Functional characteristics of lactobacilli from traditional Bulgarian fermented milk products.

After oral administration, probiotic lactobacilli meet a number of protection systems in the human body, such as exposure to gastric, pancreatic, and small intestinal juices. Overcoming these detrimental barriers allows living bacteria to adhere to the intestinal epithelium and permanently colonize the gastrointestinal tract (GIT), providing health benefits to the host. Based on this, the transit tolerance of 25 candidate probiotic lactobacilli from katak, yoghurt, and white-brined and yellow cheese to simulated bile and small intestinal juices of variable pH was investigated. To establish their resistance, in vitro model systems based on modified MRS media and a longer duration of action (up to 24 h of incubation) were designed. Six of the strains studied were found to show strain-specific survival capacity with low viability in conditions simulating stomach acidity and high resistance to bile and intestinal juices. In addition, the adherence capability (autoaggregation and hydrophobicity) of the strains was determined. Obtained results allowed to select Lactobacillus strains with high survival ratios while passing through the GIT and good adherence properties, which make them suitable for the development of new probiotics.

Characterization of a non-pigment producing Monascus purpureus mutant strain.

A characterization of a non-pigment producing mutant Monascus purpureus M12 compared with its parental strain Monascus purpureus Went CBS 109.07 has been performed aiming to investigate the relation between pigment biosynthesis and other characteristics of these fungi. A comparison has been made of morphological features, some physiological properties and biochemical activities of both strains. The albino mutant exhibits an anamorph life cycle, high conidia forming capability, slower radial growth rate and temperature sensitivity. The assimilation capacity of both strains for mono-, disaccharides and some alcohols is in the same range (Yx/c 0.2 - 0.35), while the red strain has a higher fermentation capacity. In a selected albino mutant, the growth rate, metabolic activity and capacity for production of typical for Monascus fungi secondary metabolites were reduced considerably. Hydrolytic activity towards natural substrates expressed through glucoamylase and protease was approximately 10 fold lower in the non pigment producing strain (0.05 - 0.08 U/mg protein and 0.01 - 0.07 U/mg protein respectively) compared with the red one. Important qualitative differences between both strains was found in fatty acid composition and in the production of citrinin and monacolin. The mutant strain possessed C17, C20 and C22 fatty acids and did not produce citrinin.

Superoxide dismutase during glucose repression of Hansenula polymorpha CBS 4732.

Hansenula polymorpha CBS 4732 was studied during cultivation on methanol and different glucose concentrations. Activities of Cu/Zn and Mn superoxide dismutase, catalase and methanol oxidase were investigated. During cultivation on methanol, increased superoxide dismutase and catalase activities and an induced methanol oxidase were achieved. Transfer of a methanol grown culture to medium with a high glucose concentration caused growth inhibition, low consumption of carbon, nitrogen and phosphate substrates, methanol oxidase inactivation as well as decrease of catalase activity (21.8 +/- 0.61 deltaE240 x min(-1) x mg protein(-1)). At the same time, a high value for superoxide dismutase enzyme was found (42.9 +/- 0.98 U x mg protein(-1), 25% of which was represented by Mn superoxide dismutase and 75% - by the Cu/Zn type). During derepression methanol oxidase was negligible (0.005 +/- 0.0001 U x mg protein(-1)), catalase tended to be the same as in the repressed culture, while superoxide dismutase activity increased considerably (63.67 +/- 1.72 U x mg protein(-1), 69% belonging to the Cu/Zn containing enzyme). Apparently, the cycle of growth inhibition and reactivation of Hansenula polymorpha CBS 4732 cells is strongly connected with the activity of the enzyme superoxide dismutase.