Abstract
Nitrile hydratase from Rhodococcus sp. DSM 11397 and nitrilase from Pseudomonas. DSM 11387 both retained activity in various organic/aqueous biphasic mixtures. Both enzymes were most tolerant (66–109% retained activity) of C8 and C16 alkanes with log P values greater than 4.0. Some enzyme activity (<10% nitrile hydratase, <60% nitrilase) was also retained in monophasic water-saturated C6-C11 n-alkanols. © Rapid Science Ltd. 1998
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References
Halling, P.J. (1989). Trends Biotechnol., 7, 50–56.
Laane, C., Boeren, S., Vos, K and Veeger, C. (1986). Biotechnol. and Bioeng., 30, 81–87.
Layh, N., Hirrlinger, B., Stolz, A. and Knackmuss, H-J. (1997). Appl. Micro-biol. Biotechnol., 47, 668–674.
Nagasawa, T. and Yamada, H. (1990). Chp. 14 in: Biocatalysis, D.A. Abramowicz, ed., pp. 277–318; Van Norstrand Reinhold, New York.
Nagasawa, T., Shimizu, H. and Yamada, H. (1993). Appl. Microbiol. Biotechnol., 40, 189–195.
Riva, S. and Faber, K. (1992). Synthesis, 895–936.
Wescott, C.R. and Klibanov, A.M. (1994). Biochim. Biophys. Acta, 1206, 1–9.
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Layh, N., Willetts, A. Enzymatic nitrile hydrolysis in low water systems. Biotechnology Letters 20, 329–331 (1998). https://doi.org/10.1023/A:1005358809561
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DOI: https://doi.org/10.1023/A:1005358809561