A Highly Thermostable Xylanase from Stenotrophomonas maltophilia : Purification and Partial Characterization
Open accessAbstract
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.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Some species of Stenotrophomonas are related to lignocellulosic biomass degradation.
“and some species of which were related with lignocellulosic biomass degradation41.”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar
Miller, G. L. (1959) · Analytical Chemistry · doi:10.1021/ac60147a030 · Cited by 28,963 · see citing works
Manual for the identification of medical bacteria.
Cowan, S. T., & Steel, K. (1965) · Cambridge University Press eBooks · Cited by 4,823 · see citing works
Teather, R. M., & Wood, P. J. (1982) · Applied and Environmental Microbiology · doi:10.1128/aem.43.4.777-780.1982 · Cited by 1,851 · see citing works
Microbial xylanases and their industrial applications: a review
Beg, Q. K., Kapoor, M., Mahajan, L., & Hoondal, G. S. (2001) · Applied Microbiology and Biotechnology · doi:10.1007/s002530100704 · Cited by 1,373 · see citing works
Espinosa‐Solares, T., Bombardiere, J., Mark, C., Domaschko, M., Easter, M., David, A. S., Castillo-Angeles, S., & Castellanos-Hernandez, N. (2006) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:132:1:959 · Cited by 1,112 · see citing works
Molecular and biotechnological aspects of xylanases
Kulkarni, N., Shendye, A., & Rao, M. (1999) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1999.tb00407.x · Cited by 904 · see citing works
Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application
Subramaniyan, S., & Prema, P. (2002) · Critical Reviews in Biotechnology · doi:10.1080/07388550290789450 · Cited by 672 · see citing works
Cowan and Steel's manual for the identification of medical bacteria
Cowan, S. T., Feltham, R. K. A., Steel, K., & Barrow, G. I. (1993) · Cambridge University Press eBooks · Cited by 578 · see citing works
Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1
Nakamura, S., Wakabayashi, K., Nakai, R., Aono, R., & Horikoshi, K. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.7.2311-2316.1993 · Cited by 209 · see citing works
Industrial applications and future prospects of microbial xylanases: A review
Dhiman, S. S., Sharma, J., & Battan, B. (2008) · BioResources · doi:10.15376/biores.3.4.1377-1402 · Cited by 179 · see citing works
Juhasz, A. L., Stanley, G. A., & Britz, M. L. (2000) · Letters in Applied Microbiology · doi:10.1046/j.1472-765x.2000.00733.x · Cited by 170 · see citing works
Mamo, G., Hatti‐Kaul, R., & Mattìasson, B. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.03.040 · Cited by 142 · see citing works
Khandeparkar, R., & Bhosle, N. B. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2005.12.008 · Cited by 109 · see citing works
Sanghi, A., Garg, N., Sharma, J., Kuhar, K., Kuhad, R. C., & Gupta, V. K. (2007) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-007-9521-5 · Cited by 106 · see citing works
Growth and Cellulase Formation by Cellvibrio fulvus
Berg, B., Hofsten, B. V., & Pettersson, G. (1972) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1972.tb03691.x · Cited by 99 · see citing works
Bajaj, B. K., & Singh, N. P. (2010) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-010-8960-x · Cited by 95 · see citing works
Alkaline-active xylanase produced by an alkaliphilicBacillus sp isolated from kraft pulp
Yang, V. W., Zhuang, Z., Elegir, G., & Jeffries, T. W. (1995) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/bf01569971 · Cited by 94 · see citing works
MICROBIAL XYLANASES FOR PAPER INDUSTRY
Srinivasan, M. C., & Rele, M. V. (1999) · Cited by 91 · see citing works
Molecular and biotechnological aspects of xylanases
Kulkarni, N. (1999) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(99)00006-6 · Cited by 85 · see citing works
Sharma, A. K., Adhikari, S., & Satyanarayana, T. (2006) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-006-9250-1 · Cited by 83 · see citing works
Production of alkaline xylanase by an alkaliphilic Bacillus sp. isolated from an alkalinesoda lake
Gessesse, A., & Gashe, B. A. (1997) · Journal of Applied Microbiology · doi:10.1046/j.1365-2672.1997.00242.x · Cited by 72 · see citing works
Sepahy, A. A., Ghazi, S., & Sepahy, M. A. (2011) · Enzyme Research · doi:10.4061/2011/593624 · Cited by 71 · see citing works
Enzymatic properties of a neutral endo-1,3(4)-β-xylanase Xyl II from Bacillus subtilis
