111611-91-7Relevant academic research and scientific papers
Facile Synthesis of α-Hydroxycarboxylic Acids by Ruthenium-Catalyzed Reduction od Diaalyl α-Oxalylcarboxylates with Formic Acid
Shimizu, Isao,Tekawa, Masafumi,Maruyama, Yooichiroh,Yamamoto, Akio
, p. 1365 - 1366 (1992)
Reaction of diallyl α-oxalylcarboxylates with catalytic amounts of ruthenium complexes gave α-hydroxycarboxylic acids in good yields.
Biocatalytic racemisation of α-hydroxycarboxylic acids at physiological conditions
Glueck, Silvia M.,Larissegger-Schnell, Barbara,Csar, Katrin,Kroutil, Wolfgang,Faber, Kurt
, p. 1904 - 1905 (2005)
Biocatalytic racemisation of aliphatic, aryl-aliphatic and aromatic α-hydroxycarboxylic acids was accomplished using whole resting cells of Lactobacillus paracasei DSM 20207; the mild (physiological) reaction conditions ensured an essentially 'clean' isomerization in the absence of side reactions, such as elimination or decomposition. The Royal Society of Chemistry 2005.
Improving enantioselectivity of lipase from Candida rugosa by carrier-bound and carrier-free immobilization
Velasco-Lozano, Susana,López-Gallego, Fernando,Rocha-Martin, Javier,Guisán, José Manuel,Favela-Torres, Ernesto
, p. 32 - 39 (2016)
The enantioselectivity of carrier-bound and carrier-free immobilized lipase from Candida rugosa (CRL) was studied. CRL was immobilized in six agarose-based carriers functionalized with different reactive groups and in two different CRL cross-linked aggregates. Both, activity and enantioselectivity of all the immobilized lipase preparations were evaluated with different racemic esters under different reaction conditions (temperature, pH and solvent polarity). A strong effect of reaction media and immobilization protocol on enzyme activity and selectivity was found. Enzyme immobilization and reaction engineering allowed us obtaining the best immobilization protocol and reaction conditions to achieve high activity and enantioselectivty of CRL as heterogeneous catalyst. CRL immobilized on an agarose-based carrier activated with primary amino groups preferentially hydrolyzed (S)-phenylethyl acetate with E > 200 under pH 7, 4 °C and 30% of acetonitrile. On the other hand, CRL aggregated and cross-linked through their carboxylic groups preferentially hydrolyzed the (S)-isomer of ethyl 2-hydroxy-4-phenylbutyrate with an E = 39 under pH 5, 4 °C and 30% of acetonitrile. This work demonstrates the success of the combinatorial enzyme engineering for the production of highly enantioselective heterogeneous biocatalysts by screening different immobilization protocols and reaction media conditions.
Chirality switching in the enantioseparation of 2-hydroxy-4-phenylbutyric acid: Role of solvents in selective crystallization of the diastereomeric salt
Hirose, Takuji,Kodama, Koichi,Shitara, Hiroaki,Yi, Meng
, (2020)
Chirality switching was induced by solvents in the enantioseparation of 2-hydroxy-4-phenylbutyric acid (HPBA) via diastereomeric salt formation with an enantiopure aminoalcohol. The (S)-salt was crystallized from butanol solutions and the (R)-salt was obt
Enantio-complementary deracemization of (±)-2-hydroxy-4- phenylbutanoic acid and (±)-3-phenyllactic acid using lipase-catalyzed kinetic resolution combined with biocatalytic racemization
Larissegger-Schnell, Barbara,Glueck, Silvia M.,Kroutil, Wolfgang,Faber, Kurt
, p. 2912 - 2916 (2006)
Deracemization of (±)-3-phenyllactic acid (1) and (±)-2-hydroxy-4-phenylbutanoic acid (2) was accomplished by lipase-catalysed kinetic resolution coupled to biocatalytic racemization of the non-reacting substrate enantiomers using Lactobacillus paracasei DSM 20008. Cyclic repetition of this sequence led to a single enantiomeric product from the racemate. Access to both enantiomers was achieved by switching between lipase-catalysed acyl-transfer and ester hydrolysis reactions. Both products constitute important building blocks for virus protease- and ACE-inhibitors, respectively.
A Novel Highly Diastereoselective Synthesis of Cyano Esters by Regioselective Ring Opening of Chiral Oxazolidinium Methiodides with Sodium Cyanide
Andres, Celia,Delgado, Manuel,Pedrosa, Rafael,Rodriquez, Raquel
, p. 8325 - 8328 (1993)
Sodium cyanide reacts with chiral oxazolidinium methiodides, prepared by quaternization of oxazolidines with methyl iodide, leading regio- and stereoselectively (d.e. 82-94percent) to cyano esters in moderate to good chemical yields (51-95percent).The open compounds are isolated as a pure diastereomer by a single recrystallization of their ammonium methiodides, and converted into enantiomerically pure α-hydroxy acids by heating with a concentrated solution of hydrochloric acid. - Key words: Chiral Oxazolidinium Iodides; alpha-Cyano ethers, Diastereoselective Ring Opening; alpha-Hydroxy Acids; Asymmetric Synthesis.
