A xylose-oxidizing membrane-bound aldose dehydrogenase of Gluconobacter oxydans ATCC 621

Johanna Buchert

Research output: Contribution to journalArticleScientificpeer-review

28 Citations (Scopus)

Abstract

A xylose-oxidizing membrane-bound aldose dehydrogenase was purified from Gluconobacter oxydans subsp suboxydans ATCC 621. The enzyme did not require added coenzyme for activity and could oxidize d-glucose, d-xylose, d-galactose, d-mannose and l-arabinose. d-Glucose was oxidized 1.6 times faster than d-xylose. The enzyme had a molecular mass of 87 kDa and appeared as a single polypeptide. Nitrotetrazolium blue — phenazine methosulphate and dichlorophenol indophenol — phenazine methosulphate were efficient electron acceptors.

Original languageEnglish
Pages (from-to)103 - 114
Number of pages12
JournalJournal of Biotechnology
Volume18
Issue number1
DOIs
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

Fingerprint

Gluconobacter oxydans
Methylphenazonium Methosulfate
Xylose
Oxidoreductases
2,6-Dichloroindophenol
Membranes
Nitroblue Tetrazolium
Arabinose
Glucose
Coenzymes
Enzymes
Mannose
Galactose
Polypeptides
Molecular mass
Electrons
Peptides

Cite this

@article{20f42a8c589c4880a2fa2a155313d6a4,
title = "A xylose-oxidizing membrane-bound aldose dehydrogenase of Gluconobacter oxydans ATCC 621",
abstract = "A xylose-oxidizing membrane-bound aldose dehydrogenase was purified from Gluconobacter oxydans subsp suboxydans ATCC 621. The enzyme did not require added coenzyme for activity and could oxidize d-glucose, d-xylose, d-galactose, d-mannose and l-arabinose. d-Glucose was oxidized 1.6 times faster than d-xylose. The enzyme had a molecular mass of 87 kDa and appeared as a single polypeptide. Nitrotetrazolium blue — phenazine methosulphate and dichlorophenol indophenol — phenazine methosulphate were efficient electron acceptors.",
author = "Johanna Buchert",
note = "Project code: BIO6004",
year = "1991",
doi = "10.1016/0168-1656(91)90239-R",
language = "English",
volume = "18",
pages = "103 -- 114",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "1",

}

A xylose-oxidizing membrane-bound aldose dehydrogenase of Gluconobacter oxydans ATCC 621. / Buchert, Johanna.

In: Journal of Biotechnology, Vol. 18, No. 1, 1991, p. 103 - 114.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - A xylose-oxidizing membrane-bound aldose dehydrogenase of Gluconobacter oxydans ATCC 621

AU - Buchert, Johanna

N1 - Project code: BIO6004

PY - 1991

Y1 - 1991

N2 - A xylose-oxidizing membrane-bound aldose dehydrogenase was purified from Gluconobacter oxydans subsp suboxydans ATCC 621. The enzyme did not require added coenzyme for activity and could oxidize d-glucose, d-xylose, d-galactose, d-mannose and l-arabinose. d-Glucose was oxidized 1.6 times faster than d-xylose. The enzyme had a molecular mass of 87 kDa and appeared as a single polypeptide. Nitrotetrazolium blue — phenazine methosulphate and dichlorophenol indophenol — phenazine methosulphate were efficient electron acceptors.

AB - A xylose-oxidizing membrane-bound aldose dehydrogenase was purified from Gluconobacter oxydans subsp suboxydans ATCC 621. The enzyme did not require added coenzyme for activity and could oxidize d-glucose, d-xylose, d-galactose, d-mannose and l-arabinose. d-Glucose was oxidized 1.6 times faster than d-xylose. The enzyme had a molecular mass of 87 kDa and appeared as a single polypeptide. Nitrotetrazolium blue — phenazine methosulphate and dichlorophenol indophenol — phenazine methosulphate were efficient electron acceptors.

U2 - 10.1016/0168-1656(91)90239-R

DO - 10.1016/0168-1656(91)90239-R

M3 - Article

VL - 18

SP - 103

EP - 114

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 1

ER -