Bubble Column Enables Higher Reaction Rate for Deracemization of (R,S)‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System

Mafalda Dias Gomes, Bettina Bommarius, Shelby Anderson, Brent D. Feske, John Woodley*, Andreas Bommarius

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

ne of the major drawbacks for many biocatalysts is their poor stability under industrial process conditions. A particularly interesting example is the supply of oxygen to biooxidation reactions, catalyzed by oxidases, oxygenases or alcohol dehydrogenases coupled with NAD(P)H (reduced nicotinamide adenine dinucleotide phosphate) oxidases, which all require the continuous supply of molecular oxygen as an oxidant or electron acceptor. Commonly, oxygen is supplied to the bioreactor by air sparging. To ensure sufficient oxygen transfer from the gas to the liquid phase, stirring is essential to disperse the gas bubbles and create high gas‐liquid interfacial area. Studies indicate that the presence of gas‐liquid interface induces enzyme deactivation by protein unfolding which then readily aggregates and can subsequently precipitate. This contribution has examined the effects of stirring and the presence of gas‐liquid interface on the kinetic stability of water‐forming NAD(P)H oxidase (NOX) (EC1.6.3.2). These effects were studied separately and a bubble column apparatus was successfully employed to investigate the influence of gas‐liquid interfaces on enzyme stability. Results showed that NOX deactivation increases in proportion to the gas‐liquid interfacial area. While air enhances the rate of stability loss compared to nitrogen, stirring causes faster loss of activity in comparison to a bubble column. Finally, deracemization of 1‐phenylethanol, using a coupled alcohol dehydrogenase /NADH oxidase system (ADH/NOX), proceeded with a higher rate in the bubble column than in quiescent or in a stirred solution, although, inactivation was also accelerated in the bubble column over a quiescent solution.
Original languageEnglish
JournalAdvanced Synthesis and Catalysis
Volume361
Issue number11
Pages (from-to)2574-2581
Number of pages8
ISSN1615-4150
DOIs
Publication statusPublished - 2019

Keywords

  • Bubble column
  • NADH oxidase
  • Deracemization
  • Gas-liquid interface
  • Biocatalysis

Cite this

Dias Gomes, Mafalda ; Bommarius, Bettina ; Anderson, Shelby ; Feske, Brent D. ; Woodley, John ; Bommarius, Andreas. / Bubble Column Enables Higher Reaction Rate for Deracemization of (R,S)‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System. In: Advanced Synthesis and Catalysis. 2019 ; Vol. 361, No. 11. pp. 2574-2581.
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title = "Bubble Column Enables Higher Reaction Rate for Deracemization of (R,S)‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System",
abstract = "ne of the major drawbacks for many biocatalysts is their poor stability under industrial process conditions. A particularly interesting example is the supply of oxygen to biooxidation reactions, catalyzed by oxidases, oxygenases or alcohol dehydrogenases coupled with NAD(P)H (reduced nicotinamide adenine dinucleotide phosphate) oxidases, which all require the continuous supply of molecular oxygen as an oxidant or electron acceptor. Commonly, oxygen is supplied to the bioreactor by air sparging. To ensure sufficient oxygen transfer from the gas to the liquid phase, stirring is essential to disperse the gas bubbles and create high gas‐liquid interfacial area. Studies indicate that the presence of gas‐liquid interface induces enzyme deactivation by protein unfolding which then readily aggregates and can subsequently precipitate. This contribution has examined the effects of stirring and the presence of gas‐liquid interface on the kinetic stability of water‐forming NAD(P)H oxidase (NOX) (EC1.6.3.2). These effects were studied separately and a bubble column apparatus was successfully employed to investigate the influence of gas‐liquid interfaces on enzyme stability. Results showed that NOX deactivation increases in proportion to the gas‐liquid interfacial area. While air enhances the rate of stability loss compared to nitrogen, stirring causes faster loss of activity in comparison to a bubble column. Finally, deracemization of 1‐phenylethanol, using a coupled alcohol dehydrogenase /NADH oxidase system (ADH/NOX), proceeded with a higher rate in the bubble column than in quiescent or in a stirred solution, although, inactivation was also accelerated in the bubble column over a quiescent solution.",
keywords = "Bubble column, NADH oxidase, Deracemization, Gas-liquid interface, Biocatalysis",
author = "{Dias Gomes}, Mafalda and Bettina Bommarius and Shelby Anderson and Feske, {Brent D.} and John Woodley and Andreas Bommarius",
year = "2019",
doi = "10.1002/adsc.201900213",
language = "English",
volume = "361",
pages = "2574--2581",
journal = "Advanced Synthesis & Catalysis",
issn = "1615-4150",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "11",

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Bubble Column Enables Higher Reaction Rate for Deracemization of (R,S)‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System. / Dias Gomes, Mafalda; Bommarius, Bettina; Anderson, Shelby; Feske, Brent D.; Woodley, John; Bommarius, Andreas.

