Premium
Cover Picture: Bubble Column Enables Higher Reaction Rate for Deracemization of ( R,S )‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System (Adv. Synth. Catal. 11/2019)
Author(s) -
Dias Gomes Mafalda,
Bommarius Bettina R.,
Anderson Shelby R.,
Feske Brent D.,
Woodley John M.,
Bommarius Andreas S.
Publication year - 2019
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201900637
Subject(s) - chemistry , alcohol dehydrogenase , oxygen , alcohol oxidase , immobilized enzyme , alcohol , enzyme , chromatography , stereochemistry , organic chemistry , biochemistry , pichia pastoris , gene , recombinant dna
The inside cover picture , provided by Andreas Bommarius, John Woodley, and co‐workers, illustrates how oxygen transfer into an enzyme‐containing solution and enzyme stability are often at odds with each other. A vigorously sparged and stirred tank is best for oxygen transfer but worst for enzyme stability, while a quiescent solution shows the opposite behavior: best for stability but worst for transfer of molecular oxygen. A bubble column, the focus of the work described in this contribution, allows good oxygen transfer but mostly preserves enzyme stability. Details can be found in the full paper on pages 2574–2581 (M. Dias Gomes, B. R. Bommarius, S. R. Anderson, B. D. Feske, J. M. Woodley, A. S. Bommarius, Adv. Synth. Catal . 2019 , 361 , 2574–2581; DOI: 10.1002/adsc.201900213).