Sá–Pereira, P., Costa–Ferreira, M., & Aires-Barros, M. R. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(01)00436-9 · Cited by 57 · see citing works
Kumar, K. S., Ayyachamy, M., Permaul, K., & Singh, S. (2009) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2008.12.020 · Cited by 52 · see citing works
Self-citationThermophilic and alkalophilic xylanases from several Dictyoglomus isolates
Mathrani, I. M., & Ahring, B. K. (1992) · Applied Microbiology and Biotechnology · doi:10.1007/bf00169413 · Cited by 46 · see citing works
Kuddus, M., & Pramod, W. R. (2011) · African Journal of Microbiology Research · doi:10.5897/ajmr10.806 · Cited by 42 · see citing works
Bajaj, B. K., Sharma, M., & Sharma, S. (2011) · 3 Biotech · doi:10.1007/s13205-011-0009-5 · Cited by 37 · see citing works
Parachin, N. S., de Siqueira, S. J. L., de Faria, F. P., Torres, F. A. G., & de Moraes, L. M. P. (2009) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2008.12.018 · Cited by 37 · see citing works
Bleach-enhancing abilities of Thermomyces lanuginosus xylanases produced by solid state fermentation
Christopher, L. P., Bissoon, S., Singh, S., Szendefy, J., & Szakács, G. (2005) · Process Biochemistry · doi:10.1016/j.procbio.2005.03.027 · Cited by 24 · see citing works
Self-citationXylanase Production by Bacillus circulans D1 Using Maltose as Carbon Source
Bocchini, D. A., Gomes, E., & da Silva, R. (2007) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-007-8051-9 · Cited by 16 · see citing works
Roy, N., & Kamio, Y. (2002) · PubMed · Cited by 2 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
A detailed overview of xylanases: an emerging biomolecule for current and future prospective
Bhardwaj, N., Kumar, B., & Verma, P. (2019) · Bioresources and Bioprocessing · doi:10.1186/s40643-019-0276-2 · Cited by 442 · see citing works
Bacterial xylanases: biology to biotechnology
Chakdar, H., Kumar, M., Pandiyan, K., Singh, A., Karthikeyan, N., Kashyap, P. L., & Srivastava, A. K. (2016) · 3 Biotech · doi:10.1007/s13205-016-0457-z · Cited by 208 · see citing works
“Inoculum size of 1 % and agitation rate of 120 or 200 proved to be the suitable parameters for maximum production of xylanase under submerged fermentation (Mittal et al. 2012; Raj et al. 2013; Kaur et al. 2016).”
BackgroundInfluentialProduction, characteristics, and biotechnological applications of microbial xylanases
Alokika, & Singh, B. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-10108-6 · Cited by 141 · see citing works
Yadav, P., Maharjan, J., Korpole, S., Prasad, G. S., Sahni, G., Bhattarai, T., & Sreerama, L. (2018) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2018.00065 · Cited by 105 · see citing works
“Effect of pH on Activity and Stability The purified enzyme was incubated with 1% beech wood xylan substrate prepared in buffers solutions with pH ranging from 3 to 11 at 60C for 30min (Raj et al., 2013).”
MethodXu, Z., He, H., Zhang, S., & Kong, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-14052-1 · Cited by 94 · see citing works
Kumar, S., Haq, I., Prakash, J., & Raj, A. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.01.104 · Cited by 91 · see citing works
Self-citationKumar, S., Haq, I., Prakash, J., Singh, S. K., Mishra, S., & Raj, A. (2017) · 3 Biotech · doi:10.1007/s13205-017-0615-y · Cited by 67 · see citing works
“Keywords Bacillus amyloliquefaciens Xylanase Purification Thermostability Kappa number SEM”
BackgroundMethodResultInfluentialSelf-citationCurrent status of xylanase for biofuel production: a review on classification and characterization
Chaudhary, R., Kuthiala, T., Singh, G., Rarotra, S., Kaur, A., Arya, S. K., & Kumar, P. (2021) · Biomass Conversion and Biorefinery · doi:10.1007/s13399-021-01948-2 · Cited by 65 · see citing works
“1 3 like soybean meal, wheat bran, sugar cane bagasse, and rice bran are some acceptable substrates for the production of xylanase [8, 60].”
BackgroundMethodInfluentialBiosynthesis of Polyhydroxyalkanoates (PHAs) by the Valorization of Biomass and Synthetic Waste
Javaid, H., Nawaz, A., Riaz, N., Mukhtar, H., Haq, I. U., Shah, K. A., Khan, H., Naqvi, S. M., Shakoor, S., Rasool, A., et al. (2020) · Molecules · doi:10.3390/molecules25235539 · Cited by 58 · see citing works
“Raj nd hi team [55] also reported pH 7.”
BackgroundAdıgüzel, A. O., & Tunçer, M. (2016) · Food Biotechnology · doi:10.1080/08905436.2016.1199383 · Cited by 50 · see citing works
“%) for 15 min at room temperature, the gel was destained with 1 M NaCl solution for 30 min (Raj et al., 2013).”
