Abstract
In the early days of biocatalysis, limitations of an enzyme modeled the enzymatic applications; nowadays the enzyme can be engineered to be suitable for the process requirements. This is a general bird’s-eye view and as such cannot be specific for articulated situations found in different classes of enzymes or for selected enzymatic processes. As far as the enzymatic preparation of glycosides is concerned, recent scientific literature is awash with examples of uniqueness related to the features of the biocatalyst (yield, substrate specificity, regioselectivity, and resistance to a particular reaction condition). The invention of glycosynthases is just one of the aspects that has thrust forward the research in this field. Protein engineering, metagenomics and reaction engineering have led to the discovery of an expanding number of novel enzymes and to the setting up of new bio-based processes for the preparation of glycosides. In this review, new examples from the last decade are compiled with attention both to cases in which naturally present, as well as genetically inserted, characteristics of the catalysts make them attractive for biocatalysis.
Highlights
In a brilliant, recently published analysis of the research-guided development in the field of biocatalysis during the last century, different authors recognized three historical waves of innovations that totally changed the field of biocatalysis to the present industrially accomplished level [1]
Sugar phosphates act as donors for other glycosyltransferases. Another widespread group of enzymes, named glycoside hydrolases, exists; they are involved in the carbohydrate metabolism being responsible for the hydrolysis of glycosidic linkages; they can act as exo- or endo-glycosidases and are involved in a series of important biological events such as energy uptake, in processes inherent cell wall metabolism, in glycan processing during in vivo glycoprotein synthesis, etc
Using data published up to the mid-term of 2003, Perugino et al compiled a review [39] accounting for 11 different glycoside hydrolases from bacteria, eukarya and archaea, that were modified as efficient glycosynthases
Summary
Recently published analysis of the research-guided development in the field of biocatalysis during the last century, different authors recognized three historical waves of innovations that totally changed the field of biocatalysis to the present industrially accomplished level [1]. Biomolecules 2013, 3 cannot be specific for articulated contexts in which each single class of enzyme or selected enzymatic process is at the present state In another similar general bird’s-eye analysis, Riva identified a long wave of successes still far from reaching the end in biocatalysis [2], due to the difficulties encountered in the shift from ‘classical’ processes to biobased ones. Sugar phosphates act as donors for other glycosyltransferases (non-Leloir pathway) Another widespread group of enzymes, named glycoside hydrolases (glycosidases), exists; they are involved in the carbohydrate metabolism being responsible for the hydrolysis of glycosidic linkages; they can act as exo- or endo-glycosidases and are involved in a series of important biological events such as energy uptake, in processes inherent cell wall metabolism, in glycan processing during in vivo glycoprotein synthesis, etc. This review will compile different examples where glycoside hydrolases are the key enzymes in the process
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