Background
Type: Review

Tuning chitosan's chemical structure for enhanced biological functions

Journal: Trends In Biotechnology (01677799)Year: June 2023Volume: 41Issue: Pages: 785 - 797
Aghbashlo M.Amiri H.a Moosavi Basri S.M. Rastegari H. Lam S.S. Pan J. Gupta V.K. Tabatabaei M.
DOI:10.1016/j.tibtech.2022.11.009Language: English

Abstract

Chitosan, an amino polysaccharide mostly derived from crustaceans, has been recently highlighted for its biological activities that depend on its molecular weight (MW), degree of deacetylation (DD), and acetylation pattern (AP). More importantly, for some advanced biomaterials, the homogeneity of the chitosan structure is an important factor in determining its biological activity. Here we review emerging enzymes and cell factories, respectively, for in vitro and in vivo preparation of chitosan oligosaccharides (COSs), focusing on advances in the analysis of the AP and structural modification of chitosan to tune its functions. By ‘mapping’ current knowledge on chitosan's in vitro and in vivo activity with its MW and AP, this work could pave the way for future studies in the field. © 2022 Elsevier Ltd


Author Keywords

acetylation patternbiological activitychitosanhomogeneity

Other Keywords

Biocompatible MaterialsChitosanAcetylationBioactivityacyltransferasechitin de n acetylasechitin deacetylasechitin synthasechitobiosechitosan oligosaccharidechitotrioseenzymeunclassified drugbiomaterial'currentAcetylation patternBiological functionsDegree of acetylationDegree of deacetylationHomogeneityIn-vitroStructural modificationsVitro and in vivoAeromonas hydrophilaAggregatibacter actinomycetemcomitansalkylationAlternaria brassicicolaantimicrobial activityatomic force microscopyBasidiomycetesBifidobacterium bifidumbiodegradabilityBotrytis cinereaCandida albicanscarbon nuclear magnetic resonancecarboxylationchemical analysischemical fingerprintingchemical modificationchemical structureCorynebacterium glutamicumCRISPR-CAS9 systemcrystal structurecytotoxicitydeacetylationenzyme active siteenzyme engineeringEscherichia colifield flow fractionationfluorescence microscopygene silencingglycosylationhydrolysisIC50in vitro studyin vivo studyListeria monocytogenesmass spectrometryminimum lethal concentrationmolecular interactionmolecular mechanicsmolecular weightnitrogen fixationnonhumanOgataea angustapeptide mappingPhaeodactylum tricornutumPichia kudriavzeviipolymerizationproton nuclear magnetic resonancePseudomonas aeruginosaquaternizationReviewSalmonella enterica serovar TyphimuriumShigella dysenteriaesize exclusion chromatographyStaphylococcus aureusStreptococcus mutansstructure activity relationstructure analysisThalassiosira pseudonanaThalassiosira weissflogiiVibrio choleraeVibrio parahaemolyticusX ray diffraction