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Asymmetric And Selective Biocatalysis Cesar Mateo Palomo

  • SKU: BELL-54701144
Asymmetric And Selective Biocatalysis Cesar Mateo Palomo
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Asymmetric And Selective Biocatalysis Cesar Mateo Palomo instant download after payment.

Publisher: MDPI
File Extension: PDF
File size: 13.12 MB
Pages: 154
Author: Cesar Mateo, Palomo
ISBN: 9783038978473, 3038978477
Language: English
Year: 2019

Product desciption

Asymmetric And Selective Biocatalysis Cesar Mateo Palomo by Cesar Mateo, Palomo 9783038978473, 3038978477 instant download after payment.

This Issue contains one communication, six articles, and two reviews. The communication from Paola Vitale and others represents a work where whole cells were used as biocatalysts for the reduction of optically active chloroalkyl arylketones followed by a chemical cyclization to give the desired heterocycles. Among the various whole cells screened (baker's yeast, Kluyveromyces marxianus CBS 6556, Saccharomyces cerevisiae CBS 7336, Lactobacillus reuteri DSM 20016), baker's yeast provided the best yields and the highest enantiomeric ratios (95:5) in the bioreduction of the above ketones. In this respect, valuable chiral non-racemic functionalized oxygen-containing heterocycles (e.g., (S)-styrene oxide, (S)-2-phenyloxetane, (S)-2-phenyltetrahydrofuran), amenable to be further elaborated on, can be smoothly and successfully generated from their prochiral precursors. Studies about pure biocatalysts with mechanistical studies, application in different reactions, and new immobilization methods for improving their stability were reported in five different articles. The article by Su-Yan Wang and others describes the cloning, expression, purification, and characterization of an N-acetylglucosamine 2-epimerase from Pedobacter heparinus (PhGn2E). For this, several N-acylated glucosamine derivatives were chemically synthesized and used to test the substrate specificity of the enzyme. The mechanism of the enzyme was studied by hydrogen/deuterium NMR. The study at the anomeric hydroxyl group and C-2 position of the substrate in the reaction mixture confirmed the epimerization reaction via ring-opening/enolate formation. Site-directed mutagenesis was also used to confirm the proposed mechanism of this interesting enzyme.

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