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32 results on '"Dong Zixing"'

2. Crystallographic Manipulation Strategies toward Reversible Zn Anode with Orientational Deposition

Author

Yang, Xianzhong, primary, Dong, Zixing, additional, Weng, Gao, additional, Su, Yiwen, additional, Huang, Jiawen, additional, Chai, Hong, additional, Zhang, Ying, additional, Wu, Kuan, additional, Baek, Jong‐Beom, additional, Sun, Jingyu, additional, Chao, Dongliang, additional, Liu, Huakun, additional, Dou, Shixue, additional, and Wu, Chao, additional

Published
2024
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17. Efficient expression of novel glutamate decarboxylases and high level production of γ-aminobutyric acid catalyzed by engineered Escherichia coli

Author

Hong-Ling Shi, Yuan-Yuan Jia, Lun-Guang Yao, Kan Yunchao, Lin-Feng Wang, Zhu-Jin Jiao, Dong Zixing, Xiang Li, Tang Cunduo, and Jian-He Xu

Subjects
Glutamate decarboxylase, 02 engineering and technology, medicine.disease_cause, Biochemistry, Aminobutyric acid, 03 medical and health sciences, chemistry.chemical_compound, Biosynthesis, Structural Biology, Generally recognized as safe, medicine, Escherichia coli, Molecular Biology, Pyridoxal, gamma-Aminobutyric Acid, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Glutamate Decarboxylase, Glutamate receptor, Temperature, General Medicine, 021001 nanoscience & nanotechnology, Amino acid, Kinetics, Lactobacillus, chemistry, Pyridoxal Phosphate, Fermentation, 0210 nano-technology
Abstract

Glutamate decarboxylase (GAD) has the potential of converting L-glutamate to gamma-aminobutyric acid (GABA), which is an important non-proteinogenic amino acid that has a potential use as food additive or dietary supplement for its physiological functions. A novel pyridoxal 5'-phosphate (PLP)-dependent glutamate decarboxylase (LsGAD) was cloned from GRAS (generally recognized as safe) Lactobacillus senmaizukei by genome mining and efficiently expressed in Escherichia coli BL21. The LsGAD displayed excellent temperature property, pH property and kinetic parameters compared with the probe LbGAD and the other GADs. By increasing the copy number of the LsGAD encoding gene, the expression level of LsGAD and the biosynthesis yield of GABA were increased, which was near to 2 times of that was expressed in single copy. These results established a solid foundation for increasing the added value of L-glutamate and the biosynthesis of GABA.

Published
2020

21. Bile salt hydrolases: Structure and function, substrate preference, and inhibitor development

Author

Dong, Zixing and Lee, Byong H.

Subjects
Molecular Structure, Reviews, Animals, Humans, Enzyme Inhibitors, Amidohydrolases
Abstract

The worldwide trend of limiting the use of antibiotic growth promoters (AGPs) in animal production creates challenges for the animal feed industry, thus necessitating the development of effective non-antibiotic alternatives to improve animal performance. Increasing evidence has shown that the growth-promoting effect of AGPs is highly correlated with the reduced activity of bile salt hydrolase (BSH, EC 3.5.1.24), an intestinal bacteria-producing enzyme that has a negative impact on host fat digestion and energy harvest. Therefore, BSH inhibitors may become novel, attractive alternatives to AGPs. Detailed knowledge of BSH substrate preferences and the wealth of structural data on BSHs provide a solid foundation for rationally tailored BSH inhibitor design. This review focuses on the relationship between structure and function of BSHs based on the crystal structure, kinetic data, molecular docking and comparative structural analyses. The molecular basis for BSH substrate recognition is also discussed. Finally, recent advances and future prospectives in the development of potent, safe, and cost-effective BSH inhibitors are described.

Published
2018

30. Overexpression of the Bacillus licheniformisGroES enhances thermotolerance of Bacillus subtilisWB600

Author

Dong, Zixing, Chen, Xiaoling, Cai, Ke, Shen, Peili, Tian, Kangming, Jin, Peng, Liu, Xiaoguang, and Wang, Zhengxiang

Abstract

AbstractUse of thermotolerant strains offers the advantage of conducting production process at elevated temperatures, thereby improving the catalytic efficiency and reducing the energy consumption and the production costs. In the present study, thermotolerance gene groESfrom the thermophilic strain Bacillus licheniformisB186 was implanted into B. subtilisWB600 to improve its thermotolerance. The engineered strain WB600-pHY-groES displayed reduced doubling time as well as increased specific growth rates and cell viability compared with the control. Our results suggested that introducing heat shock proteins (HSPs) from thermophiles into B. subtiliscould be an effective approach to enhance its thermotolerance, thus facilitating the development of multichaperone expression systems for constructing more thermotolerant commercial B. subtilisstrains. To the best of our knowledge, this is the first report on improving the thermotolerance of B. subtilisby overexpression of HSPs.

Published
2018
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32. Improved ethanol productivity from lignocellulosic hydrolysates by <italic>Escherichia coli</italic> with regulated glucose utilization.

Author

Sun, Jinfeng, Tian, Kangming, Wang, Jie, Dong, Zixing, Liu, Xiaoguang, Permaul, Kugenthiren, Singh, Suren, Prior, Bernard A., and Wang, Zhengxiang

Subjects
ESCHERICHIA coli, GLUCOSE, ETHANOL, LIGNOCELLULOSE, ALCOHOLS (Chemical class)
Abstract

Background: Lignocellulosic ethanol could offer a sustainable source to meet the increasing worldwide demand for fuel. However, efficient and simultaneous metabolism of all types of sugars in lignocellulosic hydrolysates by ethanol-producing strains is still a challenge. Results: An engineered strain Escherichia coli B0013-2021HPA with regulated glucose utilization, which could use all monosaccharides in lignocellulosic hydrolysates except glucose for cell growth and glucose for ethanol production, was constructed. In E. coli B0013-2021HPA, pta-ackA, ldhA and pflB were deleted to block the formation of acetate, lactate and formate and additional three mutations at glk, ptsG and manZ generated to block the glucose uptake and catabolism, followed by the replacement of the wild-type frdA locus with the ptsG expression cassette under the control of the temperature-inducible λ pR and pL promoters, and the final introduction of pEtac-PA carrying Zymomonas mobilis pdc and adhB for the ethanol pathway. B0013-2021HPA was able to utilize almost all xylose, galactose and arabinose but not glucose for cell propagation at 34 °C and converted all sugars to ethanol at 42 °C under oxygen-limited fermentation conditions. Conclusions: Engineered E. coli strain with regulated glucose utilization showed efficient metabolism of mixed sugars in lignocellulosic hydrolysates and thus higher productivity of ethanol production. [ABSTRACT FROM AUTHOR]

Published
2018
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