EC Number   |
Application |
Reference |
|---|
   3.5.1.87 | biotechnology |
production of optically pure L-amino acids by an enzymatic method named hydantoinase process |
675499 |
| 3.5.1.87 | more |
enzyme immobilization on solid matrix results in a great enhancement of the enzyme activity toward N-formyl-tryptophan, the reaction can be repeated for several cycles, method optimization, overview |
-, 733195 |
| 3.5.1.87 | more |
immobilization of the enzyme by covalent coupling to a solid support material including additional cross-linking with polyaldehyde-dextran, method development, overview. Temperature and pH optima of immobilized enzyme are increased by 10°C and 0.5 unit, respectively. The enzyme is significantly stabilized, it is recycled nine times with about 100% conversion efficiency when batch experiments are carried out at 35°C, pH 7.5, for the 180 min cycle |
-, 733544 |
| 3.5.1.87 | synthesis |
a bi-enzyme process for the synthesis of L-homophenylalanine from N-carbamoyl-D-homophenylalanine with immobilized N-acylamino acid racemase and immobilized L-N-carbamoylase. In batch operation, quantitative conversion is achieved. It is a promising alternative for the synthesis of L-homophenylalanine from racemate of N-carbamoyl-DL-homophenylalanine |
713443 |
| 3.5.1.87 | synthesis |
development of a bienzymatic biocatalyst system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting step of the system due to its lower specific activity, overview |
-, 735201 |
| 3.5.1.87 | synthesis |
production of a cell biocatalyst for the production of L-homophenylalanine from D,L-homophenylalanylhydantoin by coexpression of the pydB gene and a thermostable L-N-carbamoylase gene from Bacillus kaustophilus CCRC11223 in Escherichia coli JM109. The expression levels of dihydropyrimidinase and l-N-carbamoylase in the recombinant Escherichia coli cells are estimated to be about 20% of the respective total soluble proteins. When 1% (w/v) isopropyl-beta-D-thiogalactopyranoside-induced cells are used as biocatalysts, a conversion yield of 49% for D,L-homophenylalanylhydantoin with more than 99% enantiomeric excess can be reached in 16 h at pH 7.0 from 10 mM D,L-homophenylalanylhydantoin. The cells can be reused for at least eight cycles at a conversion yield of more than 43%. Coexpression of pydB and lnc in Escherichia coli might be a potential biocatalyst for production of L-homophenylalanylhydantoin |
-, 687885 |
| 3.5.1.87 | synthesis |
production of different optically pure L-alpha-amino acids starting from different racemic N-formyl- and N-carbamoyl-amino acids using a dynamic kinetic resolution approach with immobilized L-N-carbamoylase and N-succinyl-amino acid racemase as biocatalysts, the system is effective for the biosynthesis of natural and unnatural L-amino acids (enantiomeric excess over 99.5%), overview |
-, 733195 |
| 3.5.1.87 | synthesis |
the enzyme shows promise as a potential biocatalyst for L-alpha-amino acid production |
-, 733543 |
| 3.5.1.87 | synthesis |
to develop a recombinant Escherichia coli whole cell system for the conversion of racemic N-carbamoyl-L-homophenylalanine to L-homophenylalanine, naaar gene from Deinococcus radiodurans and L-N-carbamoylase gene from Bacillus kaustophilus BCRC11223 are cloned and coexpressed in Escherichia coli cells. Recombinant cells treated with 0.5% toluene at 30°C for 30 min exhibit enhanced N-acylamino acid racemase and L-N-carbamoylase activities, which are about 20fold and 60fold, respectively, higher than those of untreated cells. Using toluene-permeabilized recombinant Escherichia coli cells, a maximal productivity of 7.5 mmol L-homophenylalanine/l h with more than 99% yield could be obtained from 150 mmol racemic N-carbamoyl-D-homophenylalanine. Permeabilized cells show considerable stability in the bioconversion process using 10 mmol racemic N-carbamoyl-D-homophenylalanine as substrate, no significantly decrease in conversion yield for L-homophenylalanine is found in the eight cycles |
-, 689824 |
