Topic
Chitinase
About: Chitinase is a research topic. Over the lifetime, 4690 publications have been published within this topic receiving 161786 citations. The topic is also known as: 1,4-beta-poly-N-acetylglucosaminidase & poly-beta-glucosaminidase.
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TL;DR: Reexamination of the previously used procedure revealed that the β(1-3)glucanase preparation used (zymolyase) is contaminated with a small amount of endochitinase, which caused erroneous results with the double mutant.
Abstract: Previous work, using solubilization of yeast cell walls by carboxymethylation, before or after digestion with beta(1-3)- or beta(1-6)glucanase, followed by size chromatography, showed that the transglycosylases Crh1p and Crh2p/Utr2p were redundantly required for the attachment of chitin to beta(1-6)glucan. With this technique, crh1Delta crh2Delta mutants still appeared to contain a substantial percentage of chitin linked to beta(1-3)glucan. Two novel procedures have now been developed for the analysis of polysaccharide cross-links in the cell wall. One is based on the affinity of curdlan, a beta(1-3)glucan, for beta(1-3)glucan chains in carboxymethylated cell walls. The other consists of in situ deacetylation of cell wall chitin, generating chitosan, which can be extracted with acetic acid, either directly (free chitosan) or after digestion with different glucanases (bound chitosan). Both methodologies indicated that all of the chitin in crh1Delta crh2Delta strains is free. Reexamination of the previously used procedure revealed that the beta(1-3)glucanase preparation used (zymolyase) is contaminated with a small amount of endochitinase, which caused erroneous results with the double mutant. After removing the chitinase from the zymolyase, all three procedures gave coincident results. Therefore, Crh1p and Crh2p catalyze the transfer of chitin to both beta(1-3)- and beta(1-6)glucan, and the biosynthetic mechanism for all chitin cross-links in the cell wall has been established.
82 citations
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TL;DR: Results indicate that E146 probably functions as an acid/base catalyst in the hydrolytic mechanism, as do homologous residues in other glycosyl hydrolases, which includes Manduca sexta chitinase as a member.
81 citations
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TL;DR: Confocal immunofluorescence microscopy was used to demonstrate that the Autographa californica nucleopolyhedrovirus (AcMNPV) chitinase was localized within the endoplasmic reticulum (ER) of virus-infected insect cells.
Abstract: Confocal immunofluorescence microscopy was used to demonstrate that the Autographa californica nucleopolyhedrovirus (AcMNPV) chitinase was localized within the endoplasmic reticulum (ER) of virus-infected insect cells. This was consistent with removal of the signal peptide from the chitinase and an ER localization motif (KDEL) at the carboxyl end of the protein. Chitinase release from cells, a prerequisite for liquefaction of virus-infected insect larvae, appears to be aided by synthesis of the p10 protein. Deletion of p10 from the AcMNPV genome delayed the appearance of chitinase activity in the medium of virus-infected cells by 24 h and also delayed liquefaction of virus-infected Trichoplusia ni larvae by the same period.
81 citations
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TL;DR: The unique characteristics of the purified chitinase include high molecular weight, nearly neutral optimum pH, protease activity, and antimicrobial activity with bacteria and fungal phytopathogens.
Abstract: Monascus purpureus CCRC31499 produced an antimicrobial chitinase when it was grown in a medium containing shrimp and crab shell powder (SCSP) of marine wastes. An extracellular antimicrobial chitinase was purified from the culture supernatant to homology. The chitinase had a molecular weight of approximately 81,000 and a pI of 5.4. The optimal pH, optimum temperature, and pH stability of the chitinase were pH 7, 40 degrees C, and pH 6-8, respectively. The activity of the chitinase was activated by Fe(2+) and strongly inhibited by Hg(2+). The unique characteristics of the purified chitinase include high molecular weight, nearly neutral optimum pH, protease activity, and antimicrobial activity with bacteria and fungal phytopathogens. This is also the first report of isolation of a chitinase from a Monascus species.
81 citations
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TL;DR: It is revealed that sustained and timely induction and accumulation of these defense enzymes and PR-proteins enhance the resistance in groundnut against leafminer insect and collar rot disease.
81 citations