Oxidation chemistry using enzymes is approaching maturity and practical applicability in organic synthesis. Oxidoreductases (enzymes catalysing redox reactions) enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non-activated C-H bonds. For many of these reactions, no "classical" chemical counterpart is known. Hence oxidoreductases open up shorter synthesis routes based on a more direct access to the target products. The generally very mild reaction conditions may also reduce the environmental impact of biocatalytic reactions compared to classical counterparts. In this Review, we critically summarise the most important recent developments in the field of biocatalytic oxidation chemistry and identify the most pressing bottlenecks as well as promising solutions.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201800343

Biocatalytic Oxidation Reactions: A Chemist's Perspective

The photoenzymatic decarboxylation of fatty acids to alkanes is proposed as an alternative approach for the synthesis of biodiesel. By using a recently discovered photodecarboxylase from Chlorella variabilis NC64A (CvFAP) we demonstrate the irreversible preparation of alkanes from fatty acids and triglycerides. Several fatty acids and their triglycerides are converted by CvFAP in near-quantitative yield and exclusive selectivity upon illumination with blue light. Very promising turnover numbers of up to 8000 were achieved in this proof-of-concept study.

/pdf/light-driven-enzymatic-decarboxylation-of-fatty-acids-3tu2p3jahk.pdf

Light-Driven Enzymatic Decarboxylation of Fatty Acids.

Since the industrial revolution, the rapid growth and development of global industries have depended largely upon the utilization of coal-derived chemicals, and more recently, the utilization of petroleum-based chemicals. These developments have followed a linear economy model (produce, consume, and dispose). As the world is facing a serious threat from the climate change crisis, a more sustainable solution for manufacturing, i.e., circular economy in which waste from the same or different industries can be used as feedstocks or resources for production offers an attractive industrial/business model. In nature, biological systems, i.e., microorganisms routinely use their enzymes and metabolic pathways to convert organic and inorganic wastes to synthesize biochemicals and energy required for their growth. Therefore, an understanding of how selected enzymes convert biobased feedstocks into special (bio)chemicals serves as an important basis from which to build on for applications in biocatalysis, metabolic engineering, and synthetic biology to enable biobased processes that are greener and cleaner for the environment. This review article highlights the current state of knowledge regarding the enzymatic reactions used in converting biobased wastes (lignocellulosic biomass, sugar, phenolic acid, triglyceride, fatty acid, and glycerol) and greenhouse gases (CO2 and CH4) into value-added products and discusses the current progress made in their metabolic engineering. The commercial aspects and life cycle assessment of products from enzymatic and metabolic engineering are also discussed. Continued development in the field of metabolic engineering would offer diversified solutions which are sustainable and renewable for manufacturing valuable chemicals.

Enzymes, In Vivo Biocatalysis, and Metabolic Engineering for Enabling a Circular Economy and Sustainability.

Recent developments in the use of peroxygenases – Exploring their high potential in selective oxyfunctionalisations

Abstract Natural products, a chemically and structurally diverse class of molecules, possess a wide spectrum of biological activities, have been used therapeutically for millennia, and have provided many lead compounds for the development of synthetic drugs. Cytochrome P450 enzymes (P450s, CYP) are widespread in nature and are involved in the biosynthesis of many natural products. P450s are heme-containing enzymes that use molecular oxygen and the hydride donor NAD(P)H (coupled via enzymic redox partners) to catalyze the insertion of oxygen into C-H bonds in a regio- and stereo-selective manner, effecting hydroxylation and several other reactions. With the rapid development of systems biology, numerous novel P450s have been identified for the biosynthesis of natural products, but there are still several challenges to the efficient heterologous expression of active P450s. This review covers recent developments in P450 research and development, including the properties and functions of P450s, discovery and mining of novel P450s, modification and screening of P450 mutants, improved heterologous expression of P450s in microbial hosts, efficient whole-cell transformation with P450s, and current applications of P450s for the biosynthesis of natural products. This resource provides a solid foundation for the application of highly active and stable P450s in microbial cell factories to biosynthesize natural products.

