum activity of endo-xylanase has been observed in the pH range (4.0–6.5) at a temperature range (40–80)°C. The isoelectric point (pI) value of endo-xylanase produced from bacteria and fungi falls in the range of (4.0–10.3), with a molecular weight of a single subunit protein in the range (8.5–85) kDa [7].

For the hydrolysis of an unsubstituted region of arabinoxylan, the GH 11 xylanase family is suitable while GH 10 xylanase family is suitable for side-chain arabinose residuexylose linkage. The GH8 xylanase family is unique from other xylanase families as it acts only on xylan while GH5, GH7, and GH43 xylanase act on endo-glucanases, arabinofuranosidase, or licheninases. The enzymatic action of a novel endo-xylanase of the GH30 family has been reported for its specificity towards glucoronoxylan [14].

34 arabinoxylanase, a subfamily of 5 glycoside hydrolase, requires some furnishing for catalytical specificity for xylans (arabino-substituted) to generate reducing end-branched xylooligosaccharide. Enzyme catalysis of GH8 xylanase families is different from that of other GH families, as GH8 catalyzes via a net inversion mechanism while other GH family catalyzes via a retaining mechanism. Short xylooligosaccharide along with soluble and branched xylans are suitable for higher GH10 xylanase activity while insoluble xylan and unsubstituted regions of xylan are suitable for higher GH11 xylanase activity. The enzyme activity of GH 11 xylanase is lower in the case of furnished xylan. The methyl-glucuronic acid substation is mandatory for the enzyme activity of 8 xylanase, a subfamily of GH30 xylanase (glucoronoxylanase) [3].

2.2. Xylanase Sources

The availability of xylanase in both prokaryotes and eukaryotes has been reported. Documented evidence for xylanase production includes marine and terrestrial bacteria, rumen bacteria, protozoa, fungi, marine algae, snails, crustaceans, insects, and the seeds of terrestrial plants and germinating seeds. Information on xylanase production from plants and endo-xylanase from Japanese pear fruits during the over-maturing period has been reported. Along with this, higher animals such as Mollusca have been reported for xylanase production [2]. Ease of availability, higher volumetric productivity, structural stability, and ease of genetic manipulation are the reasons behind the preference for microbial sources over plants and animals [11].

Micrococcus, bacillus, paenibacillus, staphylococcus, cellulomonas, microbacterium, arthrobacter, rhodothermus, and pseudoxanthomonas are bacterial genuses that have been reported for xylanase production. Nonomuraea, Streptomyces, and Actinomadura are some actinomycetes reported for xylanase production. Malbranchea sp. Thermoascus auranticus, Chaetomium thermophilum, Humicola insolens, and Melanocarpus sp. are fungi genera that have been reported for the production of alkaline stable xylanase. The industrial processes operated at higher pH are the reason behind the benefit of bacterial xylanase over fungal xylanase, as bacterial xylanases have pH optimums in the neutral or alkaline range, while production of fungal xylanase requires additional steps due to the optimum pH in the acidic range [7].

Thermostable xylanase has been reported for production by various thermophilic bacteria belonging to genus Geobacillus, Bacillus, Thermotoga, Thermoaner obacterium, Anoxybacillus, and Acidothermus [15].

2.2.1. Bacterial Source

Bacillus species is the most potent xylanase producer among bacterial species which includes Bacillus sp., B. halodurans, B. pumilus, B. subtilis, B. amyloliquefaciens, B. circulans, and B. stearothermophilus (Table 1) [8].

2.2.2. Marine Source

Halocynthia aurantium and Deroceras reticulatumare marine invertebrates xylanase sources have been reported. Bacillus tequilensis, Achromobacter xylanoxidans, Bacillus subtilis cho40, and Bacillus subtillus SR60 are marine bacterial sources of xylanase. Streptomyces olivaceus (MSU3), Streptomyces albidoflavus SAMRC-UFH5, and Verrucosispora sp. K2-04 are marine actinomycetes sources of xylanase.Aspergillus cf. tubingensis LAMAI 31, Bartalinia robillardoides LF550, Calcarisporium sp. KF525; Penicillium pinophilum LF458, Pestalotiopsis sp. KF079, Scopulariopsis brevicaulis LF580, and Tritirachium sp. LF562 are marine xylanase-producing fungi [11].