MethodRaj, A., Kumar, S., Singh, S. K., & Prakash, J. (2018) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2018.06.018 · Cited by 50 · see citing works
Self-citationAbdella, A., Ramadan, S., Hamouda, R. A., Saddiq, A. A., Alhazmi, N. M., & Al‐Saman, M. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-95965-w · Cited by 43 · see citing works
Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6
Kiribayeva, A., Mukanov, B., Silayev, D., Akishev, Z., Ramankulov, Y. M., & Khassenov, B. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265647 · Cited by 37 · see citing works
Ghosh, A., Sutradhar, S., & Baishya, D. (2019) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-019-2605-1 · Cited by 36 · see citing works
Mu, L., Wang, Q., Cao, X., & Zhang, Z. (2022) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.11482 · Cited by 31 · see citing works
Raj, A. (2016) · Journal of Clinical Microbiology and Biochemical Technology · doi:10.17352/jcmbt.000012 · Cited by 23 · see citing works
Self-citationRecent Advances and Industrial Applications of Microbial Xylanases: A Review
Dhiman, S., & Mukherjee, G. (2018) · Springer eBooks · doi:10.1007/978-981-13-0393-7_19 · Cited by 23 · see citing works
Nawawi, M. H., Ismail, K. I., Sa’ad, N., Mohamad, R., Tahir, P. M., Asa’ari, A. Z. M., & Saad, W. Z. (2022) · Fermentation · doi:10.3390/fermentation8030119 · Cited by 22 · see citing works
Nevita, T., Sharma, G. D., & Pandey, P. (2018) · Environmental Sustainability · doi:10.1007/s42398-018-0017-z · Cited by 20 · see citing works
Singh, S. P., Arya, S. K., & Krishania, M. (2024) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-024-02475-8 · Cited by 13 · see citing works
“The decrease in xylose consumption could be since oxygen is essential for xylose uptake rate by pentose assimilating yeasts, and higher inoculum concentration reduces the oxygen level in the medium [41].”
BackgroundSelf-citationVega, H. R., Arteaga-Garibay, R. I., Maya, O., Gómez-Rodríguez, V. M., Chávez-Díaz, I. F., Ruvalcaba-Gómez, J. M., Heredia-Nava, D., Martínez-Loperena, R., & Zelaya-Molina, L. X. (2020) · Microorganisms · doi:10.3390/microorganisms8101503 · Cited by 12 · see citing works
“Stenotrophomonas exists in the whole fermentation process of corn stover silage in China and could be involved in the degradation of the lignocellulosic biomass [34,75].”
BackgroundAlkaline Active Hemicellulases
Mamo, G. (2019) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2019_101 · Cited by 12 · see citing works
Diversity in Xylan-degrading Prokaryotes and Xylanolytic Enzymes and Their Bioprospects
Verma, D., Kumar, R., V, & Satyanarayana, T. (2019) · Springer eBooks · doi:10.1007/978-981-13-8487-5_14 · Cited by 12 · see citing works
Rakkan, T., Chana, N., & Sangkharak, K. (2022) · Journal of Polymers and the Environment · doi:10.1007/s10924-022-02563-6 · Cited by 11 · see citing works
Sürmeli, Y. (2022) · Biologia · doi:10.1007/s11756-022-01169-6 · Cited by 8 · see citing works
Xylanases: For digestion of hemicellulose
Srivastava, N., Mishra, P. K., & Upadhyay, S. N. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-821010-9.00006-1 · Cited by 8 · see citing works
Salmanizadeh, H., Maal, K. B., Nayeri, H., & Torabi, L. R. (2023) · Brazilian Journal of Microbiology · doi:10.1007/s42770-023-01171-3 · Cited by 6 · see citing works
“…at 4 °C in each stage of centrifugation and in Erlenmeyer containing 1 L of 0.05 M potassium phosphate buffer and pH 7 shaker 90 rpm. Minutes and temperature of 4 °C overnight were recorded, then enzyme activity and protein content were measured and calculated in terms of light absorption [36, 42].”
