Enzyme-Catalyzed Enantioselective Hydrolysis of Dihydrouracils as a Route to Enantiomerically Pure β-Amino Acids

ACS Catalysis ◽  
2011 ◽  
Vol 1 (9) ◽  
pp. 1014-1016 ◽  
Author(s):  
Maeve O’Neill ◽  
Bernhard Hauer ◽  
Nina Schneider ◽  
Nicholas J. Turner
Keyword(s):  
Amino Acids ◽  
Enantioselective Hydrolysis ◽  
Enantiomerically Pure ◽  
Hydrolysis Of

Resolution of non-protein amino acids via the enantioselective hydrolysis of their esters mediated by sulfhydryl proteases

1994 ◽  
Vol 16 (4) ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Hitoshi Iwanaga ◽  
Takashi Yamada ◽  
Shigeru Kuwata
Keyword(s):  
Amino Acids ◽  
Enantioselective Hydrolysis ◽  
Protein Amino Acids ◽  
Hydrolysis Of

Asymmetric Synthesis of Enantiomerically Enriched a-Amino Acids Containing 2-Furyl- and 2-Thienyl-1,2,4-triazoles in the Side-Chain

2014 ◽  
Vol 69 (4) ◽  
pp. 451-460 ◽  
Author(s):  
Ashot S. Saghyan ◽  
Hayarpi M. Simonyan ◽  
Satenik G. Petrosyan ◽  
Anna F. Mkrtchyan ◽  
Lilit V. Khachatryan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Schiff Base ◽  
Asymmetric Synthesis ◽  
Efficient Method ◽  
Enantiomeric Excess ◽  
Side Chain ◽  
Chiral Auxiliaries ◽  
Enantiomerically Pure ◽  
Dehydroamino Acids ◽  
Hydrolysis Of

An efficient method for the asymmetric synthesis of a-amino acids, containing furyl- and thiophenyl-substituted triazoles in their side-chain, is reported. The strategy relies on Michael addition of 3,4,5-substituted 1,2,4-triazoles to the C=C bond of chiral NiII complexes containing the Schiff base formed from dehydroamino acids (dehydroalanine and (E + Z)-dehydroaminobutyric acid) and from chiral auxiliaries, i. e. (S)-2-N-(N0-benzylprolyl)aminobenzophenone and (S)-2-N- (N0-2-chlorobenzylprolyl) aminobenzophenone. The reactions proceeded with good to very good diastereoselectivity. Hydrolysis of the diastereomeric mixtures of metal complexes afforded the enantiomerically pure a-amino acids with high enantiomeric excess (ee> 98%).

Kinetic resolution of unnatural and rarely occurring amino acids: enantioselective hydrolysis of N-acyl amino acids catalyzed by acylase I

1989 ◽  
Vol 111 (16) ◽  
pp. 6354-6364 ◽  
Author(s):  
H. Keith Chenault ◽  
Juergen Dahmer ◽  
George M. Whitesides
Keyword(s):  
Amino Acids ◽  
Kinetic Resolution ◽  
Enantioselective Hydrolysis ◽  
Acylase I ◽  
Hydrolysis Of

Porcine Pancreatic Lipase Catalyzed Enantioselective Hydrolysis of Esters ofN-Protected Unusual Amino Acids

1989 ◽  
Vol 18 (12) ◽  
pp. 2219-2222 ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Hitoshi Iwanaga ◽  
Shinichi Ueji ◽  
Takashi Yamada ◽  
Shigeru Kuwata
Keyword(s):  
Amino Acids ◽  
Pancreatic Lipase ◽  
Enantioselective Hydrolysis ◽  
Porcine Pancreatic Lipase ◽  
Unusual Amino Acids ◽  
Hydrolysis Of Esters ◽  
Hydrolysis Of

Resolution of non-protein amino acids via the microbial protease-catalyzed enantioselective hydrolysis of their N-unprotected esters

