New Chitosan-Degrading Strains That Produce Chitosanases Similar to ChoA of
            <i>Mitsuaria chitosanitabida</i>

Yun, Choong-Soo; Amakata, Daiki; Matsuo, Yasuhiro; Matsuda, Hideyuki; Kawamukai, Makoto

doi:10.1128/aem.71.9.5138-5144.2005

Cited by 29 publications

(23 citation statements)

References 48 publications

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“…PF00933). Thus, our results showed that the primers designed for a GH80 family chitosanase by Yun et al (43) with little degeneracy can be used to amplify a GH3-like chitosanase-encoding gene of Anabaena (Fig. 1).…”

Section: Discussionmentioning

confidence: 92%

“…CsO-2. Yun et al (43) described a set of specific primers to detect new strains for production of chitosanases similar to chitosanase A of Mitsuaria chitosanitabida. In the current study, we used the same set of primers to amplify a chitosanase-encoding gene from two Anabaena species.…”

Section: Discussionmentioning

confidence: 99%

“…Genomic DNA was extracted using an Ultraclean plant DNA isolation kit (MoBio Inc., Carlsbad, CA). The concentrations in the reaction mixture, primer sets, and thermal cycler conditions used for amplification of the gene coding for chitosanase were those described by Yun et al (43). Specific primers ChoF1 (5Ј-ATG CCAGCATTGCAGAGAC-3Ј) and ChoR1 (5Ј-TTAAAAACAACAAGCGAT CGCC-3Ј) were designed to amplify the full-length chitosanase-encoding gene from both Anabaena species (Fig.…”

Section: Methodsmentioning

confidence: 99%

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Identification, Characterization, and Regulation of a Novel Antifungal Chitosanase Gene ( cho ) in Anabaena spp

Gupta

Prasanna

Natarajan

et al. 2010

Appl Environ Microbiol

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Two contrasting cyanobacterial species (Anabaena fertilissima and Anabaena sphaerica) were selected based on differences in antifungal behavior in order to study the mechanism for production of an antifungal enzyme and the genes responsible for this production. In A. fertilissima, chitosanase and antifungal activities were increased significantly under of growth-limiting conditions (8 of light and 16 h of darkness). The lack of such activities in A. sphaerica was associated with high levels of protein that accumulated during the stationary phase (at 28 days) under the same light conditions. The gene putatively responsible for chitosanase and antifungal activities was amplified using specific primers, and sequence analysis of the amplified products (1.086 and 1.101 kb in A. sphaerica and A. fertilissima, respectively) showed that they belong to the glycoside hydrolase 3 ( Cyanobacteria comprise a heterogeneous assemblage of photosynthetic prokaryotes having extraordinary biosynthetic potential and a repertoire of diverse metabolic activities. They are an important source of novel antifungal, antibacterial, and herbicidal or weedicidal compounds, which have been implicated in allelopathic interactions in water and soil (29). A majority of these metabolites are biologically active and are products of either nonribosomal polypeptide (NRP) or mixed polyketide-NRP biosynthetic pathways. The toxins produced by cyanobacteria are greatly influenced by various physiological and environmental factors, including light, temperature, nutrients, and pH (5).The antifungal properties of cyanobacterial metabolites, most of which have not been exploited, have immense potential in agriculture for use against fungal plant pathogens. In bacteria, lytic enzymes, such as chitinases, chitosanases, proteases, and ␤-1,3-glucanases, are known to have key roles in biocontrol of various soilborne fungal pathogens. Chitin is a linear polymer of 1,4-linked N-acetyl-D-glucosamine (GlcNAc) residues, and the deacetylated derivative of chitin is chitosan. In contrast to chitin, chitosan has been found in very few organisms, but it has been found in members of the Zygomycota, such as Mucor rouxii (42), Absidia coerulea (22), and Rhizopus oryzae (8). The filamentous fungi Lentinus edodes andPleurotus sajo-caju were investigated to determine their abilities to produce chitosan (30). Chitosan and chitosan-glucan complexes have been found in the mycelia of Aspergillus niger, Humicola lutea, and Fusarium moniliforme (39). Chitosanases (EC 3.2.1.132) produced by bacteria are classified into five glycoside hydrolase (GH) families (families 5, 8, 46, 75, and 80) (6, 10, 11, 12, 13). Families 5 and 8 are composed of enzymes that are hydrolytic with glycosides, and the family 46, 75, and 80 enzymes studied so far are chitosanases. This classification of chitosanases is based on amino acid sequence similarities of the catalytic domains. Recently, the family 46 chitosanase of Amycolatopsis sp. CsO-2 responsible for antifungal activity against Rhizopus oryzae ...

