Biocatalysts from Aplysia: sweet spot in enzymatic carbohydrate synthesis
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| Trefwoorden |
Aplysia fasciata Poiret, 1789 [WoRMS]; Aplysia kurodai (Baba, 1937) [WoRMS]
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| Abstract |
Speaking in general terms, glycosylation is considered to be an important method for the structural modification of compounds with useful biological activities. Glycosylation allows conversion of lipophilic compounds into hydrophilic ones, thus improving their pharmacokinetic properties or giving access to new drug delivery systems (prodrugs). Examples include synthetic carbohydrate-based polymers used as coating agents and as biomedical materials, or novel dietary carbohydrates introduced as food additives. Finally, chromophoric oligosaccharides are of widespread interest for the kinetic analysis of hydrolytic activities and to characterize the mode of action of particular enzymes (i. e., exo or endoglycosidases). Hence carbohydrate-based compounds have proved to be a valuable tool in different fields of applicative interest, such as clinical, biological, and food chemistry. Different enzymes acting on these molecules are commercially available, but a greater interest would entail a search for biocatalysts with new catalytic characteristics. The marine environment has been shown to be a very interesting source for new glycosyl hydrolases both for hydrolytic and synthetic applications. Aplysia is a genus of sea hares belonging to the family Aplysiidae, containing different species of organisms. Aplysia fasciata and Aplysia kurodai are two examples; they are herbivorous animals and eat a variety of red, green, or brown algae and have been revealed to be potent producers of a library of glycoside hydrolases applied in the synthesis and hydrolysis of glycosidic bonds. In this chapter, examples of applications of such enzymes will be discussed. |
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