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Continuous proteolysis with a stabilized protease. II. Continuous experiments
Author(s) -
Boudrant J.,
Cheftel C.
Publication year - 1976
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.260181208
Subject(s) - proteolysis , chemistry , casein , hydrolysate , protease , ultrafiltration (renal) , chromatography , substrate (aquarium) , whey protein , enzyme , hydrolysis , biochemistry , biology , ecology
Batch proteolysis experiments were performed in order to choose a protein–protease system to prepare a correct hydrolysate suitable for the enrichment of soft‐drinks. The system eventually studied was casein–Alcalase. Comparative batch and continuous proteolysis of casein by Alcalase showed that the reaction, which does not exactly follow first order kinetics with respect to the substrate concentration, is inhibited by the reaction products. Furthermore, experiments were done in order to determine the reaction conditions (pH 8.8 in the reactor, casein concentration 5%, 40°C). Determining the molecular weight of Alcalase (43,000) suggested the choice of ultrafiltration membrane PM 30. Studies of continuous proteolysis with the chemically stabilized enzyme retained by the ultrafiltration reactor showed that protease reuse for seven days at 40°C is possible and that the growth of microorganisms is practically inhibited under these conditions. Gel chromatography showed the molecular weight range of the peptides to be less than 2,000. Triangular taste tests showed that the threshold identification concentration of the dry hydrolysate in orange juice is about 0.65%.