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Chitin oligopolysaccharide (COPS), including chitosan and chitosan oligosaccharide, has unique biological properties. By producing ammonia, encouraging the growth of antagonistic bacteria, and enhancing crop tolerance, COPSs help suppress PPN growth during soil remediation. COPS is also an effective sustained-release carrier that can be used to overcome the shortcomings of nematicidal substances. This review summarizes the advancements of COPS research in nematode control from three perspectives of action mechanism as well as in slow-release carrier-loaded nematicides. Further, it discusses potential agricultural applications for nematode disease management.Conflict of interest statement Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this Study of the mode of action and site-specificity of the endo-(1----4)-beta-D-glucanases of the fungus Penicillium pinophilum with The modes of action of the five major endo-(1----4)-beta-D-glucanases (I, II, III, IV and V) purified from Penicillium pinophilum cellulase were compared by h.

p.l.c. 2'-Fucose lactose , with normal, 1-3H-labelled and reduced cello-oligosaccharides and 4-methylumbelliferyl glycosides as substrates. Significant differences were observed in the preferred site of cleavage even when substrates with the same number of glycosidic bonds were compared. Thus, although endoglucanase I was unable to attack normal cello-oligosaccharides shorter than degree of polymerization 6, it hydrolysed reduced cellopentaose to yield cellotriose and cellobi-itol, and it produced cellotriose and 4-methylumbelliferyl glucoside from 4-methylumbelliferyl cellotetraoside. Endoglucanase IV hydrolysed [1-3H]cellotriose but did not attack either cellotri-itol or 4-methylumbelliferyl cellobioside.

These and other anomalous results indicated clearly that modification of the reducing glycosyl residue on the cello-oligosaccharides induces in an apparent change in the mode of action of the endoglucanases. 2'-FL is suggested that, although cello-oligosaccharide derivatives are useful for differentiating and classifying endoglucanases, conclusions on the mechanism of cellulase action resulting from these measurements should be treated cautiously. Unequivocal information on the mode of endoglucanase action on cello-oligosaccharides was obtained with radiolabelled cello-oligosaccharides of degree of polymerization 3 to 5. Indications that transglycosylation was a property of the endoglucanases were particularly evident with the 4-methylumbelliferyl cello-oligosaccharides. Turnover numbers for hydrolysis of the umbelliferyl cello-oligosaccharides were calculated, and these, along with the other analytical data collected on the products of hydrolysis of the normal, reduced and radiolabelled cello-oligosaccharides, suggested that the various endoglucanases had different roles to play in the overall hydrolysis of cellulose to sugars small enough to be transported through the cell membrane.Differential Recognition of Deacetylated PNAG Oligosaccharides by a Biofilm Exopolysaccharides consisting of partially de-N-acetylated poly-β-d-(1→6)-N-acetyl-glucosamine (dPNAG) are key structural components of the biofilm extracellular polymeric substance of both Gram-positive and Gram-negative human pathogens. De-N-acetylation is required for the proper assembly and function of dPNAG in biofilm development suggesting that different patterns of deacetylation may be preferentially recognized by proteins that interact with dPNAG, such as Dispersin B (DspB).

The enzymatic degradation of dPNAG by the Aggregatibacter actinomycetemcomitans native β-hexosaminidase enzyme DspB plays a role in biofilm dispersal. To test the role of substrate de-N-acetylation on substrate recognition by DspB, we applied an efficient preactivation-based one-pot glycosylation approach to prepare a panel of dPNAG trisaccharide analogs with defined acetylation patterns.
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