Bacterial Chitinase System as a Model of Chitin Biodegradation

Itoh, Takafumi; Kimoto, Hisashi

doi:10.1007/978-981-13-7318-3_7

Cited by 34 publications

(22 citation statements)

References 82 publications

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“… Name of enzymes Sources Enzyme type Activity ref l -asparaginase Bacterial sources E. coli Erwinia carotovora) Asparaginase Convert l -asparagine into aspartic acid and ammonia Anti-carcinogenic activity Reduce carcinogenic acrylamide [ 150 ] [ 152 ] [ 157 ] Fungal sources Aspergillus oryzae Microalgae sources Spirulina maxima Chlamydomonas sp Carbonic anhydrase containg cadmium Marine diatom Thalassiosira weissflogii Metalloenzymes Catalyze the reversible hydration of CO2 Acquire inorganic carbon for photosynthesis [ 158 ] [ 159 ] Alkaline protease marine Psychrobacter Aureobasidium pullulan Bacillus mojavensis A21 Pseudoalteromonas sp Protease Peptide hydrolases [ 160 ] [ 161 ] Extracellular phospholipase C marine streptomycete Pseudoalteromonas sp Lipases Hydrolyze different oils [ 162 ] [ 163 ] Chitinase Chitosanase Vibrio fluvialis, Vibrio parahaemolyticus, Vibrio mimicus Vibrio alginolyticus Listonella anguillarum Aeromonas hydrophila Aspergillus griseoaurantiacus KX010988. Hydrolase Degrade chitin and chitosan [ [164] , [165] , [166] ...…”

Section: Biomaterials From Marine Organismsmentioning

confidence: 99%

Biomaterials from the sea: Future building blocks for biomedical applications

Wan

Qin

Chen

et al. 2021

Bioactive Materials

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Marine resources have tremendous potential for developing high-value biomaterials. The last decade has seen an increasing number of biomaterials that originate from marine organisms. This field is rapidly evolving. Marine biomaterials experience several periods of discovery and development ranging from coralline bone graft to polysaccharide-based biomaterials. The latter are represented by chitin and chitosan, marine-derived collagen, and composites of different organisms of marine origin. The diversity of marine natural products, their properties and applications are discussed thoroughly in the present review. These materials are easily available and possess excellent biocompatibility, biodegradability and potent bioactive characteristics. Important applications of marine biomaterials include medical applications, antimicrobial agents, drug delivery agents, anticoagulants, rehabilitation of diseases such as cardiovascular diseases, bone diseases and diabetes, as well as comestible, cosmetic and industrial applications.

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Section: Biomaterials From Marine Organismsmentioning

confidence: 99%

Biomaterials from the sea: Future building blocks for biomedical applications

Wan

Qin

Chen

et al. 2021

Bioactive Materials

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“…The copyright holder for this preprint this version posted January 14, 2021. ; https://doi.org/10.1101/2021.01.10.425899 doi: bioRxiv preprint 3 Deutsches Zentrum für Infektionsforschung (DZIF), Standort Hannover-Braunschweig, Germany. 4 Department of Chemistry, Saarland University, Saarbrücken, Germany. 5 GM/CA @ APS, Argonne National Laboratory, Lemont, Illinois, United States S1-S9 .…”

Section: Conflict Of Interestmentioning

confidence: 99%

“…The enzymatic degradation of carbohydrate polymers (glycans) in nature is generally mediated by endo- and exo-lytic glycosidases, which may act synergistically (1–3). Endo-glycosidases cleave glycosidic bonds within the inner part of glycan chains (endo-lytic cleavage), thereby solubilizing the polymers and providing oligomeric substrates for exo-glycosidases and exo-glucanases to act on, which subsequently chip off monomeric carbohydrates or disaccharides, respectively, from the non-reducing end or, in rare cases, from the reducing end (exo-lytic cleavage) (2,4). Accordingly, cellulose (poly-β-1,4-glucose), the main glycan component of plants, and chitin (poly-β-1,4- N -acetylglucosamine), the main glycan component of fungi and arthropods, are degraded by various organisms involving complex sets of lytic enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…Accordingly, cellulose (poly-β-1,4-glucose), the main glycan component of plants, and chitin (poly-β-1,4- N -acetylglucosamine), the main glycan component of fungi and arthropods, are degraded by various organisms involving complex sets of lytic enzymes. These include endo-lytic glycanases (endo-cellulases or endo-chitinases, respectively) and exo-glucanases, (cellobiohydrolases and diacetylchitobiohydrolases, respectively) as well as exo-lytic glycosidases (β-glucosidases/cellobiases and β- N -acetylglucosaminidases/diacetylchitobiases, respectively) (2,4).…”

Section: Introductionmentioning

confidence: 99%

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Exo-β-N-acetylmuramidase NamZ ofBacillus subtilisis the founding member of a family of exo-lytic peptidoglycan hexosaminidases

Müller

Calvert

Hottmann

et al. 2021

Preprint

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Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that potentially lyse bacterial cells. They catalyze an endo-lytic cleavage of the peptidoglycan, the structural component of the bacterial cell wall; i.e. they hydrolyze glycosidic N-acetylmuramic acid (MurNAc)-β-1,4-N-acetylglucosamine (GlcNAc)-bonds within the heteroglycan backbone of peptidoglycan. In contrast, little is known about exo-β-N-acetylmuramidases, catalyzing an exo-lytic cleavage of β-1,4-MurNAc entities from the non-reducing ends of peptidoglycan chains. Such an enzyme was identified earlier in the bacterium Bacillus subtilis, but the corresponding gene has remained unknown so far. We identified ybbC of B. subtilis, renamed namZ, as encoding the reported exo-β-N-acetylmuramidase. A ΔnamZ mutant accumulated specific cell wall fragments and showed growth defects under starvation conditions, indicating a role of NamZ in cell wall turnover. Recombinant NamZ protein specifically hydrolyzed the artificial substrate para-nitrophenyl β-MurNAc and the peptidoglycan-derived disaccharide MurNAc-β-1,4-GlcNAc. Together with the exo-β-N-acetylglucosaminidase NagZ and the exo-muramoyl-L-alanine amidase AmiE, NamZ degraded intact peptidoglycan by sequential hydrolysis from the non-reducing ends. NamZ is a member of the DUF1343 protein family of unknown function and shows no significant sequence identity with known glycosidases. A structural model of NamZ revealed a putative active site located in a cleft within the interface of two subdomains, one of which constituting a Rossmann-fold-like domain, unusual for glycosidases. On this basis, we propose that NamZ represents the founding member of a novel family of peptidoglycan hexosaminidases, which is mainly present in the phylum Bacteroidetes and, less frequently, within Firmicutes (Bacilli, Clostridia), Actinobacteria and Gammaproteobacteria.

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“…In addition to GHs, lytic polysaccharide monooxygenases oxidatively cleave chitin ( Vaaje-Kolstad et al, 2013 ). The degraded oligosaccharides are then imported through the bacterial cell membranes, and in the bacterial cytosol or periplasmic space, oligomers are hydrolyzed to GlcNAc by N -acetyl-D-glucosaminidases (GlcNAcases) ( Itoh and Kimoto, 2019 , Vaaje-Kolstad et al, 2013 ). The obtained GlcNAc is then transformed into the common metabolic intermediate, fructose-6-phosphate, to be further metabolized via glycolysis in the cytosol ( Nothaft et al, 2003 ).…”

Section: Introductionmentioning

confidence: 99%