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標題: Optimal covalent immobilization of alpha-chymotrypsin on Fe3O4-chitosan nanoparticles
作者: Ju, H.Y.
Kuo, C.H.
Too, J.R.
Huang, H.Y.
Twu, Y.K.
Chang, C.M.J.
Liu, Y.C.
Shieh, C.J.
關鍵字: Enzymatic peptide synthesis;alpha-Chymotrypsin;Covalent;immobilization;Fe3O4-chitosan nanoparticles;Optimization;catalyzed peptide-synthesis;membrane reactor;chitosan;particles;microspheres;purification;carrier;beads
Project: Journal of Molecular Catalysis B-Enzymatic
期刊/報告no:: Journal of Molecular Catalysis B-Enzymatic, Volume 78, Page(s) 9-15.
This study investigated the immobilization of alpha-chymotrypsin onto magnetic Fe3O4-chitosan (alpha-chymotrypsin-Fe3O4-CS) nanoparticles by covalent binding. The response surface methodology (RSM) with a 3-factor-3-level Box-Behnken experimental design was employed to evaluate the effects of the manipulated variables, including the immobilization time, temperature, and pH, on the enzyme activity. The results indicate that the immobilized temperature and pH significantly affected enzyme activity. In a ridge max analysis, the optimal condition for alpha-chymotrypsin immobilization included a reaction temperature of 21.7 degrees C, a pH of 7.6, and an incubation time of 1.1 h. The predicted and the experimental immobilized enzyme activities were 354 and 347 +/- 46.5 U/g-support, respectively, under the optimal condition. Besides, the synthesis reactions of the dipeptide derivative using the free and immobilized alpha-chymotrypsin were compared. The yields of the dipepticle derivative via the free or immobilized alpha-chymotrypsin catalyzed were almost the same. The alpha-chymotrypsin-Fe3O4-CS nanoparticles exhibited a good acid-resisting ability and the less reaction time was required for dipeptide synthesis. After twelve repeated uses in dipeptide synthesis, the immobilized alpha-chymotrypsin still retained over 60% of its original activity. The magnetic alpha-chymotrypsin-Fe3O4-CS nanoparticles can be easily recovered by magnetic field will have potential application in industry. (C) 2012 Elsevier By. All rights reserved.
ISSN: 1381-1177
DOI: 10.1016/j.molcatb.2012.01.015
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