Enzymatic cofactor regeneration systems: A new perspective on efficiency assessment

Sci Total Environ. 2023 Apr 10:868:161630. doi: 10.1016/j.scitotenv.2023.161630. Epub 2023 Jan 16.

Abstract

Nowadays, the specificity of enzymatic processes makes them more and more important every year, and their usage on an industrial scale seems to be necessary. Enzymatic cofactors, however, play a crucial part in the prospective applications of enzymes, because they are indispensable for conducting highly effective biocatalytic activities. Due to the relatively high cost of these compounds and their consumption during the processes carried out, it has become crucial to develop systems for cofactor regeneration. Therefore, in this review, an attempt was made to summarize current knowledge on enzymatic regeneration methods, which are characterized by high specificity, non-toxicity and reported to be highly efficient. The regeneration of cofactors, such as nicotinamide dinucleotides, coenzyme A, adenosine 5'-triphosphate and flavin nucleotides, which are necessary for the proper functioning of a large number of enzymes, is discussed, as well as potential directions for further development of these systems are highlighted. This review discusses a range of highly effective cofactor regeneration systems along with the productive synthesis of many useful chemicals, including the simultaneous renewal of several cofactors at the same time. Additionally, the impact of the enzyme immobilization process on improving the stability and the potential for multiple uses of the developed cofactor regeneration systems was also presented. Moreover, an attempt was made to emphasize the importance of the presented research, as well as the identification of research gaps, which mainly result from the lack of available literature on this topic.

Keywords: Adenosine 5′-triphosphate; Coenzyme A; Dual cofactor regeneration; Enzymatic cofactor regeneration; Flavin nucleotides; Nicotinamide dinucleotides.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate
  • Biocatalysis
  • Coenzymes* / chemistry
  • Enzymes, Immobilized / metabolism
  • Niacinamide*

Substances

  • Coenzymes
  • Niacinamide
  • Enzymes, Immobilized
  • Adenosine Triphosphate