Tetrahedron ◽  
2005 ◽  
Vol 61 (43) ◽  
pp. 10254-10261 ◽  
Author(s):  
Toshifumi Miyazawa ◽  
Kiwamu Imagawa ◽  
Hiroe Minowa ◽  
Toyoko Miyamoto ◽  
Takashi Yamada
Keyword(s):  
Amino Acids ◽  
Enantioselective Hydrolysis ◽  
Microbial Protease ◽  
Protein Amino Acids ◽  
Hydrolysis Of

1,3-Diastereocontrol with bromoallenes. Synthesis of enantiomerically pure β-branched α-amino acids

1994 ◽  
Vol 35 (41) ◽  
pp. 7775-7778 ◽  
Author(s):  
F D'Aniello
Keyword(s):  
Amino Acids ◽  
Enantiomerically Pure

Deinking of recycled paper by coupling of the enzyme endo-β-1,4-D-glucanasa and the cellulose, and by using a laboratory flotation column

MRS Advances ◽  
2020 ◽  
Vol 5 (52-53) ◽  
pp. 2669-2678
Author(s):  
Jeovani González P. ◽  
Ramiro Escudero G
Keyword(s):  
Amino Acids ◽  
Sodium Hydroxide ◽  
Paper Industry ◽  
Computational Simulation ◽  
Cellulose Fibers ◽  
Residual Water ◽  
Chemical Reagent ◽  
Recycled Paper ◽  
Flotation Column ◽  
Hydrolysis Of

AbstractDeinking of recycled office (MOW) paper was carried out by using a flotation column and adding separately sodium hydroxide, and the enzyme Cellulase Thricodema Sp., as defibrillators.The de-inked cellulose fibers were characterized according to the standards of the paper industry, to compare the efficiency of the deinking of each chemical reagent used to hydrolyze the fibers and defibrillate them.The computational simulation of the molecular coupling between the enzyme and cellulose was performed, to establish the enzyme-cellulose molecular complex and then to identify the principal amino-acids of endo-β-1,4-D-glucanase in this molecular link, which are responsible for the hydrolysis of the cellulose.Experimental results show the feasibility to replace sodium hydroxide with the enzyme Cellulase Thricodema Sp., by obtaining deinked cellulose with similar optical and physical properties.The use of the enzyme instead of sodium hydroxide avoids the contamination of the residual water; in addition to that, the column is operated more easily, taking into consideration that the pH of the system goes from alkaline to neutral.

Enzymological Characteristics of Catalytic Antibody-catalyzed Enantioselective Hydrolysis of Ibuprofen Ester in Water-in-oil Microemulsion*

2009 ◽  
Vol 2009 (2) ◽  
pp. 182-189
Author(s):  
Gen-Sheng YANG ◽  
Ying-Dan QI ◽  
Zhi-Min OU ◽  
Shan-Jing YAO
Keyword(s):  
Catalytic Antibody ◽  
Enantioselective Hydrolysis ◽  
Hydrolysis Of

Studies on Chromatographic Fractioning by Cations Exchangers of a Bovine Hemoglobin Hydrolysate

2018 ◽  
Vol 69 (10) ◽  
pp. 2794-2798
Author(s):  
Alina Diana Panainte ◽  
Ionela Daniela Morariu ◽  
Nela Bibire ◽  
Madalina Vieriu ◽  
Gladiola Tantaru ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Retention Time ◽  
Chromatographic Separation ◽  
Bovine Hemoglobin ◽  
Reverse Phase ◽  
Hplc System ◽  
Fast Flow ◽  
Hydrolysis Of ◽  
Phase Column

A peptidic hydrolysate has been obtained through hydrolysis of bovine hemoglobin using pepsin. The fractioning of the hydrolysate was performed on a column packed with CM-Sepharose Fast Flow. The hydrolysate and each fraction was filtered and then injected into a HPLC system equipped with a Vydak C4 reverse phase column (0.46 x 25 cm), suitable for the chromatographic separation of large peptides with 20 to 30 amino acids. The detection was done using mass spectrometry, and the retention time, size and distribution of the peptides were determined.

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