Chitin

About: Chitin is a research topic. Over the lifetime, 6590 publications have been published within this topic receiving 253993 citations.

Exocellular chitinase from a Streptomyces sp.

Abstract: SUMMARY: A number of cultures of chitin-decomposing aerobic bacteria were isolated by the enrichment technique. Chitin decomposition was followed by measurement of loss of alkali-resistant insoluble substrate. Agitated submerged cultures secured a much more rapid breakdown of chitin than static cultures. The exocellular chitinase produced by a species of Streptomyces in agitated submerged culture was studied. The effects of pH value and substrate concentration on enzyme activity were examined and the results used to establish a chitinase assay in terms of reducing-sugar production. The enzyme was an inducible one (adaptive). The enzyme was concentrated by ultrafiltration and lyophilization. The water-soluble reducing materials produced by the enzyme from chitin were identified as N-acetylglucosamine and its corresponding disaccharide, N.N-diacetylchitobiose.

Detection and characterization of chitinases and other chitin-modifying enzymes

Abstract: Multiple industrial and medical uses of chitin and its derivatives have been developed in recent years. The demand for enzymes with new or desirable properties continues to grow as additional uses of chitin, chitooligosaccharides, and chitosan become apparent. Microorganisms, the primary degraders of chitin in the environment, are a rich source of valuable chitin-modifying enzymes. This review summarizes many methods that can be used to isolate and characterize chitin-modifying enzymes including chitin depolymerases, chitodextrinases, chitin deacetylases, N-acetylglucosaminidases, chitin-binding proteins, and chitosanases. Chitin analogs, zymography, detection of reducing sugars, genomic library screening, chitooligosaccharide electrophoresis, degenerate PCR primer design, thin layer chromatography, and chitin-binding assays are discussed.

The role of chitin in the decomposition of ectomycorrhizal fungal litter

Abstract: Ectomycorrhizal fungal tissues comprise a significant forest-litter pool. Ectomycorrhizal (EM) fungi may also influence the decomposition of other forest-litter components via competitive interactions with decomposer fungi and by ensheathing fine roots. Because of these direct and indirect effects of ectomycorrhizal fungi, the factors that control the decomposition of EM fungi will strongly control forest-litter decomposition as a whole and, thus, ecosystem nutrient and carbon cycling. Some have suggested that chitin, a component of fungal cell walls, reduces fungal tissue decomposition because it is relatively recalcitrant. We therefore examined the change in chitin concentrations of EM fungal tissues during decomposition. Our results show that chitin is not recalcitrant relative to other compounds in fungal tissues and that its concentration is positively related to the decomposition of fungal tissues. Variation existing among EM fungal isolates in chitin concentration suggests that EM fungal community structure influences C and nutrient cycling.

Properties of chitosanase from Bacillus cereus S1.

Abstract: Chitosanase from Bacillus cereus S1 was purified, and the enzymatic properties were investigated. The molecular weight was estimated to 45,000 on SDS-PAGE. Optimum pH was about 6, and stable pH in the incubation at 40°C for 60 min was 6–11. This chitosanase was stable in alkaline side. Optimum temperature was around 60°C, and enzyme activity was relatively stable below 60°C. The degradations of colloidal chitosan and carboxymethyl cellulose (CMC) were about 30 and 20% relative to the value of soluble chitosan, respectively, but colloidal chitin and crystalline cellulose were not almost hydrolyzed. On the other hand, S1 chitosanase adsorbed on colloidal chitin completely and by about 50% also on crystalline cellulose, in contrast to colloidal chitosan, which it did not adsorb. S1 chitosanase finally hydrolyzed 100% N-deacetylated chitosan (soluble state) to chitobiose (27.2%), chitotriose (40.6%), and chitotetraose (32.2%). In the hydrolysis of various chitooligosaccharides, chitobiose and chitotriose were not hydrolyzed, and chitotetraose was hydrolyzed to chitobiose. Chitobiose and chitotriose were released from chitopentaose and chitohexaose. From this specificity, it was hypothesized that the active site of S1 chitosanase recognized more than two glucosamine residues posited in both sides against splitting point for glucosamine polymer.