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Enzymatic glycosylation is a versatile and sustainable biotechnological approach that plays a pivotal role in the production of bioactive compounds. This process involves the enzymatic transfer of sugar moieties onto various acceptor molecules, such as small molecules, peptides, or proteins, resulting in the synthesis of glycosides. These glycosides often exhibit enhanced bioactivity, improved solubility, and enhanced stability, making them valuable in pharmaceuticals, nutraceuticals, and the food industry. This review explores the diverse enzymatic glycosylation strategies employed in the synthesis of bioactive compounds. It highlights the enzymatic catalysts involved, including glycosyltransferases, glycosidases, glycophosphorylases, and glycosynthases. It considers the advantages and disadvantages of these biocatalysts in the stereoselective and regioselective synthesis of different types of glycosylated molecules, phenolic and aliphatic alcohols, oligosaccharides, polysaccharides, glycoderivatives, glycopeptides, and glycoproteins with a clear focus on food and pharmaceutical chemistry. Furthermore, the review outlines various sources of sugar donors, activated glycosides, and sugar nucleotides, as well as the utilization of engineered enzymes and microorganisms for glycosylation reactions. The advantages of enzymatic glycosylation, including its high regioselectivity, stereoselectivity, and sustainability, are emphasized. Therefore, these approaches combining the use of different catalytic systems, the improvement of tools such as immobilization technology or chemical or genetic modification to improve the glycosylation process, could be useful tools in continuous biotechnological advancements.

In recent years, the synthesis of novel artificial metalloenzymes by the combination of metal or complex organometallic systems and enzymes is rapidly growing field of research in catalytic applications. In this study, new artificial metalloenzymes have been designed and developed based on the combination of an enzyme and different metal salts. For this purpose, novel synthesis method has been used, where the enzyme, Lipase B from Candida antarctica (CALB), acts as an inducer of metal nanoparticles of copper and silver. Obtained biohybrids show improved stability properties compared to natural enzymes. Moreover, the synergetic effect between copper and silver has been evaluated, looking for an improvement in the catalytic efficiency of an only copper-metalloenzyme previously developed. The copper-silver-CALB metalloenzymes have been characterized by X-Ray diffraction analysis, mass spectrometry, and SEM and TEM as microscopies techniques. After that, their catalytic efficiency was tested in different reactions, in particular in the phloridzin oligomerization as laccase-like activity.

Enzymatic glycosylation is a versatile and sustainable biotechnological approach that plays a pivotal role in the production of bioactive compounds. This process involves the enzymatic transfer of sugar moieties onto various acceptor molecules, such as small molecules, peptides, or proteins, resulting in the synthesis of glycosides. These glycosides often exhibit enhanced bioactivity, improved solubility, and enhanced stability, making them valuable in pharmaceuticals, nutraceuticals, and the food industry. This review explores the diverse enzymatic glycosylation strategies employed in the synthesis of bioactive compounds. It highlights the enzymatic catalysts involved, including glycosyltransferases, glycosidases, glycophosphorylases, and glycosynthases. It considers the advantages and disadvantages of these biocatalysts in the stereoselective and regioselective synthesis of different types of glycosylated molecules, phenolic and aliphatic alcohols, oligosaccharides, polysaccharides, glycoderivatives, glycopeptides, and glycoproteins with a clear focus on food and pharmaceutical chemistry. Furthermore, the review outlines various sources of sugar donors, activated glycosides, and sugar nucleotides, as well as the utilization of engineered enzymes and microorganisms for glycosylation reactions. The advantages of enzymatic glycosylation, including its high regioselectivity, stereoselectivity, and sustainability, are emphasized. Therefore, these approaches combining the use of different catalytic systems, the improvement of tools such as immobilization technology or chemical or genetic modification to improve the glycosylation process, could be useful tools in continuous biotechnological advancements.

Present worldwide difficulties in healthcare and the environment have motivated the investigation and research of novel materials in an effort to find novel techniques to address the current challenges and requirements. In particular, the use of nanomaterials has demonstrated a significant promise in the fight against bacterial infections and the problem of antibiotic resistance. Metal nanoparticles and carbon-based nanomaterials in particular have been highlighted for their exceptional abilities to inhibit many types of bacteria and pathogens. In order for these materials to be as effective as possible, synthetic techniques are crucial. Therefore, in this review article, we highlight some recent developments in the design and synthesis of various nanomaterials, including metal nanoparticles (e.g., Ag, Zn, or Cu), metal hybrid nanomaterials, and the synthesis of multi-metallic hybrid nanostructured materials. Following that, examples of these materials’ applications in antimicrobial performance targeted at eradicating multi-drug resistant bacteria, material protection such as microbiologically influenced corrosion (MIC), or additives in construction materials have been described.