71-00-1Relevant articles and documents
An unprecedented trans-oriented product from the cleavage of a dipeptide.
Saha, Manas K,Bernal, Ivan
, p. 612 - 613 (2003)
An unusual trans cleavage reaction was observed when trans-[Co(3,2,3-tet)Cl2]Cl (3,2,3-tet = N,N'-bis(3-aminopropyl)ethylenediamine), was allowed to react with beta-alanyl-L-histidine (a bioactive dipeptide) in an aqueous medium at pH approximately 7.5 and 45 degrees C for 6 h.
Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity
De Cesare, Silvia,McKenna, Catherine A.,Mulholland, Nicholas,Murray, Lorna,Bella, Juraj,Campopiano, Dominic J.
supporting information, p. 4904 - 4909 (2021/06/16)
Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.
Safe and Effective Method of Treating Ulcerative Colitis with Anti-IL12/IL23 Antibody
-
, (2020/04/10)
Described are methods and compositions for clinical proven safe and effective treatment of ulcerative colitis, particularly moderately to severely active ulcerative colitis in patients who have had an inadequate response to or are intolerant of a conventional or existing therapy by intravenous and/or subcutaneous administration of an anti-IL-12/IL-23p40 antibody.
A green-by-design bioprocess for l-carnosine production integrating enzymatic synthesis with membrane separation
Yin, Dong-Ya,Pan, Jiang,Zhu, Jie,Liu, You-Yan,Xu, Jian-He
, p. 5971 - 5978 (2019/11/14)
l-Carnosine (l-Car, β-alanyl-l-histidine) is a bioactive dipeptide with important physiological functions. Direct coupling of unprotected β-Ala (β-alanine) with l-His (l-histidine) mediated by an enzyme is a promising method for l-Car synthesis. In this study, a new recombinant dipeptidase (SmPepD) from Serratia marcescens with a high synthetic activity toward l-Car was identified by a genome mining approach and successfully expressed in Escherichia coli. Divalent metal ions strongly promoted the synthetic activity of SmPepD, with up to 21.7-fold increase of activity in the presence of 0.1 mM MnCl2. Higher temperature, lower pH and increasing substrate loadings facilitated the l-Car synthesis. Pilot biocatalytic syntheses of l-Car were performed comparatively in batch and continuous modes. In the continuous process, an ultra-filtration membrane reactor with a working volume of 5 L was employed for catalyst retention. The dipeptidase, SmPepD, showed excellent operational stability without a significant decrease in space-time yield after 4 days. The specific yield of l-Car achieved was 105 gCar gcatalyst-1 by the continuous process and 30.1 gCar gcatalyst-1 by the batch process. A nanofiltration membrane was used to isolate the desired product l-Car from the reaction mixture by selectively removing the excess substrates, β-Ala and l-His. As a result, the final l-Car content was effectively enriched from 2.3% to above 95%, which gave l-Car in 99% purity after ethanol precipitation with a total yield of 60.2%. The recovered substrate mixture of β-Ala and l-His can be easily reused, which will enable the economically attractive and environmentally benign production of the dipeptide l-Car.