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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.

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⁻¹ 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: Rb₁ → Rd → F₂ → compound K, Rb₂ → compound O → compound Y, Rc → compound Mc₁ → compound Mc, Rg₃ → Rh₂ → aglycone protopanaxadiol (APPD), Rg₁ → F₁, and Rf → Rh₁ → aglycone protopanaxatriol (APPT). Under the optimum conditions, the enzyme converted 0.5 mM Rb₂, Rc, Rd, Rg₃, Rg₁, 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 F₁, and 0.44 mM APPT after 6 h, respectively.

journal_name

Appl Microbiol Biotechnol

journal_title

Applied microbiology and biotechnology

authors

Lee GW,Yoo MH,Shin KC,Kim KR,Kim YS,Lee KW,Oh DK

doi

10.1007/s00253-013-4828-7

subject

Has Abstract

pub_date

2013-07-01 00:00:00

pages

6315-24

issue

14

eissn

0175-7598

issn

1432-0614

journal_volume

97

pub_type

杂志文章

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