2.2.3. Protozoa Source

Entodinium sp., Diploplastron affine, Eudiplodinium maggii, Polyplastron multivesiculatum, Dasytricha ruminatium, and Epidinium caudatum, rumen protozoans, have been reported for their xylanase activity [76].

2.2.4. Archer Source

Pyrodictium abyssi, Pyrococcus furious, Sulfolobus solfataricus, Thermococcus zilligii, and Thermofilum strains of hyperthermophilic archaeal microbes have been reported to produce thermostable xylanase [6]. Highly thermostable xylanase production via Sulfolobus solfataricus has been studied [44].

2.2.5. Fungal Source

Filamentous fungi, particularly Aspergillus and Trichoderma are well known for the effective production of xylanolytic enzymes [96]. Xylanase-producing fungal sources are summarized in Table 2.

2.3. Real-World Application of Xylanase

Multifaceted applications of xylanase have driven research activities around the globe over the past few years. The real-world application arena of xylanase includes biofuel production, pulp and paper industry, baking and brewing industry, food and feed industry, and deinking of waste paper [7]. Xylanase has been reported to be used in various industries in a combined form with other enzymes which include cellulase, agarose, pectinase, amylase, phytase, hydrogenase, sucrase, β-glycosidase, polygalacturonase, FPase, CMCase, α-amylase, cellobiohydrolase, and Lytic polysaccharide monooxygenase, for synergistic activity [17].

The real-world applications of xylanase in the different arenas are discussed below.

2.3.1. Pharmaceutical Industry

Xylanase, being a hydrolytic enzyme, catalyze the hydrolysis of xylan and leads to the formation of hydrolytic products, xylooligosaccharides (XOS) [124]. Xylose is a monomer unit of XOS. Application of XOS in the biotechnology, pharmaceutical, food, and feed industries has been reported. Gastrointestinal tract absorption and hydrolysis are absent and have been reported to play a vital role as prebiotics. Selectively stimulate gastrointestinal microorganism growth, indicating the regulation of human digestive health [8]. Bifidobacteria, a healthy human gut bacteria growth promotion by the use of enzymes has been reported. Ferulic acid along with hydroxycinnamic acids, by-products of xylanolytic enzymes which are the hydrolytic products of xylan hydrolyzed by feruloyl esterase have been reported to show antimicrobial, anti-inflammatory, anti-diabetic, antithrombosis, anticancer, and cholesterol lowering agents [68].

Antiallergic activity, cytotoxic, laxative, and carbon source-promoting growth of probiotics are pharmaceutical applications of XOS that have been reported. By producing inhibitory compound action against IgE antibodies, antiallergic activity was shown. Leukemia cells obtained from lymphoblastic leukemia, the cytotoxic activity of XOS has been reported during in vitro evaluation. It has been reported that severe constipation reduction with no side effects was seen in pregnant women after the consumption of XOS. Adjunct oral administration of XOS and rice husk has been reported to maintain gut microbiota, eventually regulating blood glucose, insulin resistance, and dyslipidemia. The pharmaceutical industry can use XOS for the preparation of hydrogels and coating materials for tablets [14].

2.3.2. Food Industry

Enzyme food technology is superior to conventional chemical food technology. The reduction in energy consumption, waste, by-products, along with environmental impacts are reasonable reasons to promote enzymatically processed food over conventional chemically processed food [68].

Most of the work carried out inside the bakery involves the use of arabinoxylans, the principle raw material of the baking industry. Wheat is essential for bread manufacturing and contains arabinoxylans in higher concentration [12]. The hydrolytic property of xylanase are capable of solubilizing unextractable arabinoxylan in water, which aids in the improvement of rheological properties, i.e., softness, extensibility, and elasticity by uniform water distribution and gluten network formation in the dough [8]. It also strengthens the dough and makes it capable of tolerating changes in process parameters and flour quality. Improvements in biscuit texture and taste have been reported after the addition of xylanase. Xylose is used for xylitol production and is a hydrolytic product of xylan hydrolyzed by xylanase. Xylitol can be used in food as a natural sweetener. Thus, it is beneficial for diabetic patients as a sugar replacement. Along with these applications, dental caries reduction properties have been reported as well [68].

Baking activities are carried out usually at a low to moderate temperature scales usually below 35°C. So, xylanase showing higher enzyme activity in this range is preferable for the baking industries. Microorganisms capable of facing unharmonious process parameters are suitable for the industrial preparation of xylanase. Aspergillis sp., Trichodermasp., and Bacillus sp. have been reported to be used abundantly as sources of xylanase in the baking industry [125].

