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Penicillium janthinellum: a Source of Efficient and High Levels of β-Glucosidase

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Abstract

Penicillium janthinellum strain isolated from leaf litters of oak trees from montane alpine forests of Shivalik hills (India) produced high levels of β-glucosidase both during solid-state fermentation (796 units/gds) and shake flask cultures (65.3 units/ml). The peptide mass fingerprinting of the secretome showed a variety of glycosyl hydrolases. β-Glucosidase was purified and characterized to be a GH3 family member that had a molecular weight (M r) of 101 kDa and pI of 4.5. β-Glucosidase was optimally active at 60 °C at pH 5.0 but showed appreciable activity and thermostability under alkaline conditions (pH 9.0) also. β-Glucosidase activity was positively modulated in the presence of Mn2+ ions. The enzyme preferentially catalyzed the hydrolysis of p-nitrophenol-β-d-glucopyranoside (pNPG) but also recognized cellobiose as substrates. K m and V max for the hydrolysis of pNPG by β-glucosidase were calculated as 3.3 mM and 444 μmol min−1 mg protein−1. Purified β-glucosidase showed transglycosylation activity in the presence of methanol as an acceptor molecule.

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Acknowledgments

The financial support from NAIP (ICAR) for carrying out this research project (NAIP/Comp-4/C-30030) “Novel biotechnological processes for production of high value products from rice straw and bagasse” is duly acknowledged.

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Authors and Affiliations

  1. Department of Microbiology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India

    Amandeep Kaur & B. S. Chadha

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  1. Amandeep Kaur
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  2. B. S. Chadha
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Correspondence to B. S. Chadha.

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Kaur, A., Chadha, B.S. Penicillium janthinellum: a Source of Efficient and High Levels of β-Glucosidase. Appl Biochem Biotechnol 175, 937–949 (2015). https://doi.org/10.1007/s12010-014-1330-3

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  • DOI: https://doi.org/10.1007/s12010-014-1330-3

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