Biocatalytic synthesis of lactones and lactams

Hollmann, Frank; Kara, Selin; Opperman, Diederik J.; Wang, Yonghua

doi:10.1002/asia.201801180

Cited by 38 publications

(20 citation statements)

References 96 publications

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“…Enzymatic synthesis of lactones as polyester building blocks gained great interest as an environmentally sustainable alternative to current chemical methods. The most common biocatalysts to produce lactones are Baeyer–Villiger monooxygenases (BVMOs) and alcohol dehydrogenases (ADHs) . These two classes of enzymes require cofactor NAD(P)H regeneration, making these strategies less suitable for commercial applications.…”

Section: Results Of Aox*‐catalyzed Conversions Of Diols and Other Alcmentioning

confidence: 99%

Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase

2020

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Flavoprotein oxidases can catalyze oxidations of alcohols and amines by merely using molecular oxygen as the oxidant, making this class of enzymes appealing for biocatalysis. The FAD‐containing (FAD=flavin adenine dinucleotide) alcohol oxidase from P. chrysosporium facilitated double and triple oxidations for a range of aliphatic diols. Interestingly, depending on the diol substrate, these reactions result in formation of either lactones or hydroxy acids. For example, diethylene glycol could be selectively and fully converted into 2‐(2‐hydroxyethoxy)acetic acid. Such a facile cofactor‐independent biocatalytic route towards hydroxy acids opens up new avenues for the preparation of polyester building blocks.

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Section: Results Of Aox*‐catalyzed Conversions Of Diols and Other Alcmentioning

confidence: 99%

Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase

2020

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“…[135b] w-Hydroxy acids and lactones were also produced by oxidation of diols with ADH or alcohol oxidase. [136] Besides oxidation from alcohols,a cids can also be produced by biocatalytic oxidation of easily available hydrocarbons.T he Park group developed the cascade oxidation of the C=Cbond in oleic acid and linoleic acid into the diacids or w-hydroxy acids,y et at ar elatively low concentration. [44,137] TheL ig roup reported the whole-cell cascade oxidation of styrene to (S)-mandelic acid, (S)-or (R)-phenylglycine,a nd phenylacetic acid in up to 140 mm ( % 20 gL À1 ).…”

Section: Acid Production Via Hydrolysis Of Esters/amidesmentioning

confidence: 99%

Biocatalysis: Enzymatic Synthesis for Industrial Applications

et al. 2020

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in 2007, followed by postdoctoral studies at York University (UK) and Greifswald University (Germany). In 2010, she transitionedto industry applying and developing biocatalytic technologies at Novacta in the UK, prior to joining Chemical Process Development at GSK, with responsibility for the development and implementation of new biocatalytic technologyi nboth pre-and post-commercialization routes. Since Dec. 2016, Radka is leading the Bioreactions group in GDC at the Novartis Institute for Biomedical Research in Basel, Switzerland. Jeffrey Moore obtained his PhD in Chemical Engineeringf rom the California Institute of Technology in 1996 as Frances Arnold's first Directed Evolution graduate student. His foundational work led to an evolved p-nitrobenzyl esterase and the Lonza Centenary Prize (1997). In 1996, he joined the Biocatalysis Group of Merck & Co.in Rahway NJ, spending two decades inventing new enzymes and new enzymatic processes. In 2018, he transitionedtothe Merck Protein EngineeringG roup responsible for evolving enzymes for the discovery,d evelopmenta nd commercials cale manufacture of medicines. He has been awarded aUS Presidential Green Chemistry Award (2010), the BioCat2012 Award (2012) and the Thomas Edison Inventorship Award (2014). Kai Baldenius studied chemistry in Hamburg and Southampton. He received his PhD for research in asymmetric organometallic catalysis, supervised by H. tom Dieck and H. B. Kagan. After his postdoc on natural product synthesis with K. C. Nicolaou at the Scripps Research Institute he joined BASF in 1993. Kai served BASF in various functions (R&D, production, marketing, sales) before he took the lead of BASF'sbiocatalysis research for almost ad efcade. He left BASF to become afree-lancing consultanti n2019 and in 2020 he has founded Baldenius Biotech Consulting. Uwe T. Bornscheuer studied chemistry and received his PhD in 1993 at Hannover University followed by apostdoc at Nagoya University (Japan). In 1998, he completed his Habilitation at Stuttgart University about the use of lipases and esterasesi n organic synthesis. He has been Professor at the Institute of Biochemistry at Greifswald University since 1999. Beside other awards, he received in 2008 the BioCat2008 Award. He was just recognized as "Chemistry Europe Fellow". His current research interest focuses on the discovery and engineering of enzymes from various classes for applications in organic synthesis, lipid modification, degradation of plastics or complex marine polysaccharides.

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“…However, these substrates are most likely not the natural substrates of CYP116B46, since uncoupling with decanoic acid was 11.5 % and the total turnover numbers (TTNs) were 242 with decanoic acid and 27 with dodecanoic acid. Terminal hydroxylation is the main focus of reports on n ‐alkane and fatty alcohol hydroxylation, with very few reports on the latter, despite the potential that not only diterminal diols but also internal alkane diols hold for the synthesis of polymers and even lactones and lactams . Recently, Sakai et al.…”

Section: Methodsmentioning

confidence: 99%

“…Terminal hydroxylation is the main focus of reports on n-alkane and fatty alcohol hydroxylation, with very few reports on the latter, [5,6] despite the potential that not only diterminal diols but also internal alkane diols hold for the synthesis of polymers [5] and even lactones and lactams. [7] Recently, Sakai et al reported that CYP505D6, a self-sufficient P450 from the white-rot fungus Phanerochaete chrysosporium, preferably hydroxylates 1-dodecanol and dodecanoic acid at the sub-terminal positions (w-1 to w-3), but also yielded the in-chain hydroxylated products (w-4 to w-7) as minor products. [8] However, to date, no catalysts have been described for the regioselective in-chain oxyfunctionalization of n-alkanes, where no directing functional group is available.…”

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confidence: 99%

CYP505E3: A Novel Self‐Sufficient ω‐7 In‐Chain Hydroxylase

et al. 2020

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The self‐sufficient cytochrome P450 monooxygenase CYP505E3 from Aspergillus terreus catalyzes the regioselective in‐chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the ω‐7 position. It is the first reported P450 to give regioselective in‐chain ω‐7 hydroxylation of C10–C16 n‐alkanes, thereby enabling the one step biocatalytic synthesis of rare alcohols such as 5‐dodecanol and 7‐tetradecanol. It shows more than 70 % regioselectivity for the eighth carbon from one methyl terminus, and displays remarkably high activity towards decane (TTN≈8000) and dodecane (TTN≈2000). CYP505E3 can be used to synthesize the high‐value flavour compound δ‐dodecalactone via two routes: 1) conversion of dodecanoic acid into 5‐hydroxydodecanoic acid (24 % regioselectivity), which at low pH lactonises to δ‐dodecalactone, and 2) conversion of 1‐dodecanol into 1,5‐dodecanediol (55 % regioselectivity), which can be converted into δ‐dodecalactone by horse liver alcohol dehydrogenase.

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Biocatalytic synthesis of lactones and lactams

Cited by 38 publications

References 96 publications

Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase

Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase

Biocatalysis: Enzymatic Synthesis for Industrial Applications

CYP505E3: A Novel Self‐Sufficient ω‐7 In‐Chain Hydroxylase

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