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Fulltext Comparison of Phytochemicals, Antioxidant and Anti-Inflammatory Properties of Sun-, Oven- and Freeze-Dried Ginger Extracts

Mustafa I, Chin NL, Fakurazi S, Palanisamy A

Foods, 2019 Oct 06;8(10).
PMID: 31590464 DOI: 10.3390/foods8100456

The effects of different drying methods, including sun-, oven-, and freeze-drying on the changes in the antioxidant and anti-inflammatory activities of ginger (Zingiber officinale var. Rubra) rhizome were studied. Sun-, oven-, and freeze-dried ginger showed a significant (p < 0.05) increase in phenolic content by 1.79, 1.53, and 1.91-fold; flavonoid content increased by 6.06, 5.27, and 4.90-fold; FRAP increased by 3.95, 3.51, and 3.15-fold; ABTS•+ scavenging activity increased by 2.07, 1.72, and 1.61-fold; and DPPH• inhibition increased by 78%, 58%, and 56%, respectively. Dried ginger also exhibited better inhibitory effects on the lipopolysaccharides-induced nitric oxide production in murine macrophage RAW 264.7. The drying process demonstrated a positive effect on the bioactivities of ginger. The sun-dried ginger exhibited the most potent antioxidant properties with the best enhanced anti-inflammatory activity followed by the oven-dried ginger and lastly, the freeze-dried ginger.
Fulltext A single epitope of Epstein-Barr Virus stimulate IgG production in mice

Widodo, Pristiwanto B, Rifa'i M, Mustafa I, Huyop FZ

Ann Med Surg (Lond), 2018 Nov;35:55-58.
PMID: 30294429 DOI: 10.1016/j.amsu.2018.09.014

Background: Epstein-Barr virus (EBV) is closely associated with the high incidence of nasopharyngeal carcinoma in worldwide. Vaccination is one strategy with the potential to prevent the occurrence of EBV-associated cancers, but a suitable vaccine is yet to be licensed. Much vaccine development research focuses on the GP350/220 protein of EBV as it contains an immunogenic epitope at residues 147-165, which efficiently stimulates IgG production in vitro. We examined the ability of this epitope (EBVepitope) to induce IgG production in mice.
Methods: The antibody binding pattern of the epitope was analyzed using bioinformatics tools. The IgG production in mice were examined by FACS Calibur™ Flow cytometer.
Results: The epitope bound the 72A1 monoclonal antibody at the same site as GP350/220 protein, indicating that the epitope should stimulate B cells to produce antibody. Moreover, in vivo administration of EBVepitope successfully induced IgG expression from B cells, compared with controls. Further investigation indicated that the relative number of B cells expressing IgE in EBVepitope-treated mice was lower than controls.
Conclusions: Our data suggest that this EBV GP350 epitope is able to induce IgG expression in vivo without causing allergic reactions, and represents a potential EBV vaccine candidate.

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