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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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Journal ArticleDOI
TL;DR: Chitinases are produced by Metarhizium anisopliae when it is grown in the presence of chitin and are purified by precipitation with ammonium sulphate, followed by anion-exchange chromatography on DEAE-Sephacel.
Abstract: Chitinases are produced by Metarhizium anisopliae when it is grown in the presence of chitin A chitinase from the culture filtrate of Metarhizium anisopliae was successively purified by precipitation with ammonium sulphate, followed by anion-exchange chromatography on DEAE-Sephacel The purified enzyme, which has a molecular mass of approximately 30 kDa by sodium dodecyl sulphate – polyacrylamide gel electrophoresis, catalyses the hydrolysis of p-nitrophenyl β-N-diacetylchitobiose with an apparent Km of 0537 mmol and Vmax of 486 nmol∙mL−1∙min−1 The optimum pH and temperature were 45–50 and 40–45 °C, respectivelyKey words: chitinases, Metarhizium anisopliae, enzyme purification, enzyme characterization

80 citations

Journal ArticleDOI
TL;DR: Finely powdered alpha- andbeta-chitin can be completely hydrolyzed with chitinase (EC 3.2.1.14) and beta-N-acetylhexosaminidase ( EC 3.1-2.52) for the production of 2-acetamido-2-deoxy-D-glucose (GlcNAc).

80 citations

Journal ArticleDOI
TL;DR: Results suggest that the E. invadens cyst wall forms when the plasma membrane galactose lectin binds sugars on Jacob, which in turn binds chitin via its five chit in-binding domains.
Abstract: The infectious stage of amebae is the chitin-walled cyst, which is resistant to stomach acids. In this study an extraordinarily abundant, encystation-specific glycoprotein (Jacob) was identified on two-dimensional protein gels of cyst walls purified from Entamoeba invadens. Jacob, which was acidic and had an apparent molecular mass of approximately 100 kDa, contained sugars that bound to concanavalin A and ricin. The jacob gene encoded a 45-kDa protein with a ladder-like series of five Cys-rich domains. These Cys-rich domains were reminiscent of but not homologous to the Cys-rich chitin-binding domains of insect chitinases and peritrophic matrix proteins that surround the food bolus in the insect gut. Jacob bound purified chitin and chitin remaining in sodium dodecyl sulfate-treated cyst walls. Conversely, the E. histolytica plasma membrane Gal/GalNAc lectin bound sugars of intact cyst walls and purified Jacob. In the presence of galactose, E. invadens formed wall-less cysts, which were quadranucleate and contained Jacob and chitinase (another encystation-specific protein) in secretory vesicles. A galactose lectin was found to be present on the surface of wall-less cysts, which phagocytosed bacteria and mucin-coated beads. These results suggest that the E. invadens cyst wall forms when the plasma membrane galactose lectin binds sugars on Jacob, which in turn binds chitin via its five chitin-binding domains.

80 citations

Journal ArticleDOI
TL;DR: One major additional band with chitinase activity could be detected in Allium porrum (leek) root extracts after colonization by Glomus versiforme or GlomUS intraradix when compared to control root extracts by using a two-dimensional polyacrylamide gel electrophoresis (PAGE) system.

80 citations

Journal ArticleDOI
TL;DR: Although the exact function of CHI3L1 in inflammation and cancer is still largely unknown, CHI 3L1 plays a pivotal role in exacerbating the inflammatory processes and in promoting angiogenesis and remodeling of the extracellular matrix.
Abstract: The family of mammalian chitinases includes members both with and without glycohydrolase enzymatic activity against chitin, a polymer of N-acetylglucosamine. Chitin is the structural component of fungi, crustaceans, insects and parasitic nematodes, but is completely absent in mammals. Exposure to antigens containing chitin- or chitin-like structures sometimes induces strong T helper type-I responses in mammals, which may be associated with the induction of mammalian chitinases. Chitinase 3-like-1 (CHI3L1), a member of the mammalian chitinase family, is induced specifically during the course of inflammation in such disorders as inflammatory bowel disease, hepatitis and asthma. In addition, CHI3L1 is expressed and secreted by several types of solid tumors including glioblastoma, colon cancer, breast cancer and malignant melanoma. Although the exact function of CHI3L1 in inflammation and cancer is still largely unknown, CHI3L1 plays a pivotal role in exacerbating the inflammatory processes and in promoting angiogenesis and remodeling of the extracellular matrix. CHI3L1 may be highly involved in the chronic engagement of inflammation which potentiates development of epithelial tumorigenesis presumably by activating the mitogen-activated protein kinase and the protein kinase B signaling pathways. Anti-CHI3L1 antibodies or pan-chitinase inhibitors may have the potential to suppress CHI3L1-mediated chronic inflammation and the subsequent carcinogenic change in epithelial cells.

80 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023186
2022337
2021148
2020172
2019154
2018152