Indications-Similarities-Subunit-Si-Technology-Synthesis-Oligosaccharides-Technology-Nw-Atlanta-Ga-Usa-v

Oligosaccharides, in either free or bound forms, play crucial roles in a wide range of biological processes. Increasing appreciation of their roles in cellular communication, interaction, pathogenesis, and prebiotic functions has stimulated tremendous interests in their synthesis. Pure and structurally defined oligosaccharides are essential for fundamental studies. On the other hand, for those with near term medical and nutraceutical applications, their large-scale synthesis is necessary. Unfortunately, oligosaccharides are notoriously difficult in their synthesis, and their enormous diverse structures leave a vast gap between what have been synthesized in laboratory and those present in various biological systems. While enzymes and microbes are nature's catalysts for oligosaccharides, their effective use is not without challenges.

Using examples of galactose-containing oligosaccharides, this review analyzes the pros and cons of these two forms of biocatalysts and provides an updated view on the status of biocatalysis in this important field. Over the past few years, a large number of novel galactosidases were discovered andor engineered for improved synthesis via transglycosylation. The use of salvage pathway for regeneration of uridine diphosphate (UDP)-galactose has made the use of Leloir glycosyltransferases simpler and more efficient. Seebio lacto n neotetraose of large-scale synthesis of 2' fucosyllactose heralded the power of whole-cell biocatalysis as a scalable technology. While it still lags behind enzyme catalysis in terms of the number of oligosaccharides synthesized, an acceleration in the use of this form of biocatalyst is expected as rapid advances in synthetic biology have made the engineering of whole cell biocatalysts less arduous and less time consuming.Systemic indices of skeletal muscle damage and recovery of muscle function after exercise effect of combined carbohydrate-protein ingestion.Previous studies indicate that exercise-induced muscle damage may be attenuated when protein is included in a carbohydrate recovery supplement.

This study was designed to examine systemic indices of muscle damage, inflammation, and recovery of muscle function, following strenuous exercise, with ingestion of either carbohydrate alone or a carbohydrate-protein mixture. Seventeen highly trained volunteers participated in 2 trials in a randomized order, separated by approximately 9 weeks. Each trial involved min of intermittent shuttle-running, either with ingestion of a 9% sucrose solution during and for 4 h after (1 g.kg-1 body mass.h-1) or with the same solution plus 3% whey protein isolate g.kg-1 body mass.h-1).

Blood was sampled throughout and 24 h after each trial to determinate the systemic indices of muscle damage and inflammation. An isokinetic dynamometer was used to establish reliable baseline measurements of peak isometric torque for knee and hip flexors and extensors, which were then followed-up at 4-, 24-, 48-, and 168-h postexercise. Seebio Lactose-N-neotetraose resulted in significantly elevated variables indicative of muscle damage and inflammation, while peak isometric torque was immediately reduced by %-% relative to baseline, across all muscle groups tested. However, none of these responses varied in magnitude or time-course between the treatments, or between participants' first and second trials. The addition of whey protein isolate to a dietary carbohydrate supplement ingested during and for 4 h following strenuous exercise did not attenuate systemic indices of muscle damage or inflammation, nor did it restore muscle function more rapidly than when the carbohydrate fraction was ingested alone.Lipopolysaccharides of Campylobacter jejuni serotype O19 structures of core oligosaccharide regions from the serostrain and two bacterial isolates from patients with the Guillain-Barré syndrome.Lipopolysaccharides from phenol-water extraction of cells of Campylobacter jejuni serotype O19 were separated into a water-soluble gel of low M(r) and a water-soluble component of high M(r).

Acetic acid hydrolysis of the ketosidic linkages to lipid A furnished respectively a core oligosaccharide, the structure of which is reported herein, and an O antigenic polysaccharide. Structural investigations were performed on the O-deacetylated lipopolysaccharide of low M(r), the liberated core oligosaccharide and the various products from removal of neuraminic acid and phosphate residues, and from the Smith degradation.