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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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Journal ArticleDOI
TL;DR: Two chitinases were purified from Rhizopus oligosporus, a filamentous fungus belonging to the class Zygomycetes, and it is concluded that these chit inases are synthesized with pre- and prosequences in addition to the mature enzyme sequences and that the pro sequences are located at the C terminal.
Abstract: Two chitinases were purified from Rhizopus oligosporus, a filamentous fungus belonging to the class Zygomycetes, and designated chitinase I and chitinase II. Their N-terminal amino acid sequences were determined, and two synthetic oligonucleotide probes corresponding to these amino acid sequences were synthesized. Southern blot analyses of the total genomic DNA from R. oligosporus with these oligonucleotides as probes indicated that one of the two genes encoding these two chitinases was contained in a 2.9-kb EcoRI fragment and in a 3.6-kb HindIII fragment and that the other one was contained in a 2.9-kb EcoRI fragment and in a 11.5-kb HindIII fragment. Two DNA fragments were isolated from the phage bank of R. oligosporus genomic DNA with the synthetic oligonucleotides as probes. The restriction enzyme analyses of these fragments coincided with the Southern blot analyses described above and the amino acid sequences deduced from their nucleotide sequences contained those identical to the determined N-terminal amino acid sequences of the purified chitinases, indicating that each of these fragments contained a gene encoding chitinase (designated chi 1 and chi 2, encoding chitinase I and II, respectively). The deduced amino acid sequences of these two genes had domain structures similar to that of the published sequence of chitinase of Saccharomyces cerevisiae, except that they had an additional C-terminal domain. Furthermore, there were significant differences between the molecular weights experimentally determined with the two purified enzymes and those deduced from the nucleotide sequences for both genes. Analysis of the N- and C-terminal amino acid sequences of both chitinases and comparison of them with the amino acid sequences deduced from the nucleotide sequences revealed posttranslational processing not only at the N-terminal signal sequences but also at the C-terminal domains. It is concluded that these chitinases are synthesized with pre- and prosequences in addition to the mature enzyme sequences and that the prosequences are located at the C terminal.

105 citations

Journal ArticleDOI
TL;DR: A brief survey of recent progress in the regulation and cloning of microbial chitinase genes is given and emphasis is placed on the post-translational modification and localization of the recombinant protein in the host.
Abstract: A range of chitinase genes from microorganisms have been cloned and the potential uses of these genetically manipulated organisms are being investigated by various researchers Fungi and yeast are better producers of chitinase than bacteria Since fungi grow at a slower rate, there have been efforts to clone the fungal chitinase genes into fast-growing bacteria This review gives a brief survey of recent progress in the regulation and cloning of microbial chitinase genes Emphasis is placed on the post-translational modification and localization of the recombinant protein in the host Various amino acid domains are present in this protein The mode of catalytic activity of the recombinant protein in comparison to the wild-type protein is discussed in the available literature The different mechanisms involved in the regulation of chitinase genes from various microorganisms is discussed by the researchers The scope of future research and conclusions yet to be obtained in this particular area are also outlined in this review

105 citations

Journal ArticleDOI
01 Dec 1994-Yeast
TL;DR: Observations support the notion that the insolubilization of the glucan is caused by linkage to chitin, and the linkage of the two polymers significantly contributes to the mechanical strength of the cell wall.
Abstract: Pulse-chase experiments with [14C]glucose demonstrated that in the cell wall of wild-type Saccharomyces cerevisiae alkali-soluble (1-3)-beta-glucan serves as a precursor for alkali-insoluble (1-3)-beta-glucan. The following observations support the notion that the insolubilization of the glucan is caused by linkage to chitin: (i) degradation of chitin by chitinase completely dissolved the glucan, and (ii) disruption of the gene for chitin synthase 3 prevented the formation of alkali-insoluble glucan. These cells, unable to form a glucan-chitin complex, were highly vulnerable to hypo-osmotic shock indicating that the linkage of the two polymers significantly contributes to the mechanical strength of the cell wall. Conversion of alkali-soluble glucan into alkali-insoluble glucan occurred both early and late during budding and also in the ts-mutant cdc24-1 in the absence of bud formation.

105 citations

Journal ArticleDOI
TL;DR: There is strong evidence that OnCht plays an important role in regulating chitin content of the PM and subsequently affecting the growth and development of the ECB larvae.

105 citations

Journal ArticleDOI
TL;DR: In this article, the methylxanthine derivatives are identified as possible inhibitor leads for fungal chitinases, including theophylline, caffeine, and pentoxifylline.

104 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023186
2022337
2021148
2020172
2019154
2018152