Biotechnology and applied biochemistry, 17 ( Pt 1), 49-55 (1993-02-01)
beta-Glucosidase from Penicillium funiculosum was immobilized on nylon powder previously activated with triethyloxonium tetrafluoroborate, 1,2-diaminoethane and glutaraldehyde. The activation of the nylon powder and the immobilization processes were studied and optimized for the enzyme and the matrix. A high activity
Treatment of trypsin with triethyloxonium tetrafluoroborate at pH 8, 25 degrees C, results in abolition of binding to the enzyme of specific cationic substrates and inhibitors. The binding constant of soybean trypsin inhibitor to ethylated trypsin is 10000-fold smaller than
The alkylation of nitrite and nitrate by triethyloxonium tetrafluoroborate allows determination of their ethyl esters by headspace gas chromatography/mass spectrometry (GC/MS). In the present study, significant improvement in analytical performance is achieved using negative chemical ionization providing detection limits of
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