Abstract
We have purified and characterized an oligoxylosyl transfer enzyme (OxtA) from Bacillus sp. strain KT12. In the present study, a N-terminally His-tagged recombinant form of the enzyme, OxtA(H)E, was overproduced in Escherichia coli and applied to the reaction with xylan and hydroquinone to produce 4-hydroxyphenyl β-D-oligoxylosides, β-(Xyl)n-HQ (n =1-4), by one step reaction. The obtained β-(Xyl)n-HQ inhibited mushroom tyrosinase, which catalyzes the oxidation of L-DOPA to L-DOPA quinine, and the IC50 values of β-Xyl-HQ, β-(Xyl)2-HQ, β-(Xyl) 3-HQ, and β-(Xyl)4-HQ were 3.0, 0.74, 0.48, and 0.18mM respectively. β-(Xyl)4-HQ showed 35-fold more potent inhibitory activity than β-arbutin (4-hydroxyphenyl β-D- glucopyranoside), of which the IC50 value was measured to be 6.3mM. Kinetic analysis revealed that β-(Xyl)2-HQ, β-(Xyl)3-HQ, and β-(Xyl)4-HQ competitively inhibited the enzyme, and the corresponding Ki values were calculated to be 0.20, 0.29, and 0.057mM respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 1123-1128 |
| Number of pages | 6 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 73 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2009 |
Keywords
- 4-hydroxyphenyl β- oligoxylosides
- Transxylosylation
- Tyrosinase inhibitor
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry