Synthesis of the kyotorphin precursor benzoyl‐L‐tyrosine‐L‐argininamide with immobilized α‐chymotrypsin in sequential batch with enzyme reactivation |
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| Authors: | Carola Bahamondes Lorena Wilson Claudia Bernal Andrés Illanes Gregorio Álvaro Fanny Guzmán |
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| Institution: | 1. School of Biochemical Engineering, Pontificia Universidad Católica De Valparaiso, Chile;2. Department of Chemical Engineering, School of Engineering, Universitat Autònoma De Barcelona, Spain;3. Núcleo Biotecnología Curauma. Pontificia Universidad Católica De Valparaíso, Chile |
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| Abstract: | 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 |
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| Keywords: | enzymatic synthesis α ‐chymotrypsin kyotorphin enzymatic reactivation |
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