Abstract
An endo-1,4-β-xylanase, XynA, from Thermomyces lanuginosus VAPS-24, was purified to homogeneity and exhibited a molecular mass of approximately 20 kDa. The protein sequence of XynA was found to be similar to those of other Thermomyces lanuginosus derived xylanases and, as a result, could be used as a model enzyme for understanding the protein structure–activity relationship and facilitating protein engineering to design enzyme variants with desirable properties. Therefore, this xylanase will be an attractive candidate for applications in the biofuel and fine chemical industries for the degradation of xylans in steam pre-treated biomass.
References
de Oliveira Gorgulho Silva C, Filho EXF (2017) A review of holocellulase production using pretreated lignocellulosic substrates. BioEnergy Res 10:592–602. https://doi.org/10.1007/s12155-017-9815-x
Patel SK, Gupta RK, Kumar V, Mardina P, Lestari R, Kalia VC, Choi MS, Lee JK (2019) Influence of metal ions on the immobilization of β-glucosidase through protein-inorganic hybrids. Indian J Microbiol 59:370–374. https://doi.org/10.1007/s12088-019-00796-z
Singh S, Madlala AM, Prior BA (2003) Thermomyces lanuginosus: properties of strains and their hemicellulases. FEMS Microbiol Rev 27:3–16. https://doi.org/10.1016/S0168-6445(03)00018-4
Meng DD, Ying Y, Chen XH, Lu M, Ning K, Wang LS, Li FL (2015) Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency. Appl Environ Microbiol 81:2006–2014. https://doi.org/10.1128/AEM.03677-14
Khucharoenphaisan K, Tokuyama S, Kitpreechavanich V (2010) Purification and characterization of a high-thermostable β-xylanase from newly isolated Thermomyces lanuginosus THKU-49. Mycoscience 51:405–410. https://doi.org/10.1007/S10267-010-0054-7
Singh KR, Lee JK, Selvaraj C, Singh R, Li J, Kim SY, Kalia VC (2018) Protein engineering approaches in the post-genomic era. Curr Protein Pep Sci 19:5–15. https://doi.org/10.2174/1389203718666161117114243
Kumar V, Chhabra D, Shukla P (2017) Xylanase production from Thermomyces lanuginosus VAPS-24 using low cost agro-industrial residues via hybrid optimization tools and its potential use for saccharification. Bioresour Technol 243:1009–1019. https://doi.org/10.1016/j.biortech.2017.07.094
Laemmli UK (1970) Cleavage of structura l proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. https://doi.org/10.1038/227680a0
Shevchenko A, Tomas H, Havli J, Olsen JV, Mann M (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1:2856–2860. https://doi.org/10.1038/nprot.2006.468
Zhang J, **n L, Shan B, Chen W, **e M, Yuen D, Zhang W, Zhang Z, Lajoie GA, Ma B (2012) PEAKS DB: de novo sequencing assisted database search for sensitive and accurate peptide identification. Mol Cell Proteomics 11:M111.010587. https://doi.org/10.1074/mcp.M111.010587
Vafiadi C, Christakopoulos P, Topakas E (2010) Purification, characterization and mass spectrometric identification of two thermophilic xylanases from Sporotrichum thermophile. Process Biochem 45:419–424. https://doi.org/10.1016/j.procbio.2009.10.009
Wakarchuk WW, Campbell RL, Sung WL, Davoodi J, Yaguchi M (1994) Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase. Protein Sci 3:467–475. https://doi.org/10.1002/pro.5560030312
Shrivastava S, Shukla P, Deepalakshmi PD, Mukhopadhyay K (2013) Characterization, cloning and functional expression of novel xylanase from Thermomyces lanuginosus SS-8 isolated from self-heating plant wreckage material. World J Microbiol Biotechnol 29:2407–2415. https://doi.org/10.1007/s11274-013-1409-y
Silva CDOG, Aquino EN, Ricart CAO, Midorikawa GEO, Miller RNG (2015) GH11 xylanase from Emericella nidulans with low sensitivity to inhibition by ethanol and lignocellulose-derived phenolic compounds. FEMS Microbiol Lett 362:1–8. https://doi.org/10.1093/femsle/fnv094
Acknowledgements
We would like to thank Dr. Stoyan Stoychev (CSIR, South Africa) for identifying the xylanase used in this study using tryptic map**/MS. The authors are also grateful for the financial support received for this study from the National Research Foundation (NRF) of South Africa and Rhodes University (Sandisa Imbewu). Any opinion, findings and conclusions or recommendations expressed in this material are those of the author(s), and therefore the NRF does not accept liability in regard thereto. VK is thankful to UGC New Delhi, India, for awarding him the Junior Research Fellowship [F.17-63/2008 (SA-I)]. PS acknowledges the support from the Department of Biotechnology, Government of India (Grant No. BT/PR27437/BCE/8/1433/2018), SERB, Department of Science and Technology, Government of India (DST Fast Track Grant No. SR/FT/LS-31/2012) and the infrastructural support from Department of Science and Technology, Government of India through a FIST Grant (Grant No. 1196 SR/FST/LS-I/2017/4).
Author information
Authors and Affiliations
Corresponding authors
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Mathibe, B.N., Malgas, S., Radosavljevic, L. et al. Tryptic Map** Based Structural Insights of Endo-1, 4-β-Xylanase from Thermomyces lanuginosus VAPS-24. Indian J Microbiol 60, 392–395 (2020). https://doi.org/10.1007/s12088-020-00879-2
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12088-020-00879-2