Coeliac disease (CD) is an inflammatory disorder of the small intestine. It includes aberrant adaptive immunity with presentation of CD toxic gluten peptides by HLA-DQ2 or DQ8 molecules to gluten-sensitive T cells. A ω-gliadin/C-hordein peptide (QPFPQPEQPFPW) and a rye-derived secalin peptide (QPFPQPQQPIPQ) were proposed to be toxic in CD, as they yielded positive responses when assessed with peripheral blood T-cell clones derived from individuals with CD. We sought to assess the immunogenicity of the candidate peptides using gluten-sensitive T-cell lines obtained from CD small intestinal biopsies. We also sought to investigate the potential cross-reactivity of wheat gluten-sensitive T-cell lines with peptic-tryptic digested barley hordein (PTH) and rye secalin (PTS). Synthesised candidate peptides were deamidated with tissue transglutaminase (tTG). Gluten-sensitive T-cell lines were generated by culturing small intestinal biopsies from CD patients with peptic-tryptic gluten (PTG), PTH or PTS, along with autologous PBMCs for antigen presentation. The stimulation indices were determined by measuring the relative cellular proliferation via incorporation of H-thymidine. The majority of T-cell lines reacted to the peptides studied. There was also cross-reactivity between wheat gluten-sensitive T-cell lines and the hordein, gliadin and secalin peptides. PTH, PTS, barley hordein and rye secalin-derived CD antigen-sensitive T-cell lines showed positive stimulation with PTG. ω-gliadin/C-hordein peptide and rye-derived peptide are immunogenic to gluten-sensitive T-cell lines and potentially present in wheat, rye and barley. Additional CD toxic peptides may be shared.

Introduction: Andrographis paniculata, Tinospora crispa and Centella asiatica are known to have various pharmacological functions. This research was carried out to investigate the antibacterial activities of protein extracts from A. paniculata, T. crispa and C. asiatica. Methods: Total soluble proteins from these herbs were extracted using a modified TCA/acetone method. The protein extracts were then quantified using the Bradford assay and separated using SDS-PAGE. The antibacterial activities were determined by disc diffusion method. Results: T. crispa had a significantly higher amount of proteins (83.86 ± 0.4 µg/µl) compared to A. paniculata (81.57 ± 0.4 µg/µl) and C. asiatica (78.93 ± 0.5 µg/µl). The proteins separated by SDS-PAGE were ranged from 30kDa to 260kDa, 25kDa to 110kDa and 25kDa to 160kDa for A. paniculata, T. crispa and C. Asiatic, respectively. The high abundance proteins were observed in A. paniculata and T. crispa but not in C. asitica. Protein extracts from C. asiatica have demonstrated antibacterial activity against all tested bacteria with the diameter of inhibition zone of 11.0 ± 0.5 mm, 12.3 ± 0.6 mm, 10.7 ± 0.7 mm and 20.0 ± 0.8 mm against B. cereus, S. aureus, K. pneumonia and S. typhimurium respectively. Meanwhile, protein extracts of A. paniculata showed a positive antibacterial activity only against B.cereus (13.7 ± 0.4 mm), S. aureus (7.0 ± 0.8 mm) and S. typhimurium (11.5 ± 0.3 mm). Protein extracts from T. crispa only showed a positive antibacterial activity against B. cereus (9.7 ± 0.5 mm). Conclusions: There is a constant need in the discovery of new antibiotics for the treatment of infectious diseases.

Introduction: The collagen can be basically extracted by chemical and enzymatic hydrolysis. In industry, the chemical hydrolysis method is more commonly used. However, the enzymatic hydrolysis is more effective when the high nutritional value product will be produces based on the extracted material. Chicken (Gallus gallus domesticus) feet are used as a source of bird collagen. Methods: Optimization of collagen extraction was investigated by using three different methods which were soaked in 5% lactic acid for 36 hours, 0.5 mol/L acetic acid with 0.1% papain and 0.5 mol/L acetic acid with 0.1% bromelain. Various properties such as percentage of end yield, concentration of protein, pH, swelling percentage and SDS-PAGE patterns of collagen from chicken feet were evaluated in order to determine the best method of extraction. Results: Type I collagen was considered as a major component of chicken feet collagen, which indicated by β chain and two distinct α-chains which are α1 and α2 that observed from the electrophoresis pattern of collagen extracted from all three methods. The lactic acid method showed the highest percentage of end yield and concentration of protein compared to the other two methods. However, lactic acid method showed the lowest swelling percentage and higher pH value. Conclusions: According to these results, soaked in 5% lactic acid for 36 hours is possible as the best collagen extraction method from chicken feet.

No abstract

Previous studies have proved that chicken (Gallus gallus domesticus) feet