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Chitin
About: Chitin is a research topic. Over the lifetime, 6590 publications have been published within this topic receiving 253993 citations.
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TL;DR: Chitin, a homopolymer of N-acetylglucosamine, is obtained from a variety of sources and forms the structural component of fungal cell wall and plants.
Abstract: Chitin, a homopolymer of N-acetylglucosamine, is obtained from a variety of sources. They form the structural component of fungal cell wall and plants. They are commercially obtained from shrimp and crab shell waste from the fishing industry. Recent advances in understanding the structure and properties of chitin and its derivatives has opened a lot of new avenues for its applications. Improvements in the properties of chitin for a particular application can be easily brought about by chemical modifications. The applicability of chitin in many areas and its easy manipulation has resulted in a considerable amount of research being done on the possible applications of chitinase.
184 citations
TL;DR: The first evidence for direct binding of LysM RLK1 to chitin is presented and it is suggested that LysMRLK1 has a higher affinity for chit in having a longer residue of N-acetyl glucosamine.
184 citations
TL;DR: In this article, the brown color of chitin from cicada sloughs was removed using 6% sodium hypochlorite as an oxidizing agent, and the degree of acetylation (DA) was determined by elemental analysis (EA), attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR), proton nuclear magnetic resonance (1 H NMR), solid-state 13 C cross-polarization magic-angle-spinning nuclear Magnetic Resonance (CP/MAS) NMR spectroscope,
183 citations
TL;DR: It is proposed that the increased cross-linking of cell wall proteins via beta1,6-glucan to chitin represents a cell wall repair mechanism in yeast, which is activated in response to cell wall weakening.
Abstract: The yeast cell wall contains beta1,3-glucanase-extractable and beta1,3-glucanase-resistant mannoproteins. The beta1,3-glucanase-extractable proteins are retained in the cell wall by attachment to a beta1,6-glucan moiety, which in its turn is linked to beta1,3-glucan (J. C. Kapteyn, R. C. Montijn, E. Vink, J. De La Cruz, A. Llobell, J. E. Douwes, H. Shimoi, P. N. Lipke, and F. M. Klis, Glycobiology 6:337-345, 1996). The beta1,3-glucanase-resistant protein fraction could be largely released by exochitinase treatment and contained the same set of beta1,6-glucosylated proteins, including Cwp1p, as the B1,3-glucanase-extractable fraction. Chitin was linked to the proteins in the beta1,3-glucanase-resistant fraction through a beta1,6-glucan moiety. In wild-type cell walls, the beta1,3-glucanase-resistant protein fraction represented only 1 to 2% of the covalently linked cell wall proteins, whereas in cell walls of fks1 and gas1 deletion strains, which contain much less beta1,3-glucan but more chitin, beta1,3-glucanase-resistant proteins represented about 40% of the total. We propose that the increased cross-linking of cell wall proteins via beta1,6-glucan to chitin represents a cell wall repair mechanism in yeast, which is activated in response to cell wall weakening.
183 citations
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TL;DR: There is only a weak bonding between the chitin and the water-soluble cuticular protein, and an increase to pH 9 is necessary before all the adsorbed protein can be removed.
Abstract: The effects of pH, salt concentration, and temperature on the adsorption of a water-soluble insect cuticular protein to chitin have been investigated. The adsorption is dependent upon pH, decreasing rapidly as the pH increases from the region of the isoelectric point of the protein. Increase in salt concentration decreases adsorption but the adsorption appears to be little influenced by changes in temperature. Tyrosine-rich protein fractions are preferentially adsorbed. The adsorption is partly irreversible and an increase to pH 9 is necessary before all the adsorbed protein can be removed. It is concluded that there is only a weak bonding between the chitin and the water-soluble cuticular protein.
183 citations