Protein immobilisation is proving to be a cost-effective and environmentally friendly method of producing biochemicals with high yields. The “double-racemase hydantoinase process,” a system of four enzymes that produces optically pure L-amino acids from a racemic mixture of hydantoins, was optimised in this study. Protein hydrolysis, microbial fermentation, chemical synthesis, and enzymatic catalysis have all been utilised to make L-amino acids. The four proteins were immobilised independently, and the ideal overall relation was identified based on their particular activity. D,L-hydantoinase is the first enzyme, and it preferentially hydrolyzes D-hydantoins to N-carbamoyl-D-amino acids. The second enzyme, hydantoin racemase, racemizes the remaining L-hydantoins and continues to give substrate d-hydantoins to the first enzyme. The third enzyme, carbamoyl racemase, converts N-carbamoyl-D-amino acid to N-carbamoyl-l-amino acid. Finally, the fourth enzyme, L-carbamoylase, converts N-carbamoyl-L-amino acid to L-amino acid. As a result, one enzyme's product is the substrate for another. To avoid the accumulation of reaction intermediates and obtain an acceptable rate for commercial purposes, perfect coordination of the four activities is required. The system has a pH optimum range of 7–9, with a maximum activity at 8 and a temperature of 60°C. When the reaction velocity of the immobilised system was compared to the reaction velocity of the free protein system, the reaction velocity of norvaline, norleucine, ABA, and homophenylalanine increased, whereas it dropped for L-valine and stayed unchanged for L-methionine.
Author (s) DetailsFrancisco Javier Las Heras-Vázquez
Department of Chemistry and Physic, University of Almeria, The Agrifood Campus of International Excellence, ceiA3, E-04120 Almería, Spain and Research Centre for Agricultural and Food Biotechnology, CIAMBITAL, E-04120 Almería, Spain.
Felipe Rodríguez-Vico
Department of Chemistry and Physic, University of Almeria, The Agrifood Campus of International Excellence, ceiA3, E-04120 Almería, Spain and Research Centre for Agricultural and Food Biotechnology, CIAMBITAL, E-04120 Almería, Spain.
Lellys Mariela Contreras Moyeja
Department of Chemistry and Physic, University of Almeria, The Agrifood Campus of International Excellence, ceiA3, E-04120 Almería, Spain and Research Centre for Agricultural and Food Biotechnology, CIAMBITAL, E-04120 Almería, Spain.
Josefa María Clemente-Jiménez
Department of Chemistry and Physic, University of Almeria, The Agrifood Campus of International Excellence, ceiA3, E-04120 Almería, Spain and Research Centre for Agricultural and Food Biotechnology, CIAMBITAL, E-04120 Almería, Spain.
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