Penicillium janthinellum: a Source of Efficient and High Levels of β-Glucosidase
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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Artikel |
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Erscheinungsjahr: |
2015 |
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Erschienen: |
2015 |
Enthalten in: |
Zur Gesamtaufnahme - volume:175 |
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Enthalten in: |
Applied biochemistry and biotechnology / A - 175(2015), 2, Seite 937-949 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Kaur, Amandeep [VerfasserIn] |
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Links: |
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doi: |
10.1007/s12010-014-1330-3 |
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funding: |
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PPN (Katalog-ID): |
OLC1967121486 |
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520 | |a 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. | ||
540 | |a Nutzungsrecht: © Springer Science+Business Media New York 2015 | ||
650 | 4 | |a Biochemistry, general | |
650 | 4 | |a β-Glucosidase | |
650 | 4 | |a Penicillium janthinellum | |
650 | 4 | |a Chemistry | |
650 | 4 | |a Acid and alkaline active | |
650 | 4 | |a GH3 family | |
650 | 4 | |a Biotechnology | |
650 | 4 | |a Penicillium - metabolism | |
650 | 4 | |a Plant Leaves - metabolism | |
650 | 4 | |a Metals - pharmacology | |
650 | 4 | |a Penicillium - enzymology | |
650 | 4 | |a beta-Glucosidase - metabolism | |
650 | 4 | |a beta-Glucosidase - biosynthesis | |
650 | 4 | |a beta-Glucosidase - chemistry | |
650 | 4 | |a Quercus - microbiology | |
650 | 4 | |a beta-Glucosidase - isolation & purification | |
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