ABSTRACT
Polysaccharides are complex macromolecules long regarded as energetic storage resources or as components of plant and fungal cell walls. They have also been described as plant mucilages or microbial exopolysaccharides. The development of glycosciences has led to a partial and difficult deciphering of their other biological functions in living organisms. The objectives of glycobiochemistry and glycobiology are currently to correlate some structural features of polysaccharides with some biological responses in the producing organisms or in another one. In this context, the literature focusing on bioactive polysaccharides has increased exponentially during the last two decades, being sometimes very optimistic for some new applications of bioactive polysaccharides, notably in the medical field. Therefore, this review aims to examine bioactive polysaccharide, taking a critical look of the different biological activities reported by authors and the reality of the market. It focuses also on the chemical, biochemical, enzymatic, and physical modifications of these biopolymers to optimize their potential as bioactive agents.
Subject(s)
Antineoplastic Agents/chemistry , Antioxidants/chemistry , Antiviral Agents/chemistry , Immunomodulating Agents/chemistry , Oligosaccharides/chemistry , Phytochemicals/chemistry , Plant Mucilage/chemistry , Animals , Drug Delivery Systems/methods , Food Industry/methods , Humans , Structure-Activity RelationshipABSTRACT
Microalgae have been poorly investigated for new-lipolytic enzymes of biotechnological interest. In silico study combining analysis of sequences homologies and bioinformatic tools allowed the identification and preliminary characterization of 14 putative lipases expressed by Chlorella vulagaris. These proteins have different molecular weights, subcellular localizations, low instability index range and at least 40% of sequence identity with other microalgal lipases. Sequence comparison indicated that the catalytic triad corresponded to residues Ser, Asp and His, with the nucleophilic residue Ser positioned within the consensus GXSXG pentapeptide. 3D models were generated using different approaches and templates and demonstrated that these putative enzymes share a similar core with common α/ß hydrolases fold belonging to family 3 lipases and class GX. Six lipases were predicted to have a transmembrane domain and a lysosomal acid lipase was identified. A similar mammalian enzyme plays an important role in breaking down cholesteryl esters and triglycerides and its deficiency causes serious digestive problems in human. More structural insight would provide important information on the enzyme characteristics.
