Expression of a novel chitinase by the fungal endophyte in<i>Poa ampla</i>

Li, Huaijun Michael; Sullivan, Ray; Moy, Melinda; Kobayashi, Donald Y.; Belanger, Faith C.

doi:10.1080/15572536.2005.11832951

Cited by 25 publications

(14 citation statements)

References 46 publications

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“…Now that it is established that endophytes produce chitinase in vitro, the possibility of endophytes contributing to, or inducing host chitinases has to be addressed. In the only study so far on chitinase of endophytic fungi, Li et al (2004) showed that a novel chitinase is expressed by the endophyte in infected plant hosts. However, this work is with reference to a grass endophyte.…”

Section: Discussionmentioning

confidence: 98%

Chitinolytic enzymes from endophytic fungi

et al. 2010

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Fungal endophytes isolated from leaves of tree species of the forests of Western Ghats, southern India were screened for chitin modifying enzyme production. Thirtyone of the one hundred and sixty two isolates were positive for chitinase, while different isolates produced isoforms of the enzyme. Many isolates produced chitosanase that acted on chitosan with different degrees of acetylation. Modified chitin and different types of chitosans are used in biomedical applications including wound healing, drug delivery, gene delivery, tissue engineering, in the food industry as preservatives and emulsifying agents, and in biocatalysis. Horizontally transmitted endophytes appear to be a good source for a variety of chitin modifying enzymes with the potential to be used in biotechnology. The possibility of chitin modifying enzymes of endophytes in regulating plant defense against pathogens and pests in vivo should also be addressed.

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Section: Discussionmentioning

confidence: 98%

Chitinolytic enzymes from endophytic fungi

et al. 2010

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“…Chitinase activity was quantitatively determined by colorimetric measurements assessing the nitrophenyl group of p-nitrophenyl-β-D-N-acetyl-glucosamide which served as the substrate [24]. A typical enzyme reaction mixture contained 0.45 ml of the same buffer, 0.1 ml of the enzyme-containing sample, and 0.1 ml of 0.5 mM of substrate in 0.1 M sodium acetate buffer, at pH 5.5.…”

Section: Enzyme Activity and Storage Stability Measurementsmentioning

confidence: 99%

Thermodynamics of Chitinase Partitioning in Soy Lecithin Liposomes and Their Storage Stability

Cano-Salazar

Juárez-Ordáz

Gregorio‐Jáuregui

et al. 2011

Appl Biochem Biotechnol

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The goal of this study was to define the partitioning behavior of chitinase from Trichoderma spp. in soy lecithin liposomes, using a thermodynamic approach based on the partitioning variation with temperature. An effort has been made to define the liposomes, as well as free and immobilized enzyme stability during storage at 4 and 25 °C. The partition coefficients (K (o/w)) were greater than 1; therefore, the standard free energies of the enzyme transfer were negative, indicating an affinity of the enzymes for encapsulation in liposomes. The enthalpy calculation led to the conclusion that the process is exothermic. The presence of enzyme decreased the liposome storage stability from 70 days to an approximately 20 days at 25 °C and 30 days at 4 °C. Monitoring of the liposome's diameter demonstrated that their size and concentration decreased during storage. The liposome's diameters ranged from 1.06 to 3.30 μm. The higher percentage of liposome corresponded to a diameter range from 1.06 to 1.34 μm. This percentage increased during storage. There were no evidences for liposome fusion process. The stability of immobilized enzyme was increased in comparison with free chitinase.

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“…Subtilisin-like protease, chitinase, N-acetylglucosaminidase and -1,6-glucanase activities have been identiWed (Lindstrom et al, 1993;Li et al, 2004Li et al, , 2005Moy et al, 2002). As the genes encoding these enzymes have not been functionally characterized, the eVect that these proteins have on the endophyte-grass symbiosis is unknown.…”

Section: Introductionmentioning

confidence: 98%

“…These enzymes may degrade macromolecules to provide nutrients to support fungal growth, or be involved in physiological processes such as the autolysis of fungal hyphae (Reddy et al, 1996;Moy et al, 2000;Li et al, 2004). The enzymes could also be involved in protecting the fungus from plant defense responses (Reddy et al, 1996).…”

Section: Introductionmentioning

confidence: 98%