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: The antifungal activities of rye seed chitinase-a and -c were studied in detail using two different bioassays with Trichoderma sp.
Abstract: The antifungal activities of rye seed chitinase-a (RSC-a, class I) and -c (RSC-c, class II) were studied in detail using two different bioassays with Trichoderma sp. as well as binding and degradation experiments with the cell walls prepared from its mycelia. RSC-a inhibited more strongly the re-extension of the hyphae, containing mainly mature cells, than RSC-c did. Upon incubation of the fungus with fluorescent chitinases, FITC-labeled RSC-a was found to be located in the hyphal tips, lateral walls, and septa, while FITC-labeled RSC-c was only in the hyphal tip. RSC-a had a greater affinity for the cell walls than RSC-c. RSC-a liberated a larger amount of reducing sugar from the cell walls than RSC-c did. These results inferred that RSC-a first binds to the lateral walls and septa, consisting of the mature cell walls, and degrades mature chitin fiber, while RSC-c binds only to the hyphal tip followed by degradation of only nascent chitin. As a result, RSC-a inhibited fungal growth more effectively than RSC-c. Furthermore, it was suggested that the chitin-binding domain in RSC-a assists the antifungal action of RSC-a by binding to the fungal hypha.
70 citations
TL;DR: A crude preparation of extracellular proteins from Streptomyces sp.
Abstract: A crude preparation of extracellular proteins fromStreptomyces sp. ATCC 11238, containing chitin and laminarin degrading enzymes was active in lysing the cell walls of most of 50 viable filamentous ascomycetes tested, but was almost inactive with endomycetidae, zygomycetes and oomycetes. This mycolase preparation was fractionated by gel filtration and DEAE-ion exchange chromatography with special interest in chitin-degrading enzymes. N-Acetylglucosamine is liberated from crab shell chitin by the combined action of an exo-chitinase and β-N-acetylglucosaminidase. Both purified enzymes lysed cell wall preparations singly or together only when supplemented by protein containing endochitinase activity recovered from the gel after gel electrophoresis. Furthermore, enzymes degrading chitosan and azocoll were detected and separated.
70 citations
TL;DR: Chitinase activity has been investigated in mycorrhiza-resistant (myc−), non-nodulating (nod−) isogenic pea (Pisum sativum L.) mutants in an attempt to understand the reasons for such resistance to symbiotic fungi.
70 citations
TL;DR: Results of these experiments indicate that the lipase and protease attack the cuticle earlier than the chitinase, which enables penetration of the fungus through the cuticles of the infested insect.
70 citations
TL;DR: The role of the detected N-acetylglucosamine containing molecules as possible substrates for plant chitinases is discussed in this paper, where trathin sections of healthy and fungus-infected plant tissue were treated with either wheat-germ agglutinin (WGA) ovomucoid-gold complex or microbial CHITINase-gold complexes for localizing putative chitIN-like macromolecules.
70 citations