Application of immobilized chymotrypsin in a multistage fluidized-bed reactor.
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.
D002918:Chymotrypsin / Q000378:metabolism; D004800:Enzymes, Immobilized / Q000378:metabolism; D007221:Industry; D007700:Kinetics; D008722:Methods; D010649:Phenylalanine; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D004800:Enzymes, Immobilized; D010649:Phenylalanine; D002918:Chymotrypsin