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Zhongyuan Li
State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education & Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.

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Journal article
Published: 09 March 2019 in Toxins
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In this work of quercetin's anti-proliferation action on A. flavus, we revealed that quercetin can effectively hamper the proliferation of A. flavus in dose-effect and time-effect relationships. We tested whether quercetin induced apoptosis in A. flavus via various detection methods, such as phosphatidylserine externalization and Hoechst 33342 staining. The results showed that quercetin had no effect on phosphatidylserine externalization and cell nucleus in A. flavus. Simultaneously, quercetin reduced the levels of reactive oxygen species (ROS). For a better understanding of the molecular mechanism of the A. flavus response to quercetin, the RNA-Seq was used to explore the transcriptomic profiles of A. flavus. According to transcriptome sequencing data, quercetin inhibits the proliferation and aflatoxin biosynthesis by regulating the expression of development-related genes and aflatoxin production-related genes. These results will provide some theoretical basis for quercetin as an anti-mildew agent resource.

ACS Style

Xiu-Mei Li; Zhong-Yuan Li; Ya-Dong Wang; Jin-Quan Wang; Pei-Long Yang. Quercetin Inhibits the Proliferation and Aflatoxins Biosynthesis of Aspergillus flavus. Toxins 2019, 11, 154 .

AMA Style

Xiu-Mei Li, Zhong-Yuan Li, Ya-Dong Wang, Jin-Quan Wang, Pei-Long Yang. Quercetin Inhibits the Proliferation and Aflatoxins Biosynthesis of Aspergillus flavus. Toxins. 2019; 11 (3):154.

Chicago/Turabian Style

Xiu-Mei Li; Zhong-Yuan Li; Ya-Dong Wang; Jin-Quan Wang; Pei-Long Yang. 2019. "Quercetin Inhibits the Proliferation and Aflatoxins Biosynthesis of Aspergillus flavus." Toxins 11, no. 3: 154.

Review
Published: 01 November 2017 in Protein Expression and Purification
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A GH11 xylanase gene (xyn11-1) cloned from saline-alkali soil was successfully expressed in Pichia pastoris GS115. The purified recombinant Xyn11-1 showed its maximal activity at pH 6.0, and retained more than 60.4% of activity at pH 10.0, with good pH stability. Its optimal temperature was 50 °C and it was stable after incubation for 1 h at 30 °C. Furthermore, Xyn11-1 was highly salt-tolerant, retaining more than 77.4% of activity in the presence of 0.25-4 M NaCl and displaying more than 47.2% relative activity after being incubated in the presence of 5 M NaCl at 37 °C for 10 min. In addition, 5 mM β-Mercaptoethanol, Cu2+, Co2+, and Mn2+ increased the xylanase activity by 22.3%, 8.8%, 7.1%, and 4.4%, respectively. Significantly, 93.4% and 59.8% of the optimal activity was retained in the presence of 2% and 10% (v/v) ethanol, respectively. Under optimal conditions, the Km,Vmax, and Kcat value of Xyn11-1 for beechwood xylan were 3.7 mg ml-1, 101.0 μmol min-1 mg-1 and 42.1 s-1, respectively. Xyn11-1 is a strict endo-β-1,4-xylanase, its main enzymatic products being xylotetraose and xylopentaose. Xyn11-1 is the first reported GH11 xylanase isolated from saline-alkali soil, and has excellent tolerance of high pH, high salt concentrations and ethanol, which indicates its great potential for basic research and industrial applications.

ACS Style

Hui Wang; Zhongyuan Li; Huihui Liu; Shuang Li; Haiyan Qiu; Kun Li; Xuegang Luo; Yajian Song; Nan Wang; Hongpeng He; Hao Zhou; Wenjian Ma; Tongcun Zhang. Heterologous expression in Pichia pastoris and characterization of a novel GH11 xylanase from saline-alkali soil with excellent tolerance to high pH, high salt concentrations and ethanol. Protein Expression and Purification 2017, 139, 71 -77.

