hymecromone has been researched along with chitotriose* in 2 studies
2 other study(ies) available for hymecromone and chitotriose
| Article | Year |
|---|---|
Enhanced enzymatic hydrolysis of langostino shell chitin with mixtures of enzymes from bacterial and fungal sources.
A combination of enzyme preparations from Trichoderma atroviride and Serratia marcescens was able to completely degrade high concentrations (100 g/L) of chitin from langostino crab shells to N-acetylglucosamine (78%), glucosamine (2%), and chitobiose (10%). The result was achieved at 32 degrees C in 12 days with no pre-treatment (size reduction or swelling) of the substrate and without removal of the inhibitory end-products from the mixture. Enzymatic degradation of three forms of chitin by Serratia/Trichoderma and Streptomyces/Trichoderma blends was carried out according to a simplex-lattice mixture design. Fitted polynomial models indicated that there was synergy between prokaryotic and fungal enzymes for both hydrolysis of crab chitin and reduction of turbidity of colloidal chitin (primarily endo-type activity). Prokaryotic/fungal enzymes were not synergistic in degrading chitosan. Enzymes from prokaryotic sources had much lower activity against chitosan than enzymes from T. atroviride. Topics: Acetylglucosamine; Animals; beta-N-Acetylhexosaminidases; Brachyura; Chitin; Chitinases; Chitosan; Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Colloids; Complex Mixtures; Disaccharides; Glucosamine; Hydrolysis; Hymecromone; Kinetics; Nephelometry and Turbidimetry; Oligosaccharides; Serratia marcescens; Streptomyces; Substrate Specificity; Trichoderma; Trisaccharides | 2003 |
Identification and partial characterization of three chitinase forms in Entamoeba invadens with emphasis on their inhibition by allosamidin.
Three chitinase forms were identified in Entamoeba invadens cysts following fractionation of a soluble fraction by anionic exchange, size exclusion and hydroxyapatite adsorption chromatographies. The enzymes, named here as A, B and B', showed molecular weights of 64, 33.4 and 33.4 kDa, respectively, as measured by gel filtration. Comparison of their levels of specific activity in partially purified samples revealed chitinase A as the major species. Chitinase B' was a minor component of the chitinolytic complex. Whereas some properties were common to the three forms, analysis of other parameters revealed significant catalytic site-related differences. Accordingly, the three chitinases hydrolyzed the fluorogenic substrate 4-methylumbelliferyl chitotriose with typical Michaelian kinetics and Km values of 4.5, 11.8 and 3.8 microM for A, B and B', respectively. Allosamidin strongly inhibited the three enzyme forms with different kinetics. Dixon plots revealed competitive-type inhibition and Ki values of 10.0, 2.3 and 10.8 nM for A, B and B', respectively. Km/Ki ratios indicated 450-, 350- and 5130-fold higher affinity for the inhibitor over the substrate for the A, B and B' forms, respectively. Results are discussed in terms of the possibility that the three chitinase species correspond to different enzyme proteins. Topics: Acetylglucosamine; Animals; Chitin; Chitinases; Chromatography, Gel; Chromatography, Ion Exchange; Durapatite; Entamoeba; Enzyme Inhibitors; Glycosides; Hymecromone; Isoenzymes; Molecular Weight; Trisaccharides | 1996 |