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Application of full permeate recycling to very high gravity ethanol fermentation from corn
Zhongyang Ding,Liang Zhang,Yaye Fang,Kechang Zhang,GuiYang Shi,Ling Xu 한국화학공학회 2009 Korean Journal of Chemical Engineering Vol.26 No.3
A ceramic membrane with pore size of 0.2 μm was used to percolate grain stillage of very high gravity (VHG) ethanol fermentation from corn, and the micro-filtration permeate was completely recycled for the cooking step in the next fermentation process. The concentrations of solids, sugars, total nitrogen and Na+ in the grain stillage and permeate reached a relative steady state after two or three batches of filtration and recycling process. There are no negative effects of by-products on VHG ethanol fermentation, and the final ethanol yield was above 15% (v/v). The conditions of filtration were examined to determine the optimum conditions for the process and included an initial flux of clean water above 550 L·m−2·h−1 (0.1 MPa), an operating differential pressure of 0.15 MPa, an operating temperature above 70℃, and a permeation flux greater than 136 L·m−2·h−1. It could be concluded that full permeate recycling during ethanol production was an efficient process that resulted in less pollution and less energy consumption.
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Zhongyang Li,Qudong Wang,Huaping Tang,Tianwen Liu,Chuan Lei,Haiyan Jiang,Wenjiang Ding 대한금속·재료학회 2021 METALS AND MATERIALS International Vol.27 No.10
The variation of microstructure and mechanical properties along the cross section of squeeze cast Al-5Mg-3Zn-1Cu-1Sialloy is studied under both squeeze-cast and peak-aged condition (470 °C × 24 h + 125 °C × 24 h). For squeeze-cast alloy,along the depth direction, second dendrite arm space and the percentage of -Al increase significantly, while the volumefraction of T-Mg32(AlZnCu)49 and Mg2Siphase showed a dramatic decrease. The ultimate tensile strength of squeeze-castalloy slightly decreased from 357.04 MPa for the surface layer to 344.21 MPa for the central layer, yield strength droppedfrom 296.86 MPa to 241.03 MPa, but the elongation almost tripled from 1.42% to 3.78%. After peak aging, the ultimatetensile strength of surface layer and central layer reached 538.45 MPa and 504.03 MPa, yield strength reached 447.46 MPaand 442.65 MPa, and the elongation reached 5.23% and 3.97% respectively. Meanwhile the difference of ultimate tensilestrength and elongation was increased, but that of yield strength reduced after aging treatment. Precipitation strengtheningis the main strengthening mechanism while the improvement in ductility is due to the dissolution of T-Mg32(AlZnCu)49 andthe morphological change of eutectic Mg2Si.
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Liang Zhang,Zhongyang Ding,Peng Xu,Yuhong Wang,Zhenghua Gu,Zhu Qian,Guiyang Shi,Kechang Zhang 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.3
Tyrosinase is a key enzyme in the biosynthesis of melanin, and the use of inhibitors against tyrosinase can prevent hyperpigmentation by inhibiting enzymatic oxidation. However, the current use of tyrosine inhibitors is limited by their low activities and high toxicities. The aim of the present research was to develop novel whitening agents, or tyrosinase-targeted medicine, from a submerged culture of the fungus Ganoderma lucidum. Methyl lucidenate F was isolated from the ethanol-soluble-acidic components (ESACs) of G. lucidum, with the structure of ESACs elucidated via UV, LC-MS, and ^(13)C-NMR spectral analysis. The tyrosinase inhibitory activity was measured using catechol as a substrate. Methyl lucidenate F displayed uncompetitive inhibition of the potato tyrosinase activity,for which Lineweaver-Burk plots revealed a maximum reaction rate (V_(max)) of 0.4367/min, Michaelis constant (K_m)of 6.765 mM and uncompetitive inhibition constant (K_i) of 19.22 μM. Meanwhile, methyl lucidenate F (tetra cyclic triterpenoid) exhibited high tyrosinase inhibitory activity,with an IC_(50) of 32.23 μM. These results suggest that methyl lucidenate F may serve as a potential candidate for skin-whitening agents.
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Shuang Ping Liu,Rui Xia Liu,Jian Mao,Liang Zhang,Zhongyang Ding,Zhenghua Gu,Gui-Yang Shi 한국생물공학회 2016 Biotechnology and Bioprocess Engineering Vol.21 No.1
The aproteinogenic amino acid, L-phenylglycine, is an important side chain building block for some drugs. It would be of great commercial and environmental value to biocatalyse L-phenylalanine to L-phenylglycine, and thus replace the organic synthesis method. To produce Lphenylglycine from L-phenylalanine, an L-phenylglycine aminotransferase was screened and characterized. HpgTAO showed high homology to α-aminoadipate aminotransferase. The L-phenylalanine binding site was near the residues S26, R401, N201, and G46 in HpgTAO, and L-phenylalanine formed a hydrogen bond with Asn20, which was similar to the substrate binding mechanism of α-aminoadipate aminotransferase. HpgTAO showed increased activity in alkalescent environment below 40°C. The kinetic analysis showed that L-phenylalanine had the highest affinity to HpgTAO, which ensured the recycle biosynthesis of Lphenylglycine from L-phenylalanine. To date, it was the only aminotransferase using L-phenylalanine as an optimal amino donor. The L-phenylglycine biocatalysis operon was also constructed by co-expressing the hmaS, hmo and hpgT by a single plasmid. The first in vitro conversion of Lphenylalanine to L-phenylglycine was achieved by directly using the L-phenylalanine fermentation broth as the raw material.
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