Mild and selective hydrolysis of a large range of nitriles leading to carboxylic acids was achieved under neutral conditions by an immobilized and genetically modified enzyme preparation from Alcaligenes faecalis ATCC8750. This immobilized nitrilase has been shown to be an effective catalyst for the stereoselective hydrolysis of mandelonitrile 1a to R-(-)-mandelic acid 1c. This method is particularly useful for the production of hydroxy analogues of methionine derivatives 2c-4c that could have an interest in cattle feeding and for the transformation of compounds containing other acid- or base-sensitive groups 3a-10a. A series of aliphatic dinitriles 11a-15a was hydrolyzed to the corresponding cyano acids. The suitability of the immobilized catalyst as a robust and versatile biocatalyst is discussed, and models to account for the stereoselectivity of the enzymic hydrolysis have been proposed.
Bed‐to‐wall heat transfer was measured in three‐phase fluidized beds under conditions typical of biochemical process applications. The thermal resistance of the fluidized bed, which was significant in the absence of gas, became negligible when gas was introduced. Decreasing the particle density at constant gas and liquid velocity increased the bed‐to‐wall heat transfer coefficient.
Previously published heat transfer correlations were used and gave poor predictions of our data. A new correlation was developed which predicted very well all the heat transfer coefficient results in this paper.
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