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Arelí Durón-Castellanos Vanesa Zazueta-Novoa Hortencia Silva-Jiménez Yolanda Alvarado-Caudillo Eduardo Peña Cabrera Roberto Zazueta-Sandoval 《Applied biochemistry and biotechnology》2005,121(1-3):279-288
Different soluble NAD+-dependent alcohol dehydrogenase (ADH) isozymes were detected in cell-free homogenates from aerobically grown mycelia of YR-1
strain of Mucor circinelloides isolated from petroleumcontaminated soil samples. Depending on the carbon source present in the growth media, multiple NAD+-dependent ADHs were detected when hexadecane or decane was used as the sole carbon source in the culture media. ADH activities
from aerobically or anaerobically grown mycelium or yeast cells, respectively, were detected when growth medium with glucose
added was the sole carbon source; the enzyme activity exhibited optimum pH for the oxidation of different alcohols (methanol,
ethanol, and hexadecanol) similar to that of the corresponding aldehyde (≈7.0). Zymogram analysis conducted with partially
purified fractions of extracts from aerobic mycelium or anaerobic yeast cells of the YR-1 strain grown in glucose as the sole
carbon source indicated the presence of a single NAD+-dependent ADH enzyme in each case, and the activity level was higher in the yeast cells. ADH enzyme from mycelium grown in
different carbon sources showed high activity using ethanol as substrate, although higher activity was displayed when the
cells were grown in hexadecane as the sole carbon source. Zymogram analysis with these extracts showed that this particular
strain of M. circinelloides has four different isozymes with ADH activity and, interestingly, one of them, ADH4, was identified also as phenanthrene-diol-dehydrogenase,
an enzyme that possibly participates in the aromatic hydrocarbon biodegradation pathway. 相似文献
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Alvarado-Caudillo Yolanda Torres José Carlos Bravo Novoa Vanesa Zazueta Jiménez Hortencia Silva Torres-Guzmán J. Carlos Gutiérrez-Corona J. Félix Zazueta-Sandoval Roberto 《Applied biochemistry and biotechnology》2002,98(1-9):243-255
A soluble alcohol oxidase (AO) activity was detected in the mycelium of a filamentous fungus strain named YR-1, isolated from
petroleum-contaminated soils. AO activity from aerobically grown mycelium was detected in growth media containing the hydrocarbons
decane or hexadecane; the enzyme activity exhibited optimum pH for the oxidation of different alcohols (methanol, ethanol,
and hexadecanol) similar to that of the corresponding aldehyde. Zymogram analysis conducted with purified fractions from aerobic
mycelium of YR-1 strain extracts indicated the existence of two AO enzymes (AO-1 and AO-2). Purified samples of both enzymes
analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis indicated the presence of three protein bands with molecular
sizes 20, 38, and 46 kDa that could be part of the native enzyme. In samples of both enzymes, the 46-kDa protein gave a positive
reaction in immunodetection experiments with antibodies directed against AO from Hansenula polymorpha. The purified AO-2 enzyme oxidized different alcohols, although higher activity was displayed with hexadecanol. K
m
values obtained for methanol and hexa-decanol indicated a higher affinity for the latter. Analysis of the aminoter-minal
sequence of the 46-kDa protein of AO-2 enzyme indicated significant similarity to enzymes involved in the metabolism of biphenyl
polychloride compounds. 相似文献
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