n-carbamoyl-d-p-hydroxyphenylglycine production using immobilized d-hydantoinase from recombinant E. coli |
| |
Authors: | Cheng-Kang Lee Kung-Chern Lin |
| |
Institution: | Department of Chemical Engineering, National Taiwan Institute of Technology, Taipei, Taiwan, 10672 |
| |
Abstract: | An immobilized d-hydantoinase was characterized and employed to produce n-carbamoyl-d-p-hydroxyphenylglycine (CpHPG) in a repeated batch process. The Vmax and Km of the immobilized d-hydantoinase at 50°C were 6.28 mm min−1 g−1 biocatalyst and 71.6 mm, respectively. The product CpHPG did not inhibit the activity of d-hydantoinase. Optimal reaction temperature was 60°C. A decrease in activity of immobilized d-hydantoinase due to thermal inactivation could be described as first-order decay; the deactivation energy was 23.97Kcal mol−1. Under process conditions (50°C, 10% w/v substrate, and pH 8.5), the half-life of the immobilized d-hydantoinase was eight batches. The attrition of immobilized d-hydantoinase particles with a large amount of insoluble substrate particles during stirring resulted in fine biocatalyst particles. In addition to the thermal inactivation, the loss of fine biocatalyst particles during the recovery step contributed to the low operational stability. |
| |
Keywords: | d-hydantoinase" target="_blank">Immobilized d-hydantoinase n-carbamoyl-p-hydroxyphenylglycine" target="_blank">n-carbamoyl-p-hydroxyphenylglycine thermal stability repeated batch |
本文献已被 ScienceDirect 等数据库收录! |