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Microbiology and Biotechnology Letters

Research Article(보문)

Environmental Microbiology  |  Biodegradation and Bioremediation

Microbiol. Biotechnol. Lett.

Received: September 9, 2024; Revised: December 18, 2024

Enhanced β-glucosidase production by Penicillium simplicissimum mutant strains under solid state fermentation

Tivaporn Srisapoom 1, Thanaphon Thongrutsamee 2, Wandee Bunyatratchata 3 and Wiyada Mongkolthanaruk 4*

1Department of Microbiology, Faculty of Science, Khon Kaen University, 2Department of Microbiology, Faculty of Science, Khon Kaen University, 3Department of Microbiology, Faculty of Science, Khon Kaen University, 4Department of Microbiology, Faculty of Science, Khon Kaen University

Correspondence to :
Wiyada Mongkolthanaruk, Department of Microbiology, Faculty of Science, Khon Kaen University, 123 M.16 Mittraparp Road, Muang, Khon Kaen, Thailand [40002]
Tel : (+66)43202377, Fax : -, E-mail : wiymon@kku.ac.th

Abstract

Cellulase enzymes play a key role in degrading cellulose to produce sugars, with agricultural materials serving as primary sources after lignin removal. Fungi are efficient producers of cellulolytic enzymes, including cellulase. Penicillium JLP3201 was a potential strain that produced endocellulase, exocellulase and β-glucosidase at 3.58, 1.52 and 13.20 U/g, respectively. It produced the highest endocellulase and β-glucosidase in solid state fermentation of 1% NaOH-pretreated rain tree leaves, which outperformed other substrates. All enzymes indicated the optimum condition at pH 4.0 and 50oC; β-glucosidase was less stable above 60oC after one hour. The fungal strain was mutated by UVC radiation, called Penicillium MU8-0, that demonstrated higher endocellulase and β-glucosidase at 4.91 and 66.00 U/g, respectively, achieving a 5-fold increase in β-glucosidase. The enzyme properties of the mutant strain changed, showing stability at pH 7.0 and higher temperature tolerance up to 70oC.

Keywords: agricultural residues, fungal cellulase, rain tree leaves, random mutation, β-glucosidase

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