Efficient Synthesis of D-Phenylalanine from L-Phenylalanine via a Tri-Enzymatic Cascade Pathway
Lu, Cui,Zhang, Sheng,Song, Wei,Liu, Jia,Chen, Xiulai,Liu, Liming,Wu, Jing
, p. 3165 - 3173 (2021)
D-phenylalanine is an important intermediate in food and pharmaceutical industries. Here, to enable efficient D-phenylalanine biosynthesis from L-phenylalanine, a tri-enzymatic cascade was designed and reconstructed in vivo. The activity of Proteus vulgaris meso-diaminopimelate dehydrogenase (PvDAPDH) toward phenyl pyruvic acid was identified as the limiting step. To overcome, the tension in the phenyl pyruvic acid side-chain, PvDAPDH was engineered, generating PvDAPDHW121A/R181S/H227I, whose catalytic activity of 6.86 U mg?1 represented an 85-fold increase over PvDAPDH. Introduction of PvDAPDHW121A/R181S/H227I, P. mirabilis L-amino acid deaminase, and Bacillus megaterium glucose dehydrogenase in E. coli enabled the production of 57.8 g L?1 D-phenylalanine in 30 h, the highest titer to date using 60 g L?1 L-phenylalanine as starting substrate, which meant a 96.3 % conversion rate and >99 % enantioselectivity on a 3-L scale. The proposed tri-enzymatic cascade provides a novel potential bio-based approach for industrial production of D-phenylalanine from cheap amino acids.
Evaluation of the lipase from Bacillus thermocatenulatus as an enantioselective biocatalyst
Palomo, Jose M.,Fernandez-Lorente, Gloria,Rua, Maria L.,Guisan, Jose M.,Fernandez-Lafuente, Roberto
, p. 3679 - 3687 (2003)
The lipase from Bacillus thermocatenulatus (BTL2) has been immobilized using different techniques, and used in the resolution of different chiral substrates in hydrolytic reactions. This enzyme acts as an interesting biocatalyst for these types of reactio
Two-enzyme coexpressed recombinant strain for asymmetric synthesis of ethyl (R)-2-hydroxy-4-phenylbutyrate
Su, Yuning,Ni, Ye,Wang, Junchao,Xu, Zhihao,Sun, Zhihao
, p. 1650 - 1660 (2012)
(R)-2-Hydroxy-4-phenylbutyrate (HPBE) is an important chiral intermediate for the synthesis of angiotensin-converting enzyme (ACE) inhibitors. Asymmetric reduction of ethyl 2-oxo-4-phenyl-butyrate (OPBE) to (R)-HPBE using a recombinant strain can provide high enantioselectivity. Cofactor regeneration is a critical issue in the application of a recombinant strain. A carbonyl reductase gene (iolS) and a glucose dehydrogenase (GDH) gene from Bacillus subtilis were cloned. Recombinant IolS was purified using a Ni-NTA column and its enzyme activity properties were investigated. The purified IolS exhibited maximum activity at pH 6.0 and 30°C, and the enzyme showed good thermostability below 40°C. It retained over 75 of its activity in the acidic pH range of 5.5(7.0. Three coexpression strategies were used for the recombinant vectors. The recombinant E. coli strain containing polycistronic plasmid pET-G-T7-I showed excellent carbonyl reductase activity, and the specific activity of both IolS and GDH in the crude cell extract reached 1.5 U/mg. In the asymmetric reduction of OPBE by recombinant E. coli cells in aqueous system, the yield of (R)-HPBE reached over 99 with an enantiomeric excess of 99.5 at 10 g/L of OPBE within 15 h.
One-pot, two-step synthesis of unnatural α-amino acids involving the exhaustive aerobic oxidation of 1,2-diols
Inada, Haruki,Furukawa, Keisuke,Shibuya, Masatoshi,Yamamoto, Yoshihiko
supporting information, p. 15105 - 15108 (2019/12/26)
Herein, we report the nor-AZADO-catalyzed exhaustive aerobic oxidations of 1,2-diols to α-keto acids. Combining oxidation with transamination using dl-2-phenylglycine led to the synthesis of free α-amino acids (AAs) in one pot. This method enables the rapid and flexible preparation of a variety of valuable unnatural AAs, such as fluorescent AAs, photoactivatable AAs, and other functional AAs for bioorthogonal reactions.
