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- Title
β-Glucosidase from Penicillium aculeatum hydrolyzes exo-, 3- O-, and 6- O-β-glucosides but not 20- O-β-glucoside and other glycosides of ginsenosides.
- Authors
Lee, Gi-Woong; Yoo, Mi-Hyun; Shin, Kyung-Cheol; Kim, Kyoung-Rok; Kim, Yeong-Su; Lee, Ki-Won; Oh, Deok-Kun
- Abstract
A novel β-glucosidase from Penicillium aculeatum was purified as a single 110.5-kDa band on SDS-PAGE with a specific activity of 75.4 U mg by salt precipitation and Hi-Trap Q HP and Resource Q ion exchange chromatographies. The purified enzyme was identified as a member of the glycoside hydrolase 3 family based on its amino acid sequence. The hydrolysis activity for p-nitrophenyl-β- d-glucopyranoside was optimal at pH 4.5 and 70 °C with a half-life of 55 h. The enzyme hydrolyzed exo-, 3- O-, and 6- O-β-glucosides but not 20- O-β-glucoside and other glycosides of ginsenosides. Because of the novel specificity, this enzyme had the transformation pathways for ginsenosides: Rb → Rd → F → compound K, Rb → compound O → compound Y, Rc → compound Mc → compound Mc, Rg → Rh → aglycone protopanaxadiol (APPD), Rg → F, and Rf → Rh → aglycone protopanaxatriol (APPT). Under the optimum conditions, the enzyme converted 0.5 mM Rb Rc, Rd, Rg, Rg, and Rf to 0.49 mM compound Y, 0.49 mM compound Mc, 0.47 mM compound K, 0.23 mM APPD, 0.49 mM F, and 0.44 mM APPT after 6 h, respectively.
- Subjects
GLUCOSIDASES; PENICILLIUM; GINSENOSIDES; PRECIPITATION (Chemistry); CHROMATOGRAPHIC analysis; HYDROLYSIS
- Publication
Applied Microbiology & Biotechnology, 2013, Vol 97, Issue 14, p6315
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-013-4828-7