N,N,N‐trimethylchitosan (TMC) was prepared by reacting purified chitosan with iodomethane, in the presence of sodium hydroxide, water and sodium iodide, at room temperature. The reaction medium was N‐methyl‐2‐pyrrolidone. Different samples of TMC were obtained by adding to the reaction medium a fixed volume (5.5 mL) of aqueous NaOH solutions at different concentrations (15, 20, 30 and 40 wt.‐%) and carrying out the reactions for 9 or 24 h. The features observed in the 1H and 13C NMR spectra of these chitosan derivatives, in respect of the chemical shift, number and relative intensity of the signals, depended strongly on the excess of NaOH and H3CI added to the reaction medium, but when the lowest excess was employed, the characteristics of the derivative were not affected by the reaction time to the same extent. The average degree of quaternization of these N‐methylated derivatives of chitosan ranged from 10.5% to 44.8%, according to the reaction conditions. Increasing the excess of NaOH, in reactions carried out for 9 h, resulted in TMC samples with progressively higher content of trimethylated sites however, the reaction yields were correspondingly lower and O‐alkylation was favored in these cases.
1H NMR spectrum of sample [AX]24h dissolved in D2O (Cp = 10 g/L). 相似文献
A systematic investigation of the parameters that affect the efficiency of immobilizing heparinase onto cyanogen bromide activated
crosslinked 8% agarose beads was conducted. Two experimental measures, the “fraction bound” and the “fraction retained,” were
used to monitor the coupling efficiency. The fraction bound is the portion of the total initial enzyme that is bound to the
agarose gel. The fraction retained is the fraction of bound enzyme that is active. The product of the two measures indicates
the coupling efficiency. The activity of the immobilized heparinase was measured under conditions free of both internal and
external mass transfer limitations, and thus, the fraction retained represents the true immobilized enzyme activity.
Increasing the degree of activation of the beads results in an increase in the fraction bound, the fraction retained, and
consequently, the coupling efficiency. As the ratio of enzyme solution to gel volume increases from 1.5 to 2.2, the fraction
bound remains constant but the fraction retained decreases (heparinase concentration; 0.15 mg/mL and degree of activation;
9.5 μmol of cyanate esters/g of gel). At volume ratios greater than 2.2, both the fraction bound and the fraction retained
decline continuously. Changing the heparinase concentration in the coupling solution changes the coupling efficiency in a
manner similar to that of the volume ratio change.
When heparin is added during the coupling process, the fraction bound declines as the heparin concentration increases, whereas
the fraction retained increases up to a heparin concentration of 12 mg/mL and decreases thereafter. When arginine, lysine,
and glycine are used to block the unreacted cyanate ester groups after the coupling process, the immobilized heparinase shows
different pH optima of 6.5, 6.9, and 7.2, respectively. Based upon these findings, a protocol to optimize heparinase immobilization
is developed. 相似文献
The overall stability constantsK1 andK2 of NdNO
32+
and Nd(NO3)
2+
complexes were determined (K1=1.77;K2=1.28) using an extraction method with tri-n-butyl phosphate as the extractant. The ratio 1/2 of the stepwise stability constants is discussed. It was established that the Nd(NO3)
2+
complex was an outer-sphere ion pair.
Die Assoziation von Nitrat-Ion mit Nd3+
Zusammenfassung Mittels einer Extraktionsmethode wurden die StabilitätskonstantenK1 undK2 von NdNO
32+
- und Nd(NO3)+-Komplexen bestimmt (K1=1.77;K2=1.28; Tri-n-butylphosphat als Extraktionsmittel). Das Verhältnis 1/2 der stufenweisen Stabilitätskonstanten wird diskutiert. Es stellte sich heraus, daß der Nd(NO3)+-Komplex als ein Outer-Shere-Ionenpaar vorliegt.
