Literature DB >> 20434391

Asymmetric biocatalysis with microbial enzymes and cells.

Roland Wohlgemuth1.   

Abstract

Microbial enzymes and cells continue to be important tools and nature's privileged chiral catalysts for performing asymmetric biocatalysis from the analytical small scale to the preparative and large scale in synthesis and degradation. The application of biocatalysts for preparing molecular asymmetry has achieved high efficiency, enantioselectivity and yield and is experiencing today a worldwide renaissance. Recent developments in the discovery, development and production of stable biocatalysts, in the design of new biocatalytic processes and in the product recovery and purification processes have made biocatalytic approaches using microbial cells and enzymes attractive choices for the synthesis of chiral compounds. The methodologies of kinetic resolution and kinetic asymmetric transformation, dynamic kinetic resolution and deracemization, desymmetrization, asymmetric synthesis with or without diastereo control and multi-step asymmetric biocatalysis are finding increasing applications in research. The ever-increasing use of hydrolytic enzymes has been accompanied by new applications of oxidoreductases, transferases and lyases. Isomerases, already used in large-scale processes, and ligases, are emerging as interesting biocatalysts for new synthetic applications. The production of a wide variety of industrial products by asymmetric biocatalysis has even become the preferred method of production. Copyright 2010 Elsevier Ltd. All rights reserved.

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Year:  2010        PMID: 20434391     DOI: 10.1016/j.mib.2010.04.001

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  9 in total

1.  Directed evolution of Anabaena variabilis phenylalanine ammonia-lyase (PAL) identifies mutants with enhanced activities.

Authors:  Zachary Js Mays; Karishma Mohan; Vikas D Trivedi; Todd C Chappell; Nikhil U Nair
Journal:  Chem Commun (Camb)       Date:  2020-04-09       Impact factor: 6.222

2.  Isolation and initial characterization of a novel type of Baeyer-Villiger monooxygenase activity from a marine microorganism.

Authors:  Andrew Willetts; Ian Joint; Jack A Gilbert; William Trimble; Martin Mühling
Journal:  Microb Biotechnol       Date:  2012-03-13       Impact factor: 5.813

3.  Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1.

Authors:  Longbao Zhu; Li Zhou; Wenjing Cui; Zhongmei Liu; Zhemin Zhou
Journal:  Biotechnol Rep (Amst)       Date:  2014-06-06

4.  A simple protocol for determination of enantiopurity of amines using BINOL derivatives as chiral solvating agents via 1H- and 19F-NMR spectroscopic analysis.

Authors:  Pooja Chaudhary; Geeta Devi Yadav; Surendra Singh
Journal:  RSC Adv       Date:  2022-09-08       Impact factor: 4.036

5.  Application of lipase bearing dead mycelia as biocatalyst for octyl-octanoate synthesis.

Authors:  Ayoub Rashid; Muhammad Mushtaq; Quratulain Syed; Nergis Naz; Ahmad Adnan
Journal:  Food Sci Biotechnol       Date:  2018-06-08       Impact factor: 2.391

Review 6.  Microbial enzymes: tools for biotechnological processes.

Authors:  Jose L Adrio; Arnold L Demain
Journal:  Biomolecules       Date:  2014-01-16

7.  In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer-Villiger monooxygenase.

Authors:  Nikolin Oberleitner; Christin Peters; Florian Rudroff; Uwe T Bornscheuer; Marko D Mihovilovic
Journal:  J Biotechnol       Date:  2014-04-16       Impact factor: 3.307

8.  Enzymatic synthesis of chiral amino-alcohols by coupling transketolase and transaminase-catalyzed reactions in a cascading continuous-flow microreactor system.

Authors:  Pia Gruber; Filipe Carvalho; Marco P C Marques; Brian O'Sullivan; Fabiana Subrizi; Dragana Dobrijevic; John Ward; Helen C Hailes; Pedro Fernandes; Roland Wohlgemuth; Frank Baganz; Nicolas Szita
Journal:  Biotechnol Bioeng       Date:  2017-11-09       Impact factor: 4.530

9.  Self-sufficient asymmetric reduction of β-ketoesters catalysed by a novel and robust thermophilic alcohol dehydrogenase co-immobilised with NADH.

Authors:  Alejandro H Orrego; Daniel Andrés-Sanz; Susana Velasco-Lozano; Mercedes Sanchez-Costa; José Berenguer; José M Guisan; Javier Rocha-Martin; Fernando López-Gallego
Journal:  Catal Sci Technol       Date:  2021-03-12       Impact factor: 6.119

  9 in total

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