InfluentialTamariz-Angeles, C., Lázaro-Palomino, J., Olivera-Gonzales, P., Castañeda-Barreto, A., & Villena, G. K. (2020) · Revista Peruana de Biología · doi:10.15381/rpb.v27i1.17582 · Cited by 6 · see citing works
Chapter 5 Thermostable Enzymes and Their Industrial Applications
Kumar, S., Arumugam, N., Permaul, K., & Singh, S. (2016) · CRC Press eBooks · doi:10.1201/9781315367880-6 · Cited by 6 · see citing works
Self-citationTiwari, P., Ansari, W. A., Kumar, S. C., Tiwari, P. K., Kumar, M., Chakdar, H., Srivastava, A. K., Saxena, A. K., & Shantikumar, L. (2024) · Current Microbiology · doi:10.1007/s00284-024-03927-y · Cited by 6 · see citing works
Self-citationSources, production, and classification of xylanases
Bajpai, P. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99636-5.00003-8 · Cited by 4 · see citing works
Screening of Culture Conditions for Production of Xylanase from Landfill Soil Bacteria
Rosli, S. N. A., Man, R. C., & Masngut, N. (2019) · Indonesian Journal of Chemistry · doi:10.22146/ijc.39709 · Cited by 3 · see citing works
“Previously, xylanase was produced either by using commercial substrates such as xylan [13], birchwood xylan [14-15], and glucose [7] or by utilizing cheaper substrates such as rice straw [16], rice bran [17], wheat bran [5,17-20], wheat straw [21], orange peel, banana peel, mango peel, apple pulp, oil cake [7], grass…”
BackgroundInfluentialDegradation of cellulosic material by Cellulomonas fimi
Kane, S. D. (2015) · ERA · Cited by 2 · see citing works
Hemeda, A. A., Zahran, S. A., Ali‐Tammam, M., Ewida, M. A., Kashef, M. T., Yassin, A. S., Mitra, A., Youssef, N. H., & Elshahed, M. S. (2024) · Journal of Industrial Microbiology & Biotechnology · doi:10.1093/jimb/kuaf006 · Cited by 1 · see citing works
PRODUCTION OF SOFT CHEESE FROM ASPERGILLUS TAMARII ENZYME AND SENSORY PERCEPTION
Sambo, S., & SAMBO, Z. G. (2023) · Greener Trends in Food Science and Nutrition · doi:10.15580/gtfsn.2023.1.122822111 · Cited by 1 · see citing works
OMIC Technologies in Bioethanol Production: An Indian Context
Srivastava, P. A., & Yennamalli, R. M. (2019) · doi:10.1002/9781119509967.ch11
Xylanolytic Psychotrophs From Andosolic Sedge Fens and Moss Heaths in Iceland
Rickman, O. J., Sigurbjörnsdóttir, M. A., & Vilhelmsson, O. Þ. (2018) · Fine Focus · doi:10.33043/ff.4.2.171-186
Sambo, S., Adamu, S., & Haruna, I. (2024) · Greener Trends in Food Science and Nutrition · doi:10.15580/gtfsn.2024.1.111124166
Aladekoyi, G., Ajala, O. A., Shakpo, I. O., & Adesina, T. A. (2024) · Greener Trends in Food Science and Nutrition · doi:10.15580/gtfsn.2024.1.062424088
Kalaiselvi, P., Porkavi, B. M., Sebastian, S. P., Saravanan, V. S., Davamani, V., Parameswari, E., Poornima, R., & Ilakiya, T. (2025) · Waste and Biomass Valorization · doi:10.1007/s12649-025-03320-1
“Consistent with these findings [ 74], reported maximum xylanase yunnanense (PKKF1), and Penicillium citrinum (PKKF2).”
Singh, S. P., Arya, S. K., & Krishania, M. (2024) · Figshare · doi:10.6084/m9.figshare.26685318
Self-citationSingh, S., Arya, S. K., & Krishania, M. (2024) · Figshare · doi:10.6084/m9.figshare.26685315
Self-citationRecent advances in microbial enzyme systems for paddy straw bioconversion and composting
Keerthana, R. S., Parab, C., Prajapati, V., Bhimani, H., Jajda, H. M., & Khunt, M. D. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00541-w
- Authors
- Raj, A., Kumar, S., & Singh, S. K.
- Affiliations
- Council of Scientific and Industrial Research (IN)
- Central Drug Research Institute (IN)
- Corresponding author
- Raj, Abhay
- Venue
- Enzyme Research
- Publisher
- Wiley
- Published
- 2013-12-14
- Volume
- 2013
- Pages
- 1-8
- ISSN
- 2090-0406 (ISSN-L)
- 2090-0414
- PMC
- PMC3876469
- OpenAlex
- W2114414167
- Cited by
- 44
- References
- 32
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 7 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 4 · 2019: 7 · 2018: 5 · 2017: 3 · 2016: 4 · 2015: 1 · 2014: 1
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Enzyme Research (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Department of Biotechnology , Ministry of Science and Technology (BT/PR6343/GBD/27/404/2012)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
- Keywords
- xylanase, Stenotrophomonas maltophilia, thermostable enzymes, alkaline stability, xylanolytic bacteria, wheat bran, agro-industrial waste, enzyme purification, industrial enzymes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
