Analysis of free radical production capacity in mouse faeces and its possible application in evaluating the intestinal environment: a pilot study.

Complex interplay between the intestinal environment and the host has attracted considerable attention and has been well studied with respect to the gut microbiome and metabolome. Oxygen free radicals such as superoxide and the hydroxyl radical (OH) are generated during normal cellular metabolism. They are toxic to both eukaryotic and prokaryotic cells and might thus affect intestinal homeostasis.

Effects of oral intake of heat-killed SBC8803 (SBL88™) on dry skin conditions: A randomized, double-blind, placebo-controlled study.

Lactobacilli are important in intestinal homeostasis, which involves the regulation of immune function, digestive health, cholesterol absorption and intestinal tumor growth amongst others. Our previous investigations have suggested that oral intake of heat-killed () SBC8803 (SBL88™) suppresses dermatitis by modulating the immune function in an atopic dermatitis mouse model. The aim of the present study was to investigate the effect of heat-killed SBC8803 intake on skin hydration conditions in humans.

A Lactobacillus mutant capable of accumulating long-chain polyphosphates that enhance intestinal barrier function.

Inorganic polyphosphate (polyP) was previously identified as a probiotic-derived substance that enhances intestinal barrier function. PolyP-accumulating bacteria are expected to have beneficial effects on the human gastrointestinal tract. In this study, we selected Lactobacillus paracasei JCM 1163 as a strain with the potential to accumulate polyP, because among the probiotic bacteria stored in our laboratory, it had the largest amount of polyP.

Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus.

Although the latter portion of lysine biosynthesis, the conversion of alpha-aminoadipate (AAA) to lysine, in Thermus thermophilus is similar to the latter portion of arginine biosynthesis, enzymes homologous to ArgA and ArgJ are absent from the lysine pathway. Because ArgA and ArgJ are known to modify the amino group of glutamate to avoid intramolecular cyclization of intermediates, their absence suggests that the pathway includes an alternative N-modification system. We reconstituted the conversion of AAA to lysine and found that the amino group of AAA is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW; that the side chain of AAA is converted to the lysyl side chain while still attached to LysW; and that lysine is subsequently liberated from the LysW-lysine fusion.