Two experiments were conducted to study the effect of supplemental 100 g/day of live Bacillus cultures (2 x 10(11) cell of Bacillus subtilis and Bacillus licheniformis) on rumen fermentation as well as milk yield and composition in Chinese Holstein cows. In experiment 1, investigating 3 x 10 cows, milk yield and milk protein were increased by using B. licheniformis (p < 0.05) in comparison with an unsupplemented group and the B. subtilis group. Body weight was not significantly affected by Bacillus culture supplementation (p > 0.05). Percentage of milk fat and lactose was not significantly different between treatments (p > 0.05). But milk protein increased with B. licheniformis supplementation (p < 0.05). In experiment 2, carried out with three non-lactating ruminally and duodenally fistulated cows, results showed that B. licheniformis supplementation increased microbial crude protein flow into duodenum (p < 0.05) and decreased the ammonia nitrogen concentration in ruminal fluid at 0.5 h, 1 h, 3 h, 6 h after morning feeding (p < 0.05). Bacillus licheniformis supplementation increased total VFA and acetate concentration in ruminal fluid at 0.5 h, 1 h, 3 h, 6 h after morning feeding (p < 0.05). Bacillus subtilis had no significant effect on rumen fermentation characteristics, duodenal microbial N flow and ruminal apparent nutrient digestibility (p > 0.05). Bacillus licheniformis increased ruminal apparent nutrient digestibility of neutral detergent fibre, acid detergent fibre, and organic matter (p < 0.05).

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Antimicrobial peptides represent ancient host defense effector molecules present in organisms across the evolutionary spectrum. Lots of antimicrobial peptides were synthesized based on well-known structural motif widely existed in a variety of lives. Leucine-rich repeats (LRRs) are sequence motifs present in over 60,000 proteins identified from viruses, bacteria, and eukaryotes. To elucidate if LRR motif possesses antimicrobial potency, two peptides containing one or two LRRs were designed. The biological activity and membrane-peptide interactions of the peptides were analyzed. The results showed that the tandem of two LRRs exhibited similar antibacterial activity and significantly weaker hemolytic activity against hRBCs than the well-known membrane active peptide melittin. The peptide with one LRR was defective at antimicrobial and hemolytic activity. The peptide containing two LRRs formed α-helical structure, respectively, in the presence of membrane-mimicking environment. LRR-2 retained strong resistance to cations, heat, and some proteolytic enzymes. The blue shifts of the peptides in two lipid systems correlated positively with their biological activities. Other membrane-peptide experiments further provide the evidence that the peptide with two LRRs kills bacteria via membrane-involving mechanism. The present study increases our new understanding of well-known LRR motif in antimicrobial potency and presents a potential strategy to develop novel antibacterial agents.

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