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Application of immobilized chymotrypsin in a multistage fluidized‐bed reactor
Author(s) -
Halwachs W.,
Wandrey C.,
Schügerl K.
Publication year - 1977
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260191106
Subject(s) - continuous stirred tank reactor , chemistry , fluidized bed , hydrolysis , chymotrypsin , chromatography , phenylalanine , organic chemistry , amino acid , enzyme , biochemistry , trypsin
The stereospecific hydrolysis of D , L ‐phenylalanine methylester with immobilized α‐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.