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Dean Brady

Researcher at University of the Witwatersrand

Publications -  78
Citations -  3492

Dean Brady is an academic researcher from University of the Witwatersrand. The author has contributed to research in topics: Nitrile hydratase & Nitrilase. The author has an hindex of 25, co-authored 76 publications receiving 2897 citations. Previous affiliations of Dean Brady include Council of Scientific and Industrial Research & Tshwane University of Technology.

Papers
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Development of fructose-1,6-bisphosphate aldolase enzyme peptide mimics as biocatalysts in direct asymmetric aldol reactions

TL;DR: This study describes the design and synthesis of mimetic peptides modelled on the catalytic active site of the fructose-1,6-bisphosphate aldolase (FBPA) enzyme, which showed catalytic activity and the a Aldol products were obtained in low yields, but excellent enantioselectivity and moderate diastereoselectivities.
Journal ArticleDOI

A green, economical synthesis of β-ketonitriles and trifunctionalized building blocks from esters and lactones.

TL;DR: The acylation of the acetonitrile anion with lactones and esters in ethereal solvents was successfully exploited using inexpensive KOt-Bu to obtain a variety of β-ketonitriles and trifunctionalized building blocks, including useful O-unprotected diols.
Journal ArticleDOI

Laccase-catalysed azide-alkyne cycloadditions: Synthesis of benzothiazole and benzimidazole fused 1,2,3-triazole derivatives by copper containing oxidoreductase enzymes

TL;DR: In this article , a new approach for synthesizing triazole rings through the application of laccases, copper containing oxidoreductase enzymes, was outlined, and a series of benzothiazoles and benzimidazoles-functionalized alkynes were initially synthesized utilizing a biocatalysis laccase-based approach.
Patent

Stabilization of enzymes in an emulsion by cross-linking

TL;DR: In this paper, a process for producing enzymes structures includes providing an emulsion of droplets of a first liquid phase dispersed in a second liquid phase, which is immiscible with the hydrophilic phase, and the enzyme molecules of the respective droplets are crosslinked so that individual enzyme structures, which are stable and in which the enzymes are immobilized with a majority of active sites of the enzymes being orientated either internally or externally, are formed from individual droplets.