Immobilization of yeast alcohol dehydrogenase on polyaniline coated silver nanoparticles formed by green synthesis

Alam, Md. Fazle; Laskar, Amaj Ahmed; Zubair, Mohd; Baig, Umair; Younus, Hina

doi:10.1016/j.molcatb.2015.06.004

Cited by 35 publications

(18 citation statements)

References 46 publications

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“…[21][22][23] Numerous are the examples in literature about immobilized alcohol dehydrogenases, [24][25][26][27] however, this is the first time that immobilization has been studied on Artemisia annua's ADH. Furthermore, immobilization of ADHaa on different supports was investigated in order to re-use the enzyme in various cycles of reaction.…”

Section: Introductionmentioning

confidence: 99%

“…In this sense, immobilization often results in an increased stability of the catalyst and allows an ease separation of the enzymes from the reactor content. [21][22][23] Numerous are the examples in literature about immobilized alcohol dehydrogenases, [24][25][26][27] however, this is the first time that immobilization has been studied on Artemisia annua's ADH.…”

Section: Introductionmentioning

confidence: 99%

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Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Solé

Brummund²,

Caminal

et al. 2019

ChemCatChem

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The monoterpenoid α-isophorone is sourced from the available and renewable plant dry matter, as well as a waste recovery operation from acetone. This compound, can be hydroxylated to 4-hydroxy-isophorone which is the main precursor for the synthesis of ketoisophorone. On its turn, ketoisophorone is a key intermediate for the production of carotenoids and Vitamin E. Here, the enzymatic oxidation of 4-hydroxy-isophorone to ketoisophorone is demonstrated employing an alcohol dehydrogenase (ADHaa) from Artemisia annua and a NADPH oxidase (NOX), as a cofactor regeneration enzyme. After 24 h of reaction and an initial substrate concentration of 50 mM, 95.7 % yield and a space time yield of 6.52 g L À 1 day À 1 could be obtained. Furthermore, the immobilization of the alcohol dehydrogenase was studied on 17 different supports. An epoxy-functionalized agarose resulted in the highest metrics, 100 � 0% immobilization yield and 58.2 � 3.5 % retained activity. Finally, the immobilized ADHaa was successfully implemented in 4 reaction cycles (96 h operation) presenting a biocatalyst yield of 23.4 g product g À 1 of enzyme. It represents a 2.5-fold increase compared with the reaction with soluble enzymes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Solé

Brummund²,

Caminal

et al. 2019

ChemCatChem

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“…Another study by Li et al describes the highest obtained expressed activity of 65% at pH 7.4 and 30 °C, where ADH was immobilized onto chitosan-coated MNPs 44 . Alam et al investigated ADH immobilization on polyaniline-coated Ag nanoparticles, where the highest expressed activity of immobilized ADH was 73% at pH 8 and 40 °C 91 . Shinde et al studied immobilization of ADH onto polyvinyl alcohol fibrous carriers, where immobilized ADH retained 60% of its original activity 84 .…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, immobilization via covalent binding on crystalline Ni-Co nanoferrites, synthesized via sol-gel auto combustion techniques, was investigated, resulting in 40% expressed activity of immobilized ADH 90 . Immobilization of ADH onto polyaniline-coated silver nanoparticles, where it maintained 73% of the initial activity 91 , was also reported. However, there is a study describing immobilization of ADH onto epoxy-functionalized silica coated MNPs, where expressed activity of 92% was maintained at pH 8 and 30 °C with a 12-h immobilization time 63 , which proves the beneficial advantage of epoxy-functionalized nanoparticles for ADH immobilization.…”

mentioning

confidence: 82%

“…ADH immobilized onto polyaniline-coated Ag nanoparticles and magnetic crystalline Ni-Co nanoferrites gave higher K M values of 205.3 mM and 237 mM, respectively. Moreover, the expressed activity of immobilized ADH was only 70% and 73%, respectively 90,91 . Other immobilization protocols which gave lower K M values used different chitosan-or silica-coated nanoparticles and resulted in 37.77 mM and 31.32 mM, respectively 63,89 .…”

Section: Properties Of Immobilized Adh-cmd-mnps Thermal Stability Ofmentioning

confidence: 95%

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Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Vasić

Knez

Leitgeb

2020

Sci Rep

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A novel method is described for the immobilization of alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae onto carboxymethyl dextran (CMD) coated magnetic nanoparticles (CMD-MNPs) activated with epoxy groups, using epichlorohydrin (EClH). EClH was used as an activating agent to bind ADH molecules on the surface of CMD-MNPs. Optimal immobilization conditions (activating agent concentration, temperature, rotation speed, medium pH, immobilization time and enzyme concentration) were set to obtain the highest expressed activity of the immobilized enzyme. ADH that was immobilized onto epoxy-activated CMD-MNPs (ADH-CMD-MNPs) maintained 90% of the expressed activity. Thermal stability of ADH-CMD-MNPS after 24 h at 20 °C and 40 °C yielded 79% and 80% of initial activity, respectively, while soluble enzyme activity was only 19% at 20 °C and the enzyme was non-active at 40 °C. Expressed activity of ADH-CMD-MNPs after 21 days of storage at 4 °C was 75%. Kinetic parameters (KM, vmax) of soluble and immobilized ADH were determined, resulting in 125 mM and 1.2 µmol/min for soluble ADH, and in 73 mM and 4.7 µmol/min for immobilized ADH.

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Stairway to Stereoisomers: Engineering Short‐ and Medium‐Chain Ketoreductases To Produce Chiral Alcohols

Shanbhag

2023

ChemBioChem

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The short-and medium-chain dehydrogenase/reductase superfamilies are responsible for most chiral alcohol production in laboratories and industries. In nature, they participate in diverse roles such as detoxification, housekeeping, secondary metabolite production, and catalysis of several chemicals with commercial and environmental significance. As a result, they are used in industries to create biopolymers, active pharmaceutical intermediates (APIs), and are also used as components of modular enzymes like polyketide synthases for fabricating bioactive molecules. Consequently, random, semi-rational and rational engineering have helped transform these enzymes into product-oriented efficient catalysts. The rise of newer synthetic chemicals and their enantiopure counterparts has proved challenging, and engineering them has been the subject of numerous studies. However, they are frequently limited to the synthesis of a single chiral alcohol. The study attempts to defragment and describe hotspots of engineering short-and medium-chain dehydrogenases/reductases for the production of chiral synthons.

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Immobilization of yeast alcohol dehydrogenase on polyaniline coated silver nanoparticles formed by green synthesis

Cited by 35 publications

References 46 publications

Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Stairway to Stereoisomers: Engineering Short‐ and Medium‐Chain Ketoreductases To Produce Chiral Alcohols

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