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

Kaur, Amandeep; Chadha, B.

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) of 101 kDa and p I 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 Mn ions. The enzyme preferentially catalyzed the hydrolysis of p-nitrophenol-β- d-glucopyranoside ( pNPG) but also recognized cellobiose as substrates. K and V for the hydrolysis of pNPG by β-glucosidase were calculated as 3.3 mM and 444 μmol min mg protein. Purified β-glucosidase showed transglycosylation activity in the presence of methanol as an acceptor molecule.

PENICILLIUM; GLUCOSIDASES; FERMENTATION; PEPTIDES; HYDROLASES; GLYCOSYLASES

Applied Biochemistry & Biotechnology, 2015, Vol 175, Issue 2, p937

0273-2289

Academic Journal

10.1007/s12010-014-1330-3