4-METHYLUMBELLIFERYL BETA-D-N,N'-DIACETYL-CHITOBIOSIDE
4-METHYLUMBELLIFERYL BETA-D-N,N'-DIACETYL-CHITOBIOSIDE structure
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Common Name | 4-METHYLUMBELLIFERYL BETA-D-N,N'-DIACETYL-CHITOBIOSIDE | ||
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| CAS Number | 53643-12-2 | Molecular Weight | 582.55400 | |
| Density | 1.53g/cm3 | Boiling Point | 1000.7ºC at 760mmHg | |
| Molecular Formula | C26H34N2O13 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 559ºC | |
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Enhanced enzymatic hydrolysis of langostino shell chitin with mixtures of enzymes from bacterial and fungal sources.
Carbohydr. Res. 338(18) , 1823-33, (2003) 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%). T... |
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Bacterial chitin hydrolysis in two lakes with contrasting trophic statuses.
Appl. Environ. Microbiol. 78(3) , 695-704, (2012) Chitin, which is a biopolymer of the amino sugar glucosamine (GlcN), is highly abundant in aquatic ecosystems, and its degradation is assigned a key role in the recycling of carbon and nitrogen. In order to study the significance of chitin decomposition in tw... |
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Equilibrium and kinetic folding of pigeon lysozyme.
Biochemistry 37(19) , 6772-80, (1998) In the present study, the search for a possible intermediate state in pigeon lysozyme is addressed by equilibrium and kinetic experiments using static and stopped-flow fluorescence and circular dichroism spectroscopies. In equilibrium conditions at pH 7.5, pi... |
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Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes.
Biochemistry 33(17) , 5212-20, (1994) The refolding kinetics of hen lysozyme have been studied using a range of fluorescent probes. These experiments have provided new insight into the nature of intermediates detected in our recent hydrogen-exchange labeling studies [Radford, S.E., et al. (1992) ... |
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Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process.
J. Mol. Biol. 267(5) , 1068-74, (1997) The folding of lysozyme involves parallel events in which hydrogen exchange kinetics indicate the development of persistent structure at very different rates. We have monitored directly the kinetics of formation of the native molecule by the binding of a fluo... |
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Identification and characterization of the direct folding process of hen egg-white lysozyme.
Biochemistry 21(1) , 38-43, (1982) Refolding kinetics of hen egg-white lysozyme (HEWL) have been studied by means of the stopped-flow method with guanidinium chloride as the denaturant. We show here that the three-species model U1 in equilibrium or formed from U2 in equilibrium or formed from ... |
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Expression of chitinase-encoding genes in Bacillus thuringiensis and toxicity of engineered B. thuringiensis subsp. aizawai toward Lymantria dispar larvae.
Curr. Microbiol. 48(3) , 175-81, (2004) Chitinase genes from Aeromonas hydrophila and Bacillus circulans No.4.1 were cloned into the plasmid pHY300PLK and designated as pHYA2 and pHYB43, respectively. Both plasmids were introduced into various strains of B. thuringiensis by electroporation. Plasmid... |