Halwachs W, Wandrey C, Schügerl K
Biotechnol Bioeng. 1977 Nov;19(11):1667-77. doi: 10.1002/bit.260191106.
The stereospecific hydrolysis of D,L-phenylalanine methylester with immobilized alpha-chymotrypsin was carried out as a model reaction for the racemate resolution of aromatic amino acids in a five staged fluidized-bed reactor (FBR). Owing to ester hydrolysis, a pH shift occurred along the reactor. Because of the pH-dependent enzyme activity a particular longitudinal pH profile had to be enforced by a proper entrance pH in order to gain an optimum conversion. In the FBR with optimum pH profile, higher conversions were achieved than in a continuous stirred tank reactor (CSTR) at the pH optimum and at the same contact time. By the application of a proton balance and the results of kinetic measurements a model was developed for the prediction of the optimum longitudinal pH profile with regard to the maximum conversion.