The use of xylanase is well known for improving the bread quality by increasing the bread volume, the use of recombinant xylanase from Phoma sp. MF 13 tested in Chinese steamed bread has shown a specific volume increment of 4.45%, chewiness of 25.2%, and hardness of 25.7%, concerning the controlled Chinese steamed bread sample [11].

2.3.3. Animal Feed

Monogastric animals, i.e., poultry, pigs, humans, etc., lack endogenous digestive enzymes for the digestion of cellulose and hemicellulose. To enrich the nutritional value of animal feed, exogenous enzymes such as xylanase, cellulase, phytase, ligase, etc., have been used [68]. Cereals, triticale, and soy-based diets have been reported as the most commonly used animal feeds [6]. Xylanase added to the feed can hydrolyze water-insoluble arabinoxylan, reducing the viscosity of the feed. Hence, it enhances the digestibility of the feed and aids in nutritional value [68].

Acidothermus cellulolyticus-produced endo-xylanase aids in the improvement of the nutritional value of poultry feed[12].

Avizyme® 1505 (endo-1,4-beta-xylanase, subtilisin, and alpha-amylase) [41], Beltherm MP/ML [42], Axtra® XAP 104 TPT(endo-1,4-beta-xylanase, protease, and alpha-amylase) [98], ECONASE® XT [100], HOSTAZYM® X [99], RONOZYME ® WX [100], RONOZYME® WX CT/L [126], Endofeed® DC(endo-1,3(4)-β-glucanase and endo-1,4-β-xylanase) [127], Natugrain® TS/TS L (endo-1,4-beta-xylanase and endo-1,4-beta-glucanase) [40] are some of the commercially produced feed enzymes.

2.3.4. Juice and Brewing Industry

The use of xylanase aid in the removal of polysaccharides such as cellulose, hemicellulose, starch, pectin, and surface-bound lignin by decreasing the viscosity and improving the quality of juice [128]. Clusters, along with undissolved solids and suspended materials can be removed via a purification process which includes centrifugation and filtration methods that aid in the improvement in clarity, aroma, and color of the resulting juice. An increase in the amount of reducing sugar along with decreased turbidity of juice produced from kiwi, apple, peach, orange, apricot, grapes, and pomegranate using xylanase produced from P. acidilactici GC25 have been reported. Streptomyce sp. AOA40-produced xylanase was partially purified and used for the clarification of apple juice. Streptomyces sp.-produced xylanase used for clarification of orange, mousambi, and pineapple, resulting in an improvement in clarity by 20.9%, 23.6%, and 27.9%, respectively [8].

Xylanase is used in combination with pectinase, amylase, and cellulase in the brewing and fruit juice industry. In the brewing industry mashing of barley, wheat, rye, sorghum, corn, and rice are mashed during the brewing process to make malt which is needed for releasing the malting enzyme required for fermenting starch into alcohol. The cell wall of cereals used in the brewing process contains nonstarchy polysaccharides along with pectins, increasing the energy expenditure along with less smooth malt production. To overcome this macerating enzymes, i.e., xylanase along with cellulase and pectinase is used. The use of these macerating enzymes results in the release of hydrolysable ingredients, i.e., sugar, minerals, pigments, phenolic compounds, other nutrients, and aroma. Other beneficial outcome includes an increment in yield, stability, and a decrease in the viscosity and haze of juice and wine [17].

Novozyme 188, Celluclast 1.5L, Sihazyme extro, Trenolin, Lallzyme Ex-V, Crystalzyme Tinto, Rohapect VR-C, Vinozyme G, Extrazyme, Extrazyme fruit, Extrazyme Blanc, Enzeco® cellulase CE-2, CEP, Enzeco® xylanase S, and Enzeco® hemicellulase are well known commercial enzyme products that have been reported to be used in juice and wine industry [17].

2.3.5. Pulp and Paper Industry

Xylanase enzyme aids in the bio-bleaching, bio-deinking, and bio-pulping processes of the pulp and paper industry. Cellulose and Lignin-linked xylan of pulp fiber upon enzymatical hydrolysis by pH and temperature-dependent xylanase aid in the brightening of pulp, an increase in bonding force, and the strength of paper. The production of flexible solar cells from xylanase bio-bleached pulp is capable of having a higher storage capacity [8].

