Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity

Kazuhiro Chiku, Hirofumi Dohi, Akihiro Saito, Hiroki Ebise, Yusuke Kouzai, Hirofumi Shinoyama, Yoshihiro Nishida, Akikazu Ando

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish
Pages (from-to)1123-1128
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume73
Issue number5
DOIs
Publication statusPublished - 2009
Externally publishedYes

Fingerprint

Monophenol Monooxygenase
Enzymes
Inhibitory Concentration 50
Arbutin
Xylans
Quinine
Agaricales
Bacilli
Escherichia coli
Bacillus
Oxidation
Kinetics

Keywords

  • 4-hydroxyphenyl β- oligoxylosides
  • Transxylosylation
  • Tyrosinase inhibitor

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Analytical Chemistry
  • Organic Chemistry

Cite this

Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity. / Chiku, Kazuhiro; Dohi, Hirofumi; Saito, Akihiro; Ebise, Hiroki; Kouzai, Yusuke; Shinoyama, Hirofumi; Nishida, Yoshihiro; Ando, Akikazu.

In: Bioscience, Biotechnology and Biochemistry, Vol. 73, No. 5, 2009, p. 1123-1128.

Research output: Contribution to journalArticle

Chiku, K, Dohi, H, Saito, A, Ebise, H, Kouzai, Y, Shinoyama, H, Nishida, Y & Ando, A 2009, 'Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity', Bioscience, Biotechnology and Biochemistry, vol. 73, no. 5, pp. 1123-1128. https://doi.org/10.1271/bbb.80885
Chiku, Kazuhiro ; Dohi, Hirofumi ; Saito, Akihiro ; Ebise, Hiroki ; Kouzai, Yusuke ; Shinoyama, Hirofumi ; Nishida, Yoshihiro ; Ando, Akikazu. / Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity. In: Bioscience, Biotechnology and Biochemistry. 2009 ; Vol. 73, No. 5. pp. 1123-1128.
@article{ba41d97cd15c49f7957913b98a124cc4,
title = "Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity",
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.",
keywords = "4-hydroxyphenyl β- oligoxylosides, Transxylosylation, Tyrosinase inhibitor",
author = "Kazuhiro Chiku and Hirofumi Dohi and Akihiro Saito and Hiroki Ebise and Yusuke Kouzai and Hirofumi Shinoyama and Yoshihiro Nishida and Akikazu Ando",
year = "2009",
doi = "10.1271/bbb.80885",
language = "English",
volume = "73",
pages = "1123--1128",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "5",

}

TY - JOUR

T1 - Enzymatic synthesis of 4-hydroxyphenyl β-D-oligoxylosides and their notable tyrosinase inhibitory activity

AU - Chiku, Kazuhiro

AU - Dohi, Hirofumi

AU - Saito, Akihiro

AU - Ebise, Hiroki

AU - Kouzai, Yusuke

AU - Shinoyama, Hirofumi

AU - Nishida, Yoshihiro

AU - Ando, Akikazu

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

KW - 4-hydroxyphenyl β- oligoxylosides

KW - Transxylosylation

KW - Tyrosinase inhibitor

UR - http://www.scopus.com/inward/record.url?scp=67049118076&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67049118076&partnerID=8YFLogxK

U2 - 10.1271/bbb.80885

DO - 10.1271/bbb.80885

M3 - Article

C2 - 19420707

AN - SCOPUS:67049118076

VL - 73

SP - 1123

EP - 1128

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 5

ER -