Efficient heterologous expression of cytochrome P450 enzymes in microorganisms for the biosynthesis of natural products

P450 fatty acid
decarboxylases (FADCs) have recently been attracting considerable attention owing
to their one-step direct production of industrially important 1-alkenes from biologically abundant
feedstock free fatty acids under mild conditions. However, attempts to improve
the catalytic activity of FADCs have met with little success. Protein
engineering has been limited to selected residues and small mutant libraries
due to lack of an effective high-throughput screening (HTS) method. Here, we
devise a catalase-deficient Escherichia
coli host strain and report an HTS approach based on colorimetric detection
of H2O2-consumption activity of FADCs. Directed evolution
enabled by this method has led to effective identification for the first time
of improved FADC variants for medium-chain 1-alkene production from both DNA
shuffling and random mutagenesis libraries. Advantageously, this screening
method can be extended to other enzymes that stoichiometrically utilize H2O2
as co-substrate.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cctc.201901347

Directed Evolution of P450 Fatty Acid Decarboxylases via High-Throughput Screening towards Improved Catalytic Activity

The present invention relates to the detection of enzyme activity, in particular hydrogen conversion activity of an enzyme such as peroxygenase or peroxidase activity. More particularly, the invention provides a microplate-scale absorbance/fluorescence-based method for the detection of hydrogen conversion activity of an enzyme based on the measurement of hydrogen peroxide changes. The invention further provides screening methods for enzymes with improved hydrogen conversion activity, and a kit and combination of reagents suitable for use in the methods of the invention.

Method for detecting hydrogen peroxide conversion activity of an enzyme

The present invention relates to biocatalysts catalyzing the formation of α-olefins. In particular, the invention provides polypeptides with improved decarboxylase activity on C10-C16 free fatty acids, more particularly on C10 or C12 free fatty acids, as compared to the P450 fatty acid decarboxylase isolated from the Staphylococcus massiliensis strain S46 (Sm46). The invention further provides recombinant nucleic acids and vectors comprising the coding sequences encoding these polypeptides, genetically engineered host cells expressing said polypeptides and methods for the production of C9-C15 α-olefins, more particularly C9 or C11 α-olefins, using said polypeptides or said host cells.

Improved cytochrome p450 fatty acid decarboxylases

P450 fatty acid decarboxylases represented by the unusual CYP152 peroxygenase family member OleTJE have been receiving great attention recently since these P450 enzymes are able to catalyze the simple and direct production of 1-alkenes for potential applications in biofuels and biomaterials. To gain more mechanistic insights, broader substrate spectra, and improved decarboxylative activities, it is demanded to discover and investigate more P450 fatty acid decarboxylases. Here, we describe for the first time the expression, purification, and in vitro biochemical characterization of two new CYP152 peroxygenases, CYP-Aa162 and CYP-Sm46Δ29, that are capable of decarboxylating straight-chain saturated fatty acids. Both enzymes were found to catalyze the decarboxylation and hydroxylation of a broad range of free fatty acids (C10–C20) with overlapping substrate specificity, yet distinct chemoselectivity. CYP-Sm46Δ29 works primarily as a fatty (lauric) acid decarboxylase (66.1 ± 3.9% 1-undecene production) while CYP-Aa162 more as a fatty (lauric) acid hydroxylase (72.2 ± 0.9% hydroxy lauric acid production). Notably, the optical spectroscopic analysis of functional CYP-Sm46Δ29 revealed no characteristic P450 band, suggesting a unique heme coordination environment. Active-site mutagenesis analysis showed that substitution with the proposed key decarboxylation-modulating residues, His85 and Ile170, enhanced the decarboxylation activity of CYP-Aa162 and P450BSβ, emphasizing the importance of these residues in directing the decarboxylation pathway. Furthermore, the steady-state kinetic analysis of CYP-Aa162 and CYP-Sm46Δ29 revealed both cooperative and substrate inhibition behaviors which are substrate carbon chain length dependent. Our data identify CYP-Sm46Δ29 as an efficient OleTJE-like fatty acid decarboxylase. Oxidative decarboxylation chemoselectivity of the CYP152 decarboxylases is largely dependent upon the carbon chain length of fatty acid substrates and their precise positioning in the enzyme active site. Finally, the kinetic mode analysis of the enzymes could provide important guidance for future process design.

/pdf/in-vitro-oxidative-decarboxylation-of-free-fatty-acids-to-3zfxzl3lvk.pdf

In vitro oxidative decarboxylation of free fatty acids to terminal alkenes by two new P450 peroxygenases

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Directed Evolution of P450 Fatty Acid Decarboxylases via High-Throughput Screening towards Improved Catalytic Activity

Method for detecting hydrogen peroxide conversion activity of an enzyme

Improved cytochrome p450 fatty acid decarboxylases

In vitro oxidative decarboxylation of free fatty acids to terminal alkenes by two new P450 peroxygenases