• Korean Chemical Engineering Research
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• v.49 no.5
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• pp.664-668
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• 2011

Spherical alumina precursors represented by $AlO_xCl_y(OH)_z$, 30~200 nm in particle diameter, were prepared by partial hydrolysis of $AlCl_3$ vapor in a 500 ml reactor. Investigated on the particle morphology and size were the effects of the reaction time, the stirring speed and the reaction temperature. The particle morphology and size was insensitive to the reaction time in the range 20 to 300 s. The variation of the stirring speed from 0 to 300 and 800 rpm showed that the particle size was the largest at 0 rpm. As the temperature was varied from 180 to 190, 200, $140^{\circ}C$, the particle size showed a maximum at $190^{\circ}C$. By calcination of the as-produced particles at $1,200^{\circ}C$ for 6h with a heating rate of $10^{\circ}C$/min, ${\alpha}$-alumina particles 45 nm in surface area equivalent diameter were obtained. The particle shape after calcination turned wormlike due to sintering between neighboring particles. A rapid calcination at $1400^{\circ}C$ for 0.5 h with a higher heating rate of $50^{\circ}C$/min reduced the sintering considerably. An addition of $SiCl_4$ or TMCTS(2,4,6,8-tetramethylcyclosiloxane) to the $AlCl_3$ reduced the sintering effectively in the calcination step; however, peaks of ${\gamma}$ or mullite phase appeared. An addition of $AlF_3$ to the particles obtained from the hydrolysis resulted in a hexagonal disc shaped alumina particles.

• Microbiology and Biotechnology Letters
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• v.41 no.1
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• pp.17-25
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• 2013

The thermotolerant methylotrophic yeast Hansenula polymorpha is an attractive model organism for various fundamental studies, such as the genetic control of enzymes involved in methanol metabolism, peroxisome biogenesis, nitrate assimilation, and resistance to heavy metals and oxidative stresses. In addition, H. polymorpha has been highlighted as a promising recombinant protein expression host, especially due to the availability of strong and tightly regulatable promoters. In this study, we investigated the possibility of employing human serum albumin (HSA) as the fusion tag for the secretory expression of heterologous proteins in H. polymorpha. A set of four expression cassettes, which contained the methanol oxidase (MOX) promoter, translational HSA fusion tag, and the terminator of MOX, were constructed. The expression cassettes were also designed to contain sequences for accessory elements including His8-tag, $2{\times}(Gly_4Ser_1)$ linkers, tobacco etch virus protease recognition sites (Tev), multi-cloning sites, and strep-tags. To determine the effects of the size of the HSA fusion tag on the secretory expression of the target protein, each cassette contained the HSA gene fragment truncated at a specific position based on its domain structure. By using the Green fluorescence protein gene as the reporter, the properties of each expression cassette were compared in various conditions. Our results suggest that the translational HSA fusion tag is an efficient tool for the secretory expression of recombinant proteins in H. polymorpha.