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 | |
| Publication status | Published - 1991 |
| MoE publication type | A1 Journal article-refereed |
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