α-L-rhamnosidase from Penicillium tardum and Its Application for Biotransformation of Citrus Rhamnosides.

Enzymatic deramnosylation of flavonoids is a convenient tool for improving the quality of citrus juices. α-L-rhamnosidase with a specific activity of 33.1 units/mg was isolated and characterized from the culture liquid of Penicillium tardum.

Lipopolysaccharide of Pantoea agglomerans 7460: O-specific polysaccharide and lipid A structures and biological activity.

Lipopolysaccharide (LPS) was isolated from Pantoea agglomerans 7460 cells by phenol-water extraction. Mild acid degradation allowed to separate OPS and lipid A. Lipid A was analyzed by negative-ion mode ESI MS and found to consist mainly of hexaacylated derivative containing biphosphorylated GlcN disaccharide, four 14:0 (3-OH), 18:0 and 12:0 fatty acids.

Structure of O-Polysaccharide and Lipid A of 8488.

The 8488 lipopolysaccharide (LPS) was isolated, purified and characterized by monosaccharide and fatty acid analysis. The O-polysaccharide and lipid A components of the LPS were separated by mild acid degradation. Lipid A was studied by electrospray ionization mass spectrometry (ESI-MS) and found to consist of hexa-, penta-, tetra- and tri-acylated species.

Development and characterization of chitosan/polyvinyl alcohol polymer material with elastolytic and collagenolytic activities.

The biologically active polymeric material with entrapped peptidase Bacillus thuringiensis var. israelensis with caseinolytic, collagenase and elastase activities was developed as a promising product for medical use. We have evaluated and reported here the following physical-chemical and biochemical characteristics of entrapped enzyme: peptidase/polymer interaction and morphology analyses, film thickness, water content, time of dissolution in water and physiological saline, kinetic of casein hydrolysis and pH- and thermoprofiles of proteolytic activity.