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Synthesis of the kyotorphin precursor benzoyl‐ L ‐tyrosine‐ L ‐argininamide with immobilized α‐chymotrypsin in sequential batch with enzyme reactivation
Author(s) -
Bahamondes Carola,
Wilson Lorena,
Bernal Claudia,
Illanes Andrés,
Álvaro Gregorio,
Guzmán Fanny
Publication year - 2015
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.2187
Subject(s) - chemistry , immobilized enzyme , biocatalysis , ethanol , chromatography , acetonitrile , enzyme , agarose , organic chemistry , combinatorial chemistry , catalysis , reaction mechanism
α‐Chymotrypsin was immobilized in activated agarose support and the stability of the biocatalyst was assessed in three polar organic solvents, namely, ethanol, diglyme, and acetonitrile. Ethanol was the solvent in which the stability of the enzyme was higher and was then selected to perform the synthesis of the kyotorphin derivative benzoyl‐tyrosine argininamide, evaluating enzyme reactivation after synthesis. Substrates for reaction were benzoyl tyrosine ethyl ester and argininamide, the reaction being performed under kinetic control. High conversion yield (85%) was obtained and the immobilized enzyme was successfully used in sequential batch reactor operation with enzyme reactivation after three batches. © 2015 American Institute of Chemical Engineers Biotechnol. Prog. , 32:54–59, 2016