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Purification and characterization of a novel α-glucosidase from Malbranchea cinnamomea

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Abstract

Objectives

To characterize a novel α-glucosidase from the thermophilic fungus Malbranchea cinnamomea.

Results

The enzyme was purified to homogeneity with purification fold of 40 and a recovery of 7.2 %. It was a monomer with molecular mass of 65.7 kDa on SDS-PAGE. It was optimally active at pH 6 and 50 °C (measured over 10 min) and exhibited a wide range of substrate specificity with the highest specific activity of 47.4 U mg−1 for p-nitrophenyl α-d-glucopyranoside (pNPGlu) followed by isomaltose, panose and sucrose, suggesting that the enzyme belongs to the type I α-glucosidases. The K m values of the α-glucosidase for pNPGlu and isomaltose were 1.1 and 19.3 mM, respectively.

Conclusion

Because of its unique properties, the α-glucosidase may have a potential in several industrial applications.

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Acknowledgments

This work was financially supported by the Program for Changjiang Scholars, National Science Fund for Distinguished Young Scholars (No. 31325021) and the National Natural Science Foundation of China (Project No. 31101238).

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Authors and Affiliations

  1. Bioresource Utilization Laboratory, College of Engineering, China Agricultural University, Beijing, China

    Q. J. Yan

  2. Food Enzyme & Fermentation Engineering Laboratory, College of Food Science and Nutritional Engineering, China Agricultural University, Qinghua Donglu, Haidian District, Beijing, 100083, China

    P. Han, S. Q. Yang & Z. Q. Jiang

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  1. Q. J. Yan
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  2. P. Han
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  3. S. Q. Yang
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  4. Z. Q. Jiang
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Correspondence to Z. Q. Jiang.

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Yan, Q.J., Han, P., Yang, S.Q. et al. Purification and characterization of a novel α-glucosidase from Malbranchea cinnamomea . Biotechnol Lett 37, 1279–1286 (2015). https://doi.org/10.1007/s10529-015-1798-0

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  • DOI: https://doi.org/10.1007/s10529-015-1798-0

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