Anti-obesity effects of potential probiotic Lactobacillus strains isolated from Mongolian fermented dairy products in high-fat diet-induced obese rodent model.

This study aims to investigate the anti-obesity properties of lactic acid bacteria (LAB) isolated from fermented dairy products such as "Airag" and "Khoormog" in Mongolia. These traditional dairy products are widely used in Mongolia and believe in having potential probiotic, anti-diabetes, anti-cancer, and anti-tuberculosis properties and are made from unheated two-humped camel milk and mare milk, respectively. We chose three LAB strains based on their probiotic characteristics, including tolerance of gastric and bile acids. Then we checked the anti-obesity activity of probiotic strains in vivo. An animal model was evaluated in twenty male C57BL/6J mice by inducing obesity with a high-fat diet (HFD), which was divided into five groups: regular diet group (Negative control), HFD group (Positive control), HFD with Lacticaseibacillus paracasei X-1 (X-1), Lacticaseibacillus paracasei X-17 (X-17), and Limosilactobacillus fermentum BM-325 (BM-325). For six weeks, 5 × 109 colony-forming units (CFU) of bacteria were given orally to the LAB-fed groups. Fasting blood glucose (FBG), lipid profiles, organ index, and organ morphology were all measured. The probiotic strains suppressed growth in adipose cell volume, stabilized FBG, reduced liver cell degeneration, and slowed HFD-induced body weight gain. The results suggest that some strains increase general metabolism while lowering body weight.

N-glycans in Toxicodendron vernicifluum lacquer laccase.

The N-glycans in Toxicodendron vernicifluum (Rhus vernicifera) lacquer laccase was elucidated for the first time through a combination of enzymatic digestion and subsequent mass spectrometry measurements using LC-MS/MS and MALDI-TOF MS. Lacquer laccase was isolated from a Japanese lacquer acetone powder from consecutive Sephadex C-50 and DEAE A-50 column chromatography. Trypsin and chymotrypsin digestions of the lacquer laccase resulted in a mixture of peptides and N-glycopeptides, which were treated with peptide-N-glycosidases and then Nα-(aminooxyacetyl)tryptophanylarginine methyl ester (aoWR) to give the aoWR-labelled N-glycans. The MS measurements revealed that GlcNAc4Hex5Fuc3Xyl1 N-glycan was attached at 12 N-glycosylation sites (Asn 5, 14, 180, 194, 233, 274, 284, 347, 364, 381, 398, and 519), GlcNAc3Hex4Fuc2Xyl1 N-glycan at two sites (Asn 124 and 454), and GlcNAc3Hex6Fuc1Xyl1 N-glycan at one site (Asn 28). A database search (Mascot search) of the peptides also suggested the presence of N-glycans at the 15 potential N-glycosylation sites (Asn-X-Ser/Thr).

Analysis of interaction between sulfated polysaccharides and HIV oligopeptides by surface plasmon resonance.

This study aims to quantitatively investigate the interaction between sulfated polysaccharides with potent anti-HIV activity, dextran and curdlan sulfates with negatively charged sulfate groups, and poly-L-lysine as a model protein and oligopeptides from a HIV surface glycoprotein gp120 with positively charged amino acids using surface plasmon resonance (SPR) and dynamic light scattering (DLS) to elucidate the anti-HIV mechanism of sulfated polysaccharides. The apparent association- (ka) and dissociation rate (kd) constants of dextran and curdlan sulfates against poly-L-lysine were ka = 6.92 × 104-2.17 × 106 1/Ms and kd = 4.29 × 10-5-2.22 × 10-4 1/s; these kinetic constants were dependent on the molecular weights and degree of sulfation of sulfated polysaccharides. For interaction, the three oligopeptides from the HIV gp120 were peptide A 297TRPNNNTRKRIRIQRGPGRA316 with several lysine (K) and arginine (R) in the V3 loop region, peptide B 493PLGVAPTKAKRRVVQREKR511 with several K and R in the C-terminus region, and oligopeptide C 362KQSSGGDPEIVTHSFNCGG380 with few basic amino acids in the CD4 binding domain. Sulfated polysaccharides exhibited strong interaction against oligopeptides A and B, (ka = 5.48 × 104-2.96 × 106 1/Ms. and kd = 1.74 × 10-4-6.24 × 10-3 1/s), no interaction was noted against oligopeptide C. Moreover, the particle size and zeta potential by DLS indicated the interaction between sulfated polysaccharides and oligopeptides A and B, suggesting the anti-HIV mechanism of sulfated polysaccharides to be the electrostatic interaction of negatively charged sulfated polysaccharides and HIV at the positively charged amino acid regions.