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- W2546448516 abstract "Human nerve growth factor a member of the neurotrophin family can be used to treat neurodegenerative diseases. As it has disulfide bonds in its structure, periplasmic expression of it using appropriate signal sequence is beneficial. Therefore, in this work β-nerve growth factor (β-NGF) was expressed in Escherichia coli using pET39b expression vector containing DsbA signal sequence. In an initial step, the effect of isopropyl β-D-1-thiogalactopyranoside (IPTG) and lactose concentration as inducer on protein production was investigated using response surface methodology. Then the effect of different postinduction time and temperature on protein production was studied. Our results indicated that the highest β-NGF production was achieved with 1 mM IPTG and low concentrations of lactose (0-2% w/v), low cultivation temperature of 25°C and postinduction time of 2 hr. Also following β-NGF purification, bioassay test using PC12 cell line was done. The biological activity of the purified β-NGF showed a similar cell proliferation activity with the standard recombinant human β-NGF. In conclusion, the results indicated an optimized upstream process to obtain high yields of biologically active β-NGF." @default.
- W2546448516 created "2016-11-11" @default.
- W2546448516 creator A5020304237 @default.
- W2546448516 creator A5073430653 @default.
- W2546448516 creator A5091315104 @default.
- W2546448516 date "2017-04-21" @default.
- W2546448516 modified "2023-09-30" @default.
- W2546448516 title "Optimization of recombinant β-NGF expression in <i>Escherichia coli</i> using response surface methodology" @default.
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- W2546448516 doi "https://doi.org/10.1080/10826068.2016.1252927" @default.
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