Background: Wax esters are important ingredients in cosmetics, pharmaceuticals, lubricants and other chemical industries due to their excellent wetting property. Since the naturally occurring wax esters are expensive and scarce, these esters can be produced by enzymatic alcoholysis of vegetable oils. In an enzymatic reaction, study on modeling and optimization of the reaction system to increase the efficiency of the process is very important. The classical method of optimization involves varying one parameter at a time that ignores the combined interactions between physicochemical parameters. RSM is one of the most popular techniques used for optimization of chemical and biochemical processes and ANNs are powerful and flexible tools that are well suited to modeling biochemical processes.

Palm-based esters, synthesized through enzymatic transesterification of palm oil fractions with oleyl alcohol have potential application in pharmaceutical formulations. The phase behaviour of palm-based esters containing ibuprofen with surfactant of different HLB values was investigated for topical delivery system. The surfactants were Tween 85, Tween 60 and Tween 80, and the palm-based esters were palm oil esters (POEs) and palm kernel oil esters (PKOEs). Ternary phase diagrams of palm-based esters: Ibuprofen/surfactant/water systems were constructed. Three distinct regions were observed in the phase diagrams; isotropic liquid region, L 1 , liquid crystalline region, L c and multiphase region, M. Nanoemulsions were prepared spontaneously by the addition of water to oil:ibuprofen/surfactant mixtures based on the ternary phase diagrams constructed. Formulations from the PKOEs:Ibuprofen/Tween 80/water systems were selected due to the presence of large isotropic liquid region, which suggested that this region was suitable to be used in producing nanoemulsions. Particle size analysis showed that the mean particle sizes of these formulations ranged from 10 nm to 70 nm. Zeta potential analysis for all formulations showed negative values from -4 to -8 mV. Stability studies showed that, after 4 h of stirring at room temperature (25°C), the formulations were stable under centrifugation test at 4000 rpm for 15 min. Stability under different storage temperature showed that at 25°C, the four formulations, F1, F2, F3 and F4 were stable with no phase separation for the duration of 1 month. However, when these formulations were stored at 45°C and 4°C, respectively, only F3 and F4 were observed to be stable. These two formulations have the potential to be used for topical delivery of ibuprofen.

An alcoholysis reaction between triolein and oleyl alcohol catalyzed by Lipozyme and Novozyme was carried out to produce oleyl oleate, a wax ester. The effects of various reaction parameters such as time, reaction temperature, amount of enzyme, molar ratio of substrates (oleyl alcohol/triolein), various organic solvents used and the initial water activity, a w of the reaction system were studied. The best conditions tested to produce wax ester were respectively, incubation time, 5 h; temperature, 50°C for Lipozyme and 60°C for Novozyme; weight of enzyme, 0.30 g and molar ratio of oleyl alcohol to triolein, 6:1. The use of organic solvents greatly in¯uenced the activity of lipase. Generally, the activity of lipase was high in nonpolar solvents with log P values greater than 2.50. Heptane and hexane were the best solvents tested. The enzymatic synthesis of oleyl oleate was best carried out at a w 0.32. Analysis of the yield of the products of the reaction at optimized reaction condition using Lipozyme showed that 75.66% oleyl oleate was produced.

A specific ligand targeting the immunodominant region of hepatitis B virus is desired in neutralizing the infectivity of the virus. In a previous study, a disulfide constrained cyclic peptide cyclo S(1) ,S(9) Cys-Glu-Thr-Gly-Ala-Lys-Pro-His-Cys (S(1) , S(9) -cyclo-CETGAKPHC) was isolated from a phage displayed cyclic peptide library using an affinity selection method against hepatitis B surface antigen. The cyclic peptide binds tightly to hepatitis B surface antigen with a relative dissociation constant (KD (rel) ) of 2.9 nm. The binding site of the peptide was located at the immunodominant region on hepatitis B surface antigen. Consequently, this study was aimed to elucidate the structure of the cyclic peptide and its interaction with hepatitis B surface antigen in silico. The solution structure of this cyclic peptide was solved using (1) H, (13) C, and (15) N NMR spectroscopy and molecular dynamics simulations with NMR-derived distance and torsion angle restraints. The cyclic peptide adopted two distinct conformations due to the isomerization of the Pro residue with one structured region in the ETGA sequence. Docking studies of the peptide ensemble with a model structure of hepatitis B surface antigen revealed that the cyclic peptide can potentially be developed as a therapeutic drug that inhibits the virus-host interactions.

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