AMA Style

Hui Wang, Zhongyuan Li, Huihui Liu, Shuang Li, Haiyan Qiu, Kun Li, Xuegang Luo, Yajian Song, Nan Wang, Hongpeng He, Hao Zhou, Wenjian Ma, Tongcun Zhang. Heterologous expression in Pichia pastoris and characterization of a novel GH11 xylanase from saline-alkali soil with excellent tolerance to high pH, high salt concentrations and ethanol. Protein Expression and Purification. 2017; 139 ():71-77.

Chicago/Turabian Style

Hui Wang; Zhongyuan Li; Huihui Liu; Shuang Li; Haiyan Qiu; Kun Li; Xuegang Luo; Yajian Song; Nan Wang; Hongpeng He; Hao Zhou; Wenjian Ma; Tongcun Zhang. 2017. "Heterologous expression in Pichia pastoris and characterization of a novel GH11 xylanase from saline-alkali soil with excellent tolerance to high pH, high salt concentrations and ethanol." Protein Expression and Purification 139, no. : 71-77.

Conference paper
Published: 08 October 2017 in Lecture Notes in Electrical Engineering
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Aflatoxin B1 is highly toxic secondary metabolites predominantly produced by some fungi and commonly found in cereals worldwide, which seriously threatens the health of human and animals due to its highly toxic. The aim of this study was to isolate AFB1 degradation microorganisms from decomposed soil using coumarin medium as sole carbon source. The soil sample was inoculated in coumarin medium at 30 °C. After 7 days, the strains which grow in coumarin medium were transferred into the fresh coumarin medium for the further screening. The screening result showed that the strain 1912 and 10A could grow on the coumarin medium, and their AFB1 degradation abilities were further analyzed by high-performance liquid chromatography. Strain 1912 and 10A could degrade AFB1 rapidly and effectively, the AFB1 degradating ratio were 60.49 and 45.51% after 24 h, respectively. Based on BLAST analysis, strain 1912 belongs to the Emericellopsi sp. and strain 10A belongs to the Sarocladium sp. Respectively. This study provided a potential solution for dealing with AFB1 contamination in human diet and animal feed.

ACS Style

Hui Wang; Zhongyuan Li; Haiyan Qiu; Tongcun Zhang. Biological Degradation of Aflatoxin B1 by Emericellopsis sp. 1912 and Sarocladium sp. 10A. Lecture Notes in Electrical Engineering 2017, 444, 525 -532.

AMA Style

Hui Wang, Zhongyuan Li, Haiyan Qiu, Tongcun Zhang. Biological Degradation of Aflatoxin B1 by Emericellopsis sp. 1912 and Sarocladium sp. 10A. Lecture Notes in Electrical Engineering. 2017; 444 ():525-532.

Chicago/Turabian Style

Hui Wang; Zhongyuan Li; Haiyan Qiu; Tongcun Zhang. 2017. "Biological Degradation of Aflatoxin B1 by Emericellopsis sp. 1912 and Sarocladium sp. 10A." Lecture Notes in Electrical Engineering 444, no. : 525-532.

Conference paper
Published: 08 October 2017 in Lecture Notes in Electrical Engineering
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Xylanase, as critical hemicellulose degrading enzyme, it could degrade xylan into oligosaccharides and has been widely used in medicine, paper-making, animal forage, marine functional foods and textile industry. So exploring new xylanase with excellent enzymatic characteristic will be benefit for improving production efficiency and reducing cost. In this study, a novel xylanase of family 10 (Xyn13-3) was obtained from the genomic DNA of alkaline soil by touchdown-PCR and thermal asymmetric interlaced (TAIL) PCR methods, which shares the highest identity (61%) with the reported GH10 xylanase (XP_018659952.1) in GenBank database. Xyn13-3 contained a catalytic motif of GH10 (339 residues). The recombinant plasmid pPIC9-Xyn13-3 was constructed and the recombinant protein was successfully expressed in Pichia pastoris GS115. The special activity of recombinant xylanase was 135.24 U/mg. Exploring the use of novel enzymes from different organisms, with distinct characteristics, could contribute to the development of a highly efficient system for lignocellulose conversion.

ACS Style

Haiyan Qiu; Zhongyuan Li; Hui Wang; Tongcun Zhang. A Novel GH10 Xylanase Xyn13-3 from Alkaline Soil: Gene Cloning and Heterogenous Expression. Lecture Notes in Electrical Engineering 2017, 444, 97 -103.

