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Utilization of Pineapple Juice Base Growth Medium for Lipid Production by Xanthophyllomyces dendrorhous Andriani, Ria Dewi; Akeprathumchai, Saengchai; Laoteng, Kobkul; Poomputsa, Kanokwan; Mekvichitsaeng, Phenjun
Jurnal Teknologi Pertanian Vol 14, No 3 (2013)
Publisher : Fakultas Teknologi Pertanian Universitas Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (347.96 KB)

Abstract

The main objective of this study lies in utilization of pineapple juice concentrate, an agricultural by-product derived from canned pineapple industry, as a low cost base growth medium to cultivate and simultaneously produce lipid by the red yeast X. dendrorhous. Pineapple juice was characterized and revealed that sucrose, glucose, and fructose were present at the concentration of 23.58, 39.14, and 36.86 g/L, respectively. In addition, acetic acid, citric acid, propionic acid concentrations of 21.70, 2751.30, and 51.00 mM were found to be the main acid in pineapple juice concentrate together with several amino acids; therefore, it possible to employ as base culture medium to cultivate X. dendrorhous. Results on cultivation of X. dendrorhous in the concentration of total sugar 10 g/L pineapple juice without supplemented of nitrogen source was satisfactory in comparison with that of yeast medium. Biomass and lipid content obtained of when cultivated X. dendrorhous in pineapple juice were of 5.14 g/L and 8.90 % in dry cell weight, respectively, while biomass and lipid content when cultivated in yeast medium were 4.88 g/L and 4.10 % in dry cell weight, respectively. Since yeast medium was rather expensive, moreover, cultivation of X. dendrorhous in pineapple juice concentrate, a low cost substrate, was fairly reasonable. Therefore, pineapple juice could be an excellent substrate for cultivating X. dendrorhous when appropriately optimized.Keywords: biomass, lipid, X. dendrorhous, pineapple juice
Baculovirus Surface Display Using Infuenza Neuraminidase (NA) Transmembrane Anchor Trianti, Irisa; Akeprathumchai, Saengchai; Mekvichitsaeng, Phenjun; Poomputsa, Kanokwan
Journal of Tropical Life Science Vol 6, No 3 (2016)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.06.03.12

Abstract

Baculovirus surface display has been employed as an excellent tools for presentation of foreign peptides and proteins on virus surface with native conformation, functions and immunogenicity. A baculovirus major envelope protein, gp64, or a capsid protein, vp39 are generally used as fusion partners for displaying of polypeptides on the surface of virions. Alternatively, a membrane anchoring domain of vesicular stomatitis virus G protein (VSV-G) can also be used. In this study, an influenza neuraminidase (NA) was proposed as a new membrane anchor for the display of Angiotensin II (AngII), DRVYIHPFHL, peptides. The AngII peptides were inserted into NA by replacing NA amino acid number 60-67 with AngII, and then integrated into a baculovirus genome. A recombinant baculovirus expressing the NA fusion-AngII peptides was generated from infected insect cells. Those peptides were found to express and translocated on the membrane of the baculovirus infected insect cell (Sf9 cell) as detected by immunocytochemistry using anti-AngII monoclonal antibody. Upon budding of the recombinant baculovirus progenies through the insect cells membrane, the recombinant NA-AngII peptides was acquired to envelopes of the new baculovirus progenies. The conformation of NA on baculovirus surface was not affected by the deletion, as the 55 kDa band of NA can be detected from Western Blotting analysis by specific anti-NA monoclonal antibody. In addition, the same protein was also found by anti-AngII antibody indicating that the AngII peptides had been successfully fused with the recombinant NA. Interestingly, electron microscopy analysis demonstrated that not only the recombinant baculovirus displaying AngII peptides were generated by infected insect cells, but also the NA virus-like-particle displaying AngII peptides.