A pretreatment method using aqueous ammonia was investigated with the intent of minimizing the liquid throughput. This process uses a flowthrough packed column reactor (or percolation reactor). In comparison to the ammonia recycle percolation (ARP) process developed previously in our laboratory, this process significantly reduces the liquid throughput to one reactor void volume in packed bed (2.0-4.7 mL of liquid/g of corn stover) and, thus, is termed low-liquid ARP (LLARP). In addition to attaining short residence time and reduced energy input, this process achieves 59-70% of lignin removal and 48-57% of xylan retention. With optimum operation of the LLARP to corn stover, enzymatic digestibilities of 95, 90, and 86% were achieved with 60, 15, and 7.5 filter paper units/g of glucan, respectively. In the simultaneous saccharification and fermentation test of the LLARP samples using Saccharomyces cerevisiae (NREL-D5A), an ethanol yield of 84% of the theoretical maximum was achieved with 6% (w/v) glucan loading. In the simultaneous saccharification and cofermentation (SSCF) test using recombinant Escherichia coli (KO11), both the glucan and xylan in the solid were effectively utilized, giving an overall ethanol yield of 109% of the theoretical maximum based on glucan, a clear indication that the xylan content was converted into ethanol. The xylooligomers existing in the LLARP effluent were not effectively hydrolyzed by cellulase enzyme, achieving only 60% of digestibility. SSCF of the treated corn stover was severely hampered when the substrate was supplemented with the LLARP effluent, giving only 56% the overall yield of ethanol. The effluent appears to significantly inhibit cellulase and microbial activities.
Bacillus subtilis TD6 was isolated from Takifugu rubripes, also known as puffer fish. Cellulase from this strain was partially purified by ammonium sulphate precipitation up to 80% saturation, entrapped in calcium alginate beads, and finally characterized using CMC as the substrate. For optimization, various parameters were observed, including pH maximum, temperature maximum, sodium alginate, and calcium chloride concentration. pH maximum of the enzyme showed no changes before and after immobilization and remained stable at 6.0. The temperature maximum showed a slight increase to 60 °C. Two percent sodium alginate and a 0.15 M calcium chloride solution were the optimum conditions for acquisition of enzyme with greater stability. K (m) and V (max) values for the immobilized enzyme were slightly increased, compared with those of free enzyme, 2.9 mg/ml and 32.1 μmol/min/mL, respectively. As the purpose of immobilization, reusability and storage stability of the enzyme were also observed. Immobilized enzyme retained its activity for a longer period of time and can be reused up to four times. The storage stability of entrapped cellulase at 4 °C was found to be up to 12 days, while at 30 °C, the enzyme lost its activity within 3 days.
Titanium dioxide thin films were grown by atomic layer deposition (ALD) at 100–250 °C with tetrakis-dimethyl-amido titanium, using H2O2 as a counter-reactant. We have explored the effects of deposition temperature and the reactant pulse and purge times on the film growth rate to optimize the ALD process of TiO2. The film growth rate decreased with growth temperature below 175 °C, but was saturated to 0.28Å∕cycle at 175–250 °C. All the as-deposited films were highly pure, and the root-mean-square roughness was less than 2.5% of the film thickness. The films deposited at 150 °C and above were polycrystalline with an anatase structure, whereas those deposited at 125 ° C were amorphous. There was no change of crystal structure after annealing the crystalline films at temperatures of 450–650 °C. All the crystalline films were shown to have a photocatalytic activity in decomposing methylene blue in an aqueous solution. The films prepared at higher deposition temperatures were shown to have a better photocatalytic activity in decomposing methylene blue.
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