In: Advanced Synthesis and Catalysis, Vol. 361, No. 11, 2019, p. 2574-2581.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Bubble Column Enables Higher Reaction Rate for Deracemization of (R,S)‐1‐Phenylethanol with Coupled Alcohol Dehydrogenase/NADH Oxidase System

AU - Dias Gomes, Mafalda

AU - Bommarius, Bettina

AU - Anderson, Shelby

AU - Feske, Brent D.

AU - Woodley, John

AU - Bommarius, Andreas

PY - 2019

Y1 - 2019

N2 - ne of the major drawbacks for many biocatalysts is their poor stability under industrial process conditions. A particularly interesting example is the supply of oxygen to biooxidation reactions, catalyzed by oxidases, oxygenases or alcohol dehydrogenases coupled with NAD(P)H (reduced nicotinamide adenine dinucleotide phosphate) oxidases, which all require the continuous supply of molecular oxygen as an oxidant or electron acceptor. Commonly, oxygen is supplied to the bioreactor by air sparging. To ensure sufficient oxygen transfer from the gas to the liquid phase, stirring is essential to disperse the gas bubbles and create high gas‐liquid interfacial area. Studies indicate that the presence of gas‐liquid interface induces enzyme deactivation by protein unfolding which then readily aggregates and can subsequently precipitate. This contribution has examined the effects of stirring and the presence of gas‐liquid interface on the kinetic stability of water‐forming NAD(P)H oxidase (NOX) (EC1.6.3.2). These effects were studied separately and a bubble column apparatus was successfully employed to investigate the influence of gas‐liquid interfaces on enzyme stability. Results showed that NOX deactivation increases in proportion to the gas‐liquid interfacial area. While air enhances the rate of stability loss compared to nitrogen, stirring causes faster loss of activity in comparison to a bubble column. Finally, deracemization of 1‐phenylethanol, using a coupled alcohol dehydrogenase /NADH oxidase system (ADH/NOX), proceeded with a higher rate in the bubble column than in quiescent or in a stirred solution, although, inactivation was also accelerated in the bubble column over a quiescent solution.

AB - ne of the major drawbacks for many biocatalysts is their poor stability under industrial process conditions. A particularly interesting example is the supply of oxygen to biooxidation reactions, catalyzed by oxidases, oxygenases or alcohol dehydrogenases coupled with NAD(P)H (reduced nicotinamide adenine dinucleotide phosphate) oxidases, which all require the continuous supply of molecular oxygen as an oxidant or electron acceptor. Commonly, oxygen is supplied to the bioreactor by air sparging. To ensure sufficient oxygen transfer from the gas to the liquid phase, stirring is essential to disperse the gas bubbles and create high gas‐liquid interfacial area. Studies indicate that the presence of gas‐liquid interface induces enzyme deactivation by protein unfolding which then readily aggregates and can subsequently precipitate. This contribution has examined the effects of stirring and the presence of gas‐liquid interface on the kinetic stability of water‐forming NAD(P)H oxidase (NOX) (EC1.6.3.2). These effects were studied separately and a bubble column apparatus was successfully employed to investigate the influence of gas‐liquid interfaces on enzyme stability. Results showed that NOX deactivation increases in proportion to the gas‐liquid interfacial area. While air enhances the rate of stability loss compared to nitrogen, stirring causes faster loss of activity in comparison to a bubble column. Finally, deracemization of 1‐phenylethanol, using a coupled alcohol dehydrogenase /NADH oxidase system (ADH/NOX), proceeded with a higher rate in the bubble column than in quiescent or in a stirred solution, although, inactivation was also accelerated in the bubble column over a quiescent solution.

KW - Bubble column

KW - NADH oxidase

KW - Deracemization

KW - Gas-liquid interface

KW - Biocatalysis

U2 - 10.1002/adsc.201900213

DO - 10.1002/adsc.201900213

M3 - Journal article

VL - 361

SP - 2574

EP - 2581

JO - Advanced Synthesis & Catalysis

JF - Advanced Synthesis & Catalysis

SN - 1615-4150

IS - 11

ER -