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.

Chitin Degradation Proteins Produced by the Marine Bacterium Vibrio harveyi Growing on Different Forms of Chitin.

Abstract: Relatively little is known about the number, diversity, and function of chitinases produced by bacteria, even though chitin is one of the most abundant polymers in nature. Because of the importance of chitin, especially in marine environments, we examined chitin-degrading proteins in the marine bacterium Vibrio harveyi. This bacterium had a higher growth rate and more chitinase activity when grown on (beta)-chitin (isolated from squid pen) than on (alpha)-chitin (isolated from snow crab), probably because of the more open structure of (beta)-chitin. When exposed to different types of chitin, V. harveyi excreted several chitin-degrading proteins into the culture media. Some chitinases were present with all of the tested chitins, while others were unique to a particular chitin. We cloned and identified six separate chitinase genes from V. harveyi. These chitinases appear to be unique based on DNA restriction patterns, immunological data, and enzyme activity. This marine bacterium and probably others appear to synthesize separate chitinases for efficient utilization of different forms of chitin and chitin by-products.

Control of plant diseases by chitinase expressed from cloned DNA in Escherichia coli

Abstract: When Sclerotium rolfsii was sprayed with partially purified chitinase produced by the cloned gene, rapid and extensive bursting of the hyphal tips was observed. This chitinase preparation was found to be effective in reduction of disease incidence caused by S. rolfsii in beans and Rhizoctonia solani in cotton under greenhouse conditions (62% disease reduction in both diseases). A similar effect was obtained when we used viable cells of E. coli containing the plasmid pLCHIA. However, E. coli carrying the plasmid lacking the pL promotor did not have any effect. These results suggest a role for chitinase in biological control of plant pathogenic fungi

Chitinolytic assay of indigenous Trichoderma isolates collected from different geographical locations of Chhattisgarh in Central India

Abstract: Chitin is the second most abundant polymer in nature after cellulose and plays a major role in fungal cell walls. As a producer of variety of chitinase enzymes Trichoderma has become an important means of biological control of fungal diseases. A simple and sensitive method based on the use of basal medium with colloidal chitin as sole carbon source supplemented with Bromo cresol purple (pH indicator dye) is proposed to evaluate large populations of Trichoderma for chitinase activity. The soluble substrate with pH indicator dye (Bromo cresol purple, BCP) for the assay of chitinase activity on solid media is sensitive, easy, reproducible semi-quantitative enzyme diffusion plate assay and economic option to determine chitinases. Colloidal chitin derived from Rhizoctonia cell wall and commercial chitin included as a carbon source in broth also allowed selection and comparison of chitinolytic and exochitinase activity in Trichoderma spectrophotometrically. Released N-acetyl-β--D-glucosamine (NAGA) ranged from 37.67 to 174.33 mg/ml and 37.67 to 327.67 mg/ml and p-nitrophenol (pNP) ranged from 0.17 to 35.78 X 10-3 U/ml and 0.62 to 32.6 X 10-3 U/ml) respectively with Rhizoctonia cell wall and commercial chitin derived colloidal chitin supplemented broth.

Chitinase in roots of mycorrhizal Allium porrum: regulation and localization

Abstract: Chitinase (EC 3.2.1.14) activity was measured in roots of Allium prorrum L. (leek) during development of a vesicular-arbuscular mycorrhizal symbiosis with Glomus versiforme (Karst.) Berch. During the early stages of infection, between 10 and 20 d after inoculation, the specific activity of chitinase was higher in mycorrhizal roots than in the uninfected controls. However, 60-90 d after inoculation, when the symbiosis was fully established, the mycorrhizal roots contained much less chitinase than control roots. Chitinase was purified from A. porrum roots. An antiserum against beanleaf chitinase was found to cross-react specifically with chitinase in the extracts from non-mycorrhizal and mycorrhizal A. porrum roots. This antiserum was used for the immunocytochemical localization of the enzyme with fluorescent and gold-labelled probes. Chitinase was localized in the vacuoles and in the extracellular spaces of non-mycorrhizal and mycorrhizal roots. There was no immunolabelling on the fungal cell walls in the intercellular or the intracellular phases. It is concluded that the chitin in the fungal walls is inaccessible to plant chitinase. This casts doubts on the possible involvement of this hydrolase in the development of the mycorrhizal fungus. However, fungal penetration does appear to cause a typical defense response in the first stages that is later depressed.

Evidence that chitinase produced by Aeromonas caviae is involved in the biological control of soil-borne plant pathogens by this bacterium.

Abstract: A chitinolytic isolate of Aeromonas caviae was isolated from roots of healthy bean plants grown in soil artificially infested with Sclerotium rolfsii. Under greenhouse conditions, the bacterium controlled Rhizoctonia solani and Fusarium oxysporum f.sp. vasinfectum in cotton (78 and 57% disease reduction, respectively) and S. rolfsii in beans (60% disease reduction). Seed coating was the most effective application method for controlling R. solani in cotton. There was no evidence of inhibition of the fungal pathogens by A. caviae. A caviae partially lysed live mycelium of R. solani, S. rolfsii and F. oxysporum f.sp. vasinfectum when their mycelium served as a sole carbon source in liquid medium. A high chitinolytic activity was found when colloidal chitin was used as a sole carbon source, with an optimum pH between 6.0–7.0. No β-3-glucanase was produced by the bacterium. After partial purification of the enzyme by affinity adsorption to colloidal chitin, three bands appear in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). One strong band with a molecular weight of ca. 80 kDa, and two weak bands with molecular weights of 48 and 59 kDa. Using the chromogenic substrate pNp-chitobiose, the partially purified chitinase from A. caviae was shown to act in an exo-splitting manner.