Physicochemical characteristics of a thermostable gellan lyase from Geobacillus stearothermophilus 98.

A purified thermostable gellan lyase, produced by a thermophilic bacterium, Geobacillus stearothermophilus 98, was characterized in relation to its physicochemical properties. The gellan lyase was established to have a molecular weight of 216 kDa, defined by capillary gel electrophoresis. Amino acid analysis revealed high quantities of Lys, His, Ala, Val, Ile, Glx, and Pro residues.

Stabilization of neutral NH2-R-COOH form of the antihypertensive peptides L-Valyl-L-Prolyl-L-Proline and L-Isoleucyl-L-Prolyl-L-Proline.

Spectroscopic and structural elucidation of the peptides L-Valyl-L-Prolyl-L-Proline (1) and L-Isoleucyl-L-Prolyl-L-Proline (2) are reported on the basis of experimental linear-polarized IR-spectroscopy in solid-state, 1H-NMR data and DFT. Curiously, the experimental data shown that both peptides stabilized in solution and in solid-state neutral H2N-R-COOH form. Conformational analysis made, shown two strong intramolecular NH2-O=C-N(Amide) and O=C-OH-NH2 hydrogen bonds with lengths of 2.

Anti-platelet fraction from Galega officinalis L. inhibits platelet aggregation.

A fraction from crude extract of Galega officinalis L. was purified by gel filtration on Sephadex G-25, Sepharose 4B, and ion-exchange chromatography on diethylaminoethyl (DEAE)-cellulose. The fraction with molecular weight 100-140 kDa appears to have a polysaccharide nature, including protein.