Elizabethkingia anophelis is an emerging human pathogen causing neonatal meningitis, catheterassociated infections and nosocomial outbreaks with high mortality rates. Besides, they are resistant to most antibiotics used in empirical therapy. In this study, therefore, we used immunoinformatic approaches to design an epitope-based vaccine against E. anophelis as an alternative preventive measure. Initially, T-cell (CTL and HTL) and B-cell (LBL) epitopes were predicted from the highest antigenic protein. The CTL and HTL epitopes together had a population coverage of 99.97% around the world. Eventually, 6 CTL, 7 HTL, and 2 LBL epitopes were selected and used to construct a multiepitope vaccine. The vaccine protein was found to be highly immunogenic, non-allergenic, and non-toxic. Codon adaptation and in silico cloning were performed to ensure better expression within E. coli K12 host system. The stability of the vaccine structure was also improved by disulphide bridging. In addition, molecular docking and dynamic simulation revealed good and stable binding affinity between the vaccine and receptor. The immune simulation showed higher levels of T-cell and B-cell activities which was in coherence with actual immune response. Repeated exposure simulation resulted in higher clonal selection and faster antigen clearance. Nevertheless, experimental validation is required to ensure the immunogenic potency and safety of this vaccine to control E. anophelis infection in the future.

A whipping method for the measurement of overrun and foam stability was developed. Using this method the characteristic foams formed by the following proteins were studied: sodium caseinate, milk protein isolate and whey protein. The method was able to detect differences between foams produced by different proteins. The effects of copper sulfate and proteose-peptone on egg white foams were studied to show the reliability of the method. It was demonstrated that the addition of I mM copper sulfate stabilized (p < 0.05) foams made from both fresh and powdered egg white. Addition of proteose-peptone (0.05% and 0.1%) reduced the overrun and destabilized egg white foams.

Mixtures of /c-casein and /Mactoglobulin (/?-lg) were heated at 70 °C in 20 mM-imidazole buffer, pH 6-8 containing 20 mM-EGTA. Aggregation of the *-casein//?-lg mixture occurred within 90 s and susceptibility to hydrolysis by chymosin decreased significantly within 180 s even though covalent interaction was not detected until after 4000 s. UV-absorbance indicated initial structural destabilization of the heated /c-casein//?-lg mixture followed by a return (> 350 s) to a spectrum comparable to the native state, indicating molecular rearrangement. Apparent hydrophobicity of /c-casein decreased 80 % within 250 s compared to a 38% decrease for /?-lg. Under similar conditions, the /c-casein//?-lg mixture (1:1) showed a faster (2 -5 times) decrease in apparent hydrophobicity than /c-casein alone with concomitant exposure of acidic (hydrophilic) groups. The results suggested that the driving force for the rearrangement was mainly hydrophobic, i.e. entropic in origin. The tendency of heated and subsequently cooled /c-casein//?-lg to aggregate reached a maximum after heating at 70 °C for 720 s.

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