Enzyme immobilization has been developing since the 1960s and although many industrial biocatalytic processes use the technology to improve enzyme performance, still today we are far from full exploitation of the field. One clear reason is that many evaluate immobilization based on only a few experiments that are not always well-designed. In contrast to many other reviews on the subject, here we highlight the pitfalls of using incorrectly designed immobilization protocols and explain why in many cases sub-optimal results are obtained. We also describe solutions to overcome these challenges and come to the conclusion that recent developments in material science, bioprocess engineering and protein science continue to open new opportunities for the future. In this way, enzyme immobilization, far from being a mature discipline, remains as a subject of high interest and where intense research is still necessary to take full advantage of the possibilities.

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization.

Multistep enzyme cascades as a route towards green and sustainable pharmaceutical syntheses

Biocatalysis community has witnessed a drastic increase in the number of studies for the use of enzymes in continuously operated flow reactors. This significant interest arose from the possibility of combining the strengths of the two worlds: enhanced mass transfer and resource efficient synthesis achieved in flow chemistry at micro-scales and excellent selectivities obtained in biocatalysis. Within this review, we present very recent (from 2018 to September 2020) developments in the field of biocatalysis in continuously operated systems. Briefly, we describe the fundamentals of continuously operated reactors with a special focus on enzyme-catalyzed reactions. We devoted special attention on future perspectives in this key emerging technological area ranging from process analytical technologies to digitalization.

/pdf/the-rise-of-continuous-flow-biocatalysis-fundamentals-very-yvdsie0fcf.pdf

The rise of continuous flow biocatalysis – fundamentals, very recent developments and future perspectives

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.

Round, round we go - strategies for enzymatic cofactor regeneration.

There is currently considerable interest in the intensification of biocatalytic processes to reduce the cost of goods for biocatalytically produced chemicals, including pharmaceuticals and advanced pharmaceutical intermediates. Continuous-flow biocatalysis shows considerable promise as a method for process intensification; however, the reliance of some reactions on the use of diffusible cofactors (such as the nicotinamide cofactors) has proven to be a technical barrier for key enzyme classes. This minireview covers attempts to overcome this limitation, including the cofactor recapture and recycling retention of chemically modified cofactors. For the latter, we also consider the state of science for cofactor modification, a field reinvigorated by the current interest in continuous-flow biocatalysis.

https://www.mdpi.com/2073-4344/12/11/1454/pdf?version=1668683197

Cofactor and Process Engineering for Nicotinamide Recycling and Retention in Intensified Biocatalysis

Introduction Introduction Results Conclusions Author Contributions Competing Interests Statement General DNA manipulation G3PDEc NoxCa GlpKTk AceKMs GlpKTk-AceKMs G3PDEc-NOXCa GlpKTk-AceKMsE2Aa G3PDEc-NOXCa-Est2Aa FruASc-Est2Aa Engineered Fusion Protein... Expression of individual enzymes... Expression of GlpKTk-AceKMs-E2Aa Expression and purification of... Expression and purification of... Protein Expression and... Synthesis of N6-2AE-ADP ...

/pdf/engineered-enzymes-that-retain-and-regenerate-their-4evbh09z54.pdf

Engineered Enzymes that Retain and Regenerate their Cofactors Enable Continuous-Flow Biocatalysis

Nanomachine biocatalysts: Tools for cell-free artificial metabolic networks

Biocatalysis is an attractive route for the synthesis of complex organic molecules, such as pharmaceuticals, due to the properties of enzymes (high specificity and high catalytic rate). Ideally, we would be able to use enzymes in continuous-flow reactors to benefit from the advantages of continuous-flow chemistry (flexibility, control, product stream purity, low capital cost and improved yields for some reactions). However, continuous-flow applications for biocatalysis face substantial technical obstacles, particularly for enzymes that require cofactors. In the work presented here we tackle two of these obstacles: the provision of cofactor and cofactor recycling in flow, and enzyme immobilization without loss of activity. This is achieved through the production of modular biocatalysts that retain and recycle their cofactors, and that allow orthogonal, site-specific covalent conjugation to a surface. This generalizable engineering approach allowed us to build a complex, multistep flow reactor that outperforms previously published systems for cofactor-dependent continuous-flow biocatalysis. Tackling the loss of expensive cofactors is a key challenge in continuous-flow biocatalysis. This work reports immobilized enzymes with a tethered cofactor that is channelled between a recycling and a catalysis module facilitating total turnover numbers of NAD+ and ATP exceeding 10,000 in biocatalytic flow systems.

/pdf/engineered-enzymes-that-retain-and-regenerate-their-4shnz01ibn.pdf

Engineered enzymes that retain and regenerate their cofactors enable continuous-flow biocatalysis

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Cofactor and Process Engineering for Nicotinamide Recycling and Retention in Intensified Biocatalysis

Engineered Enzymes that Retain and Regenerate their Cofactors Enable Continuous-Flow Biocatalysis

Nanomachine biocatalysts: Tools for cell-free artificial metabolic networks

Engineered enzymes that retain and regenerate their cofactors enable continuous-flow biocatalysis