ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary The alkane-induced, membrane-bound fatty alcohol oxidase of Candida tropicalis was functional with decanol as a model substrate in C8 to C12 alkanes and in cyclohexane. Optimal activity was with octane. Although some reaction took place without added water, 5–10% water gave optimal activity. A continuous spectrophotometric assay for following the enzyme activity in this system was developed. The enzyme, besides oxidizing primary long straight-chained alcohols, also oxidized long-chain diols, ω-hydroxy fatty acids, unsaturated fatty alcohols and branched-chained unsaturated fatty alcohols, although at diminished rates. Secondary alcohols or arylalkan-1-ols were not attacked. The K m for dodecanol was some 5000-fold higher than the K m for the same substrate when the reaction was carried out in water.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00180567
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