Efficient enzymatic kinetic resolution of 2-heptylamine with a highly active acyl donor

2010 ◽  
Vol 11 (11) ◽  
pp. 987-991 ◽  
Author(s):  
Jian-Hua Sun ◽  
Rong-Ji Dai ◽  
Wei-Wei Meng ◽  
Yu-lin Deng
Keyword(s):  
Kinetic Resolution ◽  
Acyl Donor ◽  
Highly Active ◽  
Enzymatic Kinetic Resolution

scholarly journals Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase of Aspergillus nidulans

2013 ◽  
Vol 2013 ◽  
pp. 1-11 ◽  
Author(s):  
Carolina Peña-Montes ◽  
María Elena Mondragón-Tintor ◽  
José Augusto Castro-Rodríguez ◽  
Ismael Bustos-Jaimes ◽  
Arturo Navarro-Ocaña ◽  
...  
Keyword(s):  
Kinetic Resolution ◽  
Storage Stability ◽  
Enantiomeric Excess ◽  
Residual Activity ◽  
Biochemical Properties ◽  
Maximum Activity ◽  
Acyl Donor ◽  
Initial Activity ◽  
Enzymatic Kinetic Resolution ◽  
Repeated Use

The recombinant NStcI A. nidulans esterase was adsorbed on Accurel MP1000, where protein yield and immobilization efficiency were 42.48% and 81.94%, respectively. Storage stability test at 4°C and RT showed 100% of residual activity after 40 days at both temperatures. The biocatalyst retains more than 70% of its initial activity after 3 cycles of repeated use. Biochemical properties of this new biocatalyst were obtained. Maximum activity was achieved at pH 11 and 30°C, while the best stability was observed with the pH between 9 and 11 at 40°C. NStcI thermostability was increased after immobilization, as it retained 47.5% of its initial activity after 1 h at 60°C, while the free enzyme under the same conditions displayed no activity. NStcI preserved 70% of its initial activity in 100% hexane after 72 h. Enzymatic kinetic resolution of (R,S)-1-phenylethanol was chosen as model reaction, using vinyl acetate as acyl donor. After optimization of reaction parameters, the highest possible conversion (42%) was reached at 37°C, aw of 0.07, and 120 h of bioconversion in hexane with an enantiomeric excess of 71.7%. NStcI has selectivity for (R)-enantiomer. The obtained E value (31.3) is in the range considered useful to resolve enantiomeric mixtures.

scholarly journals Preparation of (R)-1-(2-Naphthyl)ethylamine by Enzymatic Kinetic Resolution with A New Acyl Donor

2012 ◽  
Vol 32 (03) ◽  
pp. 526 ◽  
Author(s):  
Simin Fu ◽  
Gang Xu ◽  
Yongjun Chen ◽  
Jianping Wu ◽  
Lirong Yang
Keyword(s):  
Kinetic Resolution ◽  
Acyl Donor ◽  
Enzymatic Kinetic Resolution

Enzymatic kinetic resolution of Morita-Baylis-Hillman acetates

2017 ◽  
Vol 28 (9) ◽  
pp. 1169-1174 ◽  
Author(s):  
Wanyama P. Juma ◽  
Varsha Chhiba ◽  
Dean Brady ◽  
Moira L. Bode
Keyword(s):  
Kinetic Resolution ◽  
Enzymatic Kinetic Resolution
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