Bacillus stearothermophillus and Bacillus pumilus produce alkali-tolerant xylanase capable of showing enzymatic action at higher temperatures and pHs and are suitable for use in the paper and pulp industry [12].

Printed paper is reused after recycling by removing the ink. Though reusing by recycling is a convenient method for pollution reduction along with need fulfillment, the use of chemicals such as chlorine or chlorine-based derivatives, ClO⁻, NaOH, NaCO₃, H₂O₂, and Na₂SiO₂ increases the processing cost, energy, and is baleful for the environment. The use of enzymes during recycling aids to overcome it. Bacterial alkalophilic xylanase along with laccase results in an increment of the brightness of old newsprint pulp by 21.6%, inject print pulp by 4.1%, laser print pulp by 3.1%, magazine pulp by 8.3%, and Xerox paper pup by 1.9%. Reports regarding the improvement of the physical properties of old newspaper freeness by 17.8%, breaking length by 34.8%, burst factor by 2.77%, and tear factor by 2.4% have been reported [8].

The reduction of chlorine dioxide by 10% and chlorine by 20% during bio-bleaching of eucalyptus kraft pulp using xylanase produced from Bacillus pumilus have been reported [12].

2.3.6. Biorefinery Industry

Biofuel generation from lignocellulose biomass composed of cellulose (40–50) %, hemicellulose (xylan and others) (25–35) %, and lignin (15–20) % is carried out in three steps. Delignification, saccharification, and fermentation in the presence of yeast result in the production of bioethanol [17]. Xylanase assists in the pretreatment of agro-residue and saccharification of carbohydrate polymers to increase the sugar yield, eventually resulting in an increment in bioethanol yield [6].

Cellulomonas flavigena-produced xylanase Cfl Xyn11A was used for pretreatment of lignocellulose biomass resulting in an improvement in the yield of fermentable sugar required for bioethanol production. Lignocellulose biomass pretreatment done by enzyme cocktails (Xylanase, laccase, and cellulase) has been reported as a novel way for bioethanol production [7]. Coculture of Geobacillus sp. strain DUSELR 13 with Geobacillus thermoglucosidasius to produce ethanol by the enzymatic hydrolysis of lignocellulose biomass has been reported [15].

2.3.7. Textile Industry

Desizing, sourcing, and bleaching are the different processes involved in the textile industry. Alkali thermostable xylanase are used during the desizing and sourcing process. Desizing involves the adhering sizing material, sourcing involves whitening and absorbency improvement and bleaching involves imparting fixed standard whiteness to the fabric. The significance of enzymatic activity during processing is due to its specific action capable of removing hemicellulose impurity without loss in strength of the fiber. Snag regarding the commercialization of the enzymatic method is due to the hydrolysis of seed coat present within the fiber that may lead to the unwanted exposure to chemicals during the later stages i.e. bleaching and finishing [8].

Xylanase from Bacillus pumilus was used for enzymatic desizing of cotton and monopoly fabric.

Report demonstrating the bio-sourcing of jute fabric using xylanase produced from Bacillus pumilus ASH have been reported. Xylanase used along with surfactant like tween 80, EDTA shows significant improvement in fabric whiteness by 1.2%, brightness by 3.2%, and decrease in yellowness by 4.2%. T. longibrachiatum KT 693225-produced xylanase has been reported to show significant improvement in desizing, bio-sourcing, and bio-finishing without the addition of surfactant [8].

2.4. Commercial Xylanases

Commercially available xylanase brands are summarized in Table 3. Brand list of commercially produced xylanase in combination with other enzymes is listed in Table 4.

3. Conclusion

In this review paper, xylanase-producing sources along with the real-world application and some commercial products were presented which reflect the significance of this enzyme. To narrow down the subject matter for this review, optimized process parameters, an optimized substrate for higher enzyme production, and a detailed overview of the enzyme structure were not incorporated herein. Since much research work has been carried out due to their significance, this review could aid researchers around the globe by acknowledging researchers with multiple sources of xylanase along with its real-world application in a single sheet.

Conflicts of Interest

The authors declare that there are no conflicts of interest regarding the publication of this paper.

Acknowledgments

This research was supported by Kathmandu University-Integrated Rural Development Program/Nepal Technology Innovation Center (KU-IRDP/NTIC) grant funded by the Korean International Cooperation Agency (KOICA).

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Copyright © 2023 Milan Phuyal et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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