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Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Identification, Characterization, and Regulation of a Novel Antifungal Chitosanase Gene ( cho ) in Anabaena spp

Gupta

Prasanna

Natarajan

et al. 2010

Appl Environ Microbiol

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“…GH-5 and GH-8 contain a variety of glycoside hydrolases, such as chitosanase, cellulase, licheninase, and endo-1,4-␤-xylanase, whereas, GH-46, GH-75, and GH-80 are currently exclusively classified for chitosanase. Among these families, GH-46, especially those from Bacillus (17) and Streptomyces strains (18), have been studied extensively for their catalytic features (18), enzymatic mechanisms (19), and protein structures (20), whereas GH-75 and GH-80 have only been studied for protein purification (11)(12)(13)(14) and gene cloning (21,22). An interesting finding is that all GH-75 chitosanases are fungal enzymes, such as those from Aspergillus (11,14), Penicillium (12), Beauveria (GenBank TM accession number AY008269), Cordyceps (GenBank TM accession number AY008269), Fusarium (13), Hypocrea (GenBank TM accession number AY571342), Magnaporthe (GenBank TM accession number AACU01000927), Metarhizium (GenBank TM accession number AJ293219), and Neurospora (GenBank TM accession number AABX01000003).…”

mentioning

confidence: 99%

Exploration of Glycosyl Hydrolase Family 75, a Chitosanase from Aspergillus fumigatus

Cheng

Chang

et al. 2006

Journal of Biological Chemistry

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Tandem mass spectrum analysis of the enzymatic hydrolysate revealed that the recombinant CSN can cleave linkages of GlcNAcGlcN and GlcN-GlcN in its substrate, suggesting that it is a subclass I chitosanase. In addition, an extensive site-directed mutagenesis study on 10 conserved carboxylic amino acids of glycosyl hydrolase family 75 was performed. This showed that among these various mutants, D160N and E169Q lost nearly all activity. Further investigation using circular dichroism measurements of D160N, E169Q, wild-type CSN, and other active mutants showed similar spectra, indicating that the loss of enzymatic activity in D160N and E169Q was not because of changes in protein structure but was caused by loss of the catalytic essential residue. We conclude that Asp 160 and Glu 169 are the essential residues for the action of A. fumigatus endo-chitosanase.Chitosanase (EC 3.2.1.132) is a hydrolytic enzyme acting on the ␤-1,4-glycosidic linkage of chitosan, a linear biopolymer of ␤-1,4-linked GlcN, to release chito-oligosaccharides. The oligomers GlcNAc and GlcN have interesting biological activities (1), including anti-tumor effects (2, 3), hypo-cholesterolemic effects (4), anti-microbial activities (5, 6), disease-resistance responses, and as phytoalexin elicitors in higher plants (7,8). Hence chitosanase, chito-oligosaccharides and their derivatives have attracted interest from the food and pharmaceutical industries because they can be used as edible additives, agricultural immunity controls and promise many other prospective applications as prophylactic agents for liver diseases (4), atherosclerosis, and hypertension.

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“…Based on similarity of amino acid sequences, GH has been classified into 115 families [http://www.cazy.org/], among which GH-5 [Tanabe et al, 2003], -8 [Mitsutomi et al, 1998;Kimoto et al, 2002;Yatsunami et al, 2002;Choi et al, 2004;Kim et al, 2004;Ogura et al, 2006], -46 [Masson et al, 1994[Masson et al, , 1995Akiyama et al, 1999;Shimosaka et al, 2000;Yoon et al, 2000;Lee et al, 2006], -75 [Zhang et al, 2001;Shimosaka et al, 2005;Cheng et al, 2006] and -80 [Park et al, 1999;Yun et al, 2005] are known to have chitosanase activity. Founded on substrate specificity, these chitosanases have been further divided into 3 subclasses [Izume et al, 1992;Fukamizo et al, 1994Fukamizo et al, , 1995.…”

Section: Introductionmentioning

confidence: 99%

Discoidin Domain of Chitosanase Is Required for Binding to the Fungal Cell Wall

Kimoto

Akamatsu²,

Fujii³

et al. 2010

Microb Physiol

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Previously, we reported properties of a glycosylase belonging to GH-8 glycosyl hydrolase (GH) and having both chitosanase and glucanase activities. This enzyme (D2), whose molecular mass (86 kDa) was the largest among the GH-8 group, has its catalytic domain at the N-terminal region, and discoidin domain (DD) at the C-terminal region. Although various chitosanases, chitinases and glucanases have been known, DD is unique to the D2 enzyme. Glucanase and chitinase, but not chitosanase, are known to have functional domain such as carbohydrate-binding module, besides catalytic domain. Accordingly, function of the DD of D2 chitosanase was analyzed, using zygomycete cell wall containing chitosan, glucan and chitin as the basic constituents. The DD specifically and tightly bound to chitosan, but did not participate in affinity for glucan and chitin. Deletion of the DD caused marked reduction in absorbability to cell wall and in hydrolytic activity toward chitosan and glucan. These results suggest that the DD is concerned in binding of the enzyme to cell wall and in effective digestion of the insoluble substrate, through hydrolysis of not only chitosan but also coexisting glucan. Thus, this is the first example of chitosan-binding domain among various carbohydrate-binding modules reported thus far.

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New Chitosan-Degrading Strains That Produce Chitosanases Similar to ChoA of Mitsuaria chitosanitabida

Cited by 29 publications

References 48 publications

Identification, Characterization, and Regulation of a Novel Antifungal Chitosanase Gene ( cho ) in Anabaena spp

Identification, Characterization, and Regulation of a Novel Antifungal Chitosanase Gene ( cho ) in Anabaena spp

Exploration of Glycosyl Hydrolase Family 75, a Chitosanase from Aspergillus fumigatus

Discoidin Domain of Chitosanase Is Required for Binding to the Fungal Cell Wall

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