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

Johanna Buchert

doi:10.1016/0168-1656(91)90239-R

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

Johanna Buchert

VTT Technical Research Centre of Finland

Research output: Contribution to journal › Article › Scientific › peer-review

30 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 language	English
Pages (from-to)	103-114
Journal	Journal of Biotechnology
Volume	18
Issue number	1
DOIs	https://doi.org/10.1016/0168-1656(91)90239-R
Publication status	Published - 1991
MoE publication type	A1 Journal article-refereed

Access to Document

10.1016/0168-1656(91)90239-R

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 B.V.",

number = "1",

}

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

SN - 0168-1656

VL - 18

SP - 103

EP - 114

JO - Journal of Biotechnology

JF - Journal of Biotechnology

IS - 1

ER -

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

Abstract

Access to Document

Fingerprint

Cite this