Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasiliense
Keyword(s):
An L-arabino-aldose dehydrogenase responsible for the oxidation of L-arabinose to L-arabino-γ-lactone has been purified 59-fold from L-arabinose grown cells of Azospirillum brasiliense. The dehydrogenase was found to be specific for substrates with the L-arabino-configuration at carbons 2, 3, and 4. Km values for L-arabinose of 75 and 140 μM were found with NADP and NAD as coenzymes, respectively. The enzyme had a pH optimum of 9.5 in glycine buffer and was stable when heated to 55 °C for 5 min. No enhancement of activity in the presence of any divalent cation or reducing agent tested was found. L-Arabinose dehydrogenase had a molecular weight of 175 000 as measured by the gel filtration technique.
1981 ◽
Vol 27
(10)
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pp. 1053-1059
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Keyword(s):
Keyword(s):
1974 ◽
Vol 31
(01)
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pp. 072-085
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1974 ◽
Vol 52
(3)
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pp. 231-240
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Keyword(s):
1978 ◽
Vol 56
(11)
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pp. 1028-1035
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