Purification and characterization of methanol dehydrogenase of Methylobacterium nodulans rhizosphere phytosymbionts |
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Authors: | T A Kuznetsova A P Beschastny O N Ponamoreva Yu A Trotsenko |
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Institution: | 2. Tula State University, Tula, 300600, Russia 1. Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, Pushchino, Moscow oblast, 142290, Russia
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Abstract: | Methanol dehydrogenase (MDH) of the facultative methylotrophic phytosymbiont Methylobacterium nodulans has been purified for the first time to an electrophoretically homogeneous state and characterized. The native protein with a molecular mass of 70 kDa consists of large (60 kDa) and small (6.5 kDa) subunits. The purified protein displayed a spectrum identical to that of pyrroloquinoline quinone (PQQ)-containing MDH, pI 8.7, pH optimum in the range 9–10. The enzyme was inactive in the absence of ammonium or methylamine and exhibited a wide substrate specificity with regard to C1–C5 alcohols with the high-est affinity to methanol (K M = 70 μM), but it did not oxidize benzyl and secondary alcohols. The apparent K M values to primary alcohols increased with the length of the carbon chain. The enzyme was characterized by a high stability level even in the absence of a substrate. An immobilized enzyme was used for amperometric methanol detection. |
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