3.2.1.14

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Showing 1-11 of 11 results for "3.2.1.14 " within Papers

Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases.

M Legrand et al.

Proceedings of the National Academy of Sciences of the United States of America, 84(19), 6750-6754 (1987-10-01)

Four endochitinases (poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase, EC 3.2.1.14) have been purified from leaves of Nicotiana tabacum cv. Samsun NN reacting hypersensitively to tobacco mosaic virus. Two of them are acidic proteins of molecular weights 27,500 and 28,500 and have been identified as

Detection and quantification of N-acetyl-beta-D-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels.

A Tronsmo et al.

Analytical biochemistry, 208(1), 74-79 (1993-01-01)

Procedures are described for the direct assay of N-acetyl-beta-glucosaminidase (EC 3.2.1.30), chitobiosidase, and endochitinase (EC 3.2.1.14) after separation on starch or polyacrylamide electrophoresis gels. The enzymes were visualized as fluorescent bands by using an agarose overlay containing 4-methylumbelliferyl derivatives of

Identification and characterization of acidic mammalian chitinase inhibitors.

Derek C Cole et al.

Journal of medicinal chemistry, 53(16), 6122-6128 (2010-07-30)

Acidic mammalian chitinase (AMCase) is a member of the glycosyl hydrolase 18 family (EC 3.2.1.14) that has been implicated in the pathophysiology of allergic airway disease such as asthma. Small molecule inhibitors of AMCase were identified using a combination of

Comparative biocontrol ability of chitinases from bacteria and recombinant chitinases from the thermophilic fungus Thermomyces lanuginosus.

Ruth Nyanduko Okongo et al.

Journal of bioscience and bioengineering, 127(6), 663-671 (2019-01-24)

Microbial chitinases (EC 3.2.1.14) are known to hydrolyse the chitinous gut epithelium of insects and cell walls of many fungi. In this study, seven chitinases from different bacteria and fungi were produced, characterized and their biocontrol abilities against graminaceous stem

Biotechnological aspects of chitinolytic enzymes: a review.

Neetu Dahiya et al.

Applied microbiology and biotechnology, 71(6), 773-782 (2005-10-27)

Chitin and chitinases (EC 3.2.1.14) have an immense potential. Chitinolytic enzymes have wide-ranging applications such as preparation of pharmaceutically important chitooligosaccharides and N-acetyl D-glucosamine, preparation of single-cell protein, isolation of protoplasts from fungi and yeast, control of pathogenic fungi, treatment

Trichoderma viride induces pathogenesis related defense response against rot pathogen infection in groundnut (Arachis hypogaea L.).

H P Gajera et al.

Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 34, 314-325 (2015-07-15)

The study examine induction of defense enzymes involved in phenylpropanoid pathway and accumulation of pathogenesis related proteins in rot pathogen (Aspergillus niger Van Tieghem) challenged groundnut seedlings in response to Trichoderma viride JAU60. Seeds of five groundnut varieties differing in

Chitinases: biomarkers for human diseases.

Shou-Ping Guan et al.

Protein and peptide letters, 16(5), 490-498 (2009-05-16)

Human chitinases (EC.3.2.1.14) are classified into family 18 of glycosyl hydrolase (GH18) superfamily based on their amino acid sequence similarities. Active chitinase hydrolyzes chitin, a beta-1,4-linked N-acetyl-D-glucosamine oligosaccharide. Chitin is a major structural component of the insect exoskeletons and fungal

Leishmania donovani: expression and characterization of Escherichia coli-expressed recombinant chitinase LdCHT1.

A Razek-Desouky et al.

Experimental parasitology, 99(4), 220-225 (2002-03-13)

Leishmania parasites produce chitinase activity (EC. 3.2.1.14) thought to be important in parasite-sandfly interactions and transmission of the parasite to the vertebrate host. Previous observations have suggested that parasite chitinases are involved in degradation of the sandfly peritrophic matrix and

Kinetic characterization of Aspergillus niger chitinase CfcI using a HPAEC-PAD method for native chitin oligosaccharides.

Jolanda M van Munster et al.

Carbohydrate research, 407, 73-78 (2015-02-28)

The abundant polymer chitin can be degraded by chitinases (EC 3.2.1.14) and β-N-acetyl-hexosaminidases (EC 3.2.1.52) to oligosaccharides and N-acetyl-glucosamine (GlcNAc) monomers. Kinetic characterization of these enzymes requires product quantification by an assay method with a low detection limit, preferably compatible

Characterization of two novel bacterial type A exo-chitobiose hydrolases having C-terminal 5/12-type carbohydrate-binding modules.

Shariza B Jamek et al.

Applied microbiology and biotechnology, 101(11), 4533-4546 (2017-03-11)

Type A chitinases (EC 3.2.1.14), GH family 18, attack chitin ((1 → 4)-2-acetamido-2-deoxy-β-D-glucan) and chito-oligosaccharides from the reducing end to catalyze release of chitobiose (N,N'-diacetylchitobiose) via hydrolytic cleavage of N-acetyl-β-D-glucosaminide (1 → 4)-β-linkages and are thus "exo-chitobiose hydrolases." In this study, the chitinase type

Purification of several bacteriolytic enzymes by affinity chromatography on lysozyme-lysate of Micrococcus lysodeikticus cell wall coupled with sepharose.

T Yoshimoto et al.

Journal of biochemistry, 78(2), 253-259 (1975-08-01)

Using lysozyme-lysate of Micrococcus lysodeikticus cell wall coupled with Sepharose, several bacteriolytic enzymes were purified from crude preparations of animal and microbial origin. Quail egg-white, human milk and salivary lysozymes [EC 3.2.1.17] were adsorbed onto the adsorbent at pH 5-7

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