43163-93-5Relevant articles and documents
Sustainable and Continuous Synthesis of Enantiopure l-Amino Acids by Using a Versatile Immobilised Multienzyme System
Velasco-Lozano, Susana,da Silva, Eunice S.,Llop, Jordi,López-Gallego, Fernando
, p. 395 - 403 (2017/11/13)
The enzymatic synthesis of α-amino acids is a sustainable and efficient alternative to chemical processes, through which achieving enantiopure products is difficult. To more address this synthesis efficiently, a hierarchical architecture that irreversibly co-immobilises an amino acid dehydrogenase with polyethyleneimine on porous agarose beads has been designed and fabricated. The cationic polymer acts as an irreversible anchoring layer for the formate dehydrogenase. In this architecture, the two enzymes and polymer colocalise across the whole microstructure of the porous carrier. This multifunctional heterogeneous biocatalyst was kinetically characterised and applied to the enantioselective synthesis of a variety of canonical and noncanonical α-amino acids in both discontinuous (batch) and continuous modes. The co-immobilised bienzymatic system conserves more than 50 % of its initial effectiveness after five batch cycles and 8 days of continuous operation. Additionally, the environmental impact of this process has been semiquantitatively calculated and compared with the state of the art.
ω-Transaminase-catalyzed asymmetric synthesis of unnatural amino acids using isopropylamine as an amino donor
Park, Eul-Soo,Dong, Joo-Young,Shin, Jong-Shik
, p. 6929 - 6933 (2013/10/08)
Isopropylamine is an ideal amino donor for reductive amination of carbonyl compounds by ω-transaminase (ω-TA) owing to its cheapness and high volatility of a ketone product. Here we developed asymmetric synthesis of unnatural amino acids via ω-TA-catalyzed amino group transfer between α-keto acids and isopropylamine.
Kinetic resolution of 3-fluoroalanine using a fusion protein of D-amino acid oxidase with Vitroscilla hemoglobin
Seo, Young-Man,Khang, Yong-Ho,Yun, Hyungdon
body text, p. 820 - 822 (2011/11/30)
In this study, a fusion protein (VHb-DAAO) of D-amino acid oxidase (DAAO) with Vitreoscilla hemoglobin (VHb) was functionally expressed in Escherichia coli and purified. The kcat value VHb-DAAO (47.1 s-1) towards rac-3-flouroalanine was about 2-fold higher than that of DAAO (21.9 s -1). rac-3-Flouroalanine (500 mm) was kinetically resolved into (R)-3-fluoroalanine with high enatiomeric excess (>99%) by VHb-DAAO with about 52% conversion.