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Purification and characterization of a novel alkaline β-1,3-1,4-glucanase (lichenase) from thermophilic fungus Malbranchea cinnamomea

  • Biocatalysis
  • Published:
Journal of Industrial Microbiology & Biotechnology

Abstract

A novel alkaline β-1,3-1,4-glucanase (McLic1) from a thermophilic fungus, Malbranchea cinnamomea, was purified and biochemically characterized. McLic1 was purified to homogeneity with a purification fold of 3.1 and a recovery yield of 3.7 %. The purified enzyme was most active at pH 10.0 and 55 °C, and exhibited a wide range of pH stability (pH 4.0–10.0). McLic1 displayed strict substrate specificity for barley β-glucan, oat β-glucan and lichenan, but did not show activity towards other tested polysaccharides and synthetic p-nitrophenyl derivates, suggesting that it is a specific β-1,3-1,4-glucanase. The K m values for barley β-glucan, oat β-glucan and lichenan were determined to be 0.69, 1.11 and 0.63 mg mL−1, respectively. Moreover, the enzyme was stable in various non ionic surfactants, oxidizing agents and several commercial detergents. Thus, the alkaline β-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries.

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Acknowledgments

This study was financially supported by the National Science Fund for Distinguished Young Scholars (No. 31325021) and National Natural Science Foundation of China (No. 31071508).

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Correspondence to Zhengqiang Jiang.

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Yang, S., Xiong, H., Yan, Q. et al. Purification and characterization of a novel alkaline β-1,3-1,4-glucanase (lichenase) from thermophilic fungus Malbranchea cinnamomea . J Ind Microbiol Biotechnol 41, 1487–1495 (2014). https://doi.org/10.1007/s10295-014-1494-4

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  • DOI: https://doi.org/10.1007/s10295-014-1494-4

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