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Chemical modification of xylanase from Chainia sp. (NCL 82.5.1)

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Summary

The high molecular weight xylanase from Chainia (NCL 82. 5. 1) is extracellular, cellulase-free and stable at alkaline pH (pH 8.0) at 50°C. The enzyme showed inhibition by N-bromosuccinimide(NBS) and by cysteine-specific reagents p-hydroxy mercuric-benzoate(PHMB) and N-ethyl maleimide(NEM) implying that tryptophan and cysteine are present at or near the active site of the enzyme. The enzyme was reversibly inhibited by low concentrations (0.5 M) of guanidine hydrochloride (Gdn.HCl) indicative of the presence of a carboxylate group in the active site of the enzyme. Kinetics of inactivation of enzyme by Gdn.HCl revealed that the essential carboxylate residues are present at the substrate-binding region of the enzyme.

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References

  • Bastawde, K.B., Tabatabai, L.B., Meagher, M.M., Srinivasan, M.C., Vartak, H.G., Rele, M.V. and Reilly, P.J. (1991) ACS Symp. Ser.460, 417–425.

    Google Scholar 

  • Chauthaiwale, J.V. and Rao, M. (1993) Biochem. Biophys. Res. Commun.191, 922–927.

    Google Scholar 

  • Chauthaiwale, V.M. and Deshpande, V. (1992) FEMS Microbiol. Lett.99, 265–270.

    Google Scholar 

  • Deshpande, V.V., Hinge, J. amd Rao, M. (1990) Biochemica et Biophysica Acta1041, 172–177.

    Google Scholar 

  • Ghatge, M.S. and Deshpande, V.V. (1993) Biochem. Biophys. Res. Commun.193, 979–984.

    Google Scholar 

  • Keskar, S.S., Rao, M. and Deshpande, V.V. (1992) Biochem. J.281, 601–605.

    Google Scholar 

  • Keskar, S.S., Srinivasan, M.C. and Deshpande, V.V. (1989) Biochem. J.261, 49–55.

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) J. Biol. Chem.193, 265.

    Google Scholar 

  • Mandels, M. and Weber, J. (1969) Adv. Chem. Ser.95, 391.

    Google Scholar 

  • Miller, G.L. (1959) Anal. Chem.31, 426–428.

    Google Scholar 

  • Srinivasan, M.C. and Rele, M.V. (1992) Fifth International Conference on Biotechnology in the Pulp and Paper Industry, Kyoto, Japan, May 27–30.

  • Srinivasan, M.C., Vartak, H.G., Powar, V.K., Rele, M.V., and Bastawde, K.B. (1984) Biotech. Lett.6, 715–718.

    Google Scholar 

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Authors and Affiliations

  1. Division of Biochemical Sciences, National Chemical Laboratory, 411008, Pune, India

    M. Rao, S. Khadilkar & V. Deshpande

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  1. M. Rao
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  2. S. Khadilkar
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  3. V. Deshpande
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Rao, M., Khadilkar, S. & Deshpande, V. Chemical modification of xylanase from Chainia sp. (NCL 82.5.1). Biotechnol Lett 17, 589–592 (1995). https://doi.org/10.1007/BF00129383

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  • DOI: https://doi.org/10.1007/BF00129383

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