AMA Style

Haiyan Qiu, Zhongyuan Li, Hui Wang, Tongcun Zhang. A Novel GH10 Xylanase Xyn13-3 from Alkaline Soil: Gene Cloning and Heterogenous Expression. Lecture Notes in Electrical Engineering. 2017; 444 ():97-103.

Chicago/Turabian Style

Haiyan Qiu; Zhongyuan Li; Hui Wang; Tongcun Zhang. 2017. "A Novel GH10 Xylanase Xyn13-3 from Alkaline Soil: Gene Cloning and Heterogenous Expression." Lecture Notes in Electrical Engineering 444, no. : 97-103.

Journal article
Published: 14 August 2017 in Biotechnology & Biotechnological Equipment
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A novel xylanase gene of family 10 (xyn27) was obtained from the genomic DNA of frozen soil of Daxinganling in China by Touch-down polymerase chain reaction (PCR) and thermal asymmetric interlaced (TAIL) PCR methods. Xyn27 contained a putative signal peptide (20 residues) and a catalytic motif of GH10 (327 residues) and shared the highest similarity (83%) with the reported GH10 xylanase (XM_003662144). The recombinant xyn27 was successfully expressed in Pichia pastoris GS115 and the optimal induction condition was 30 °C for 48 h. Xyn27 was demonstrated to be a cold-active xylanase, which shows its highest activity at 35 °C and still had 60.25%, 38.70% and 10.8% relative activity at 20 °C, 10 °C and 0 °C. Further analysis showed that Xyn27 has fewer arginine and more alanine residues compared with its mesophilic or thermophilic counterparts. The optimal pH of Xyn27 was 7.0, and it was stable after incubating under the pH range from 3.0 to 9.0 for 1 h. Besides, Xyn27 exhibited superior metal ion tolerance than other GH10 cold-active xylanases, being tolerant to most metal ions and organic solvents, and significantly enhanced by Ca2+, Mn2+ and Zn2+ metal ions. In addition, the Km, Vmax, kcat and kcatKm−1 against beechwood xylan were 13.42 mg mL−1, 9.07 μmol min−1 mg−1, 192.98 min−1 and 14.38 mL min−1 mg−1, and Xyn27 could completely degrade xylan into xylobiose. The features of cold activity and metal-ion tolerance suggested that xylanase Xyn27 could have potential application in basic research and various industries like food possessing.

ACS Style

Haiyan Qiu; Zhongyuan Li; Hui Wang; Haiying Zhang; Shuang Li; Xuegang Luo; Yajian Song; Nan Wang; Hongpeng He; Hao Zhou; Wenjian Ma; Tongcun Zhang. Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil. Biotechnology & Biotechnological Equipment 2017, 31, 955 -963.

AMA Style

Haiyan Qiu, Zhongyuan Li, Hui Wang, Haiying Zhang, Shuang Li, Xuegang Luo, Yajian Song, Nan Wang, Hongpeng He, Hao Zhou, Wenjian Ma, Tongcun Zhang. Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil. Biotechnology & Biotechnological Equipment. 2017; 31 (5):955-963.

Chicago/Turabian Style

Haiyan Qiu; Zhongyuan Li; Hui Wang; Haiying Zhang; Shuang Li; Xuegang Luo; Yajian Song; Nan Wang; Hongpeng He; Hao Zhou; Wenjian Ma; Tongcun Zhang. 2017. "Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil." Biotechnology & Biotechnological Equipment 31, no. 5: 955-963.

Journal article
Published: 05 September 2016 in Journal of the Science of Food and Agriculture
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BACKGROUNDContamination of food and feed by Aflatoxin B1 (AFB1) has posed serious economic and health problem worldwide, developing biological methods for AFB1 degradation is highly required.RESULTSAmong three AFB1 degrading microorganisms isolated from moldy peanut, Fusarium sp. WCQ3361 could remove AFB1 extremely effective with a degradation ratio of 70.20% after 1 min and 95.38% after 24 h. Its degradation ratio was not much affected by temperature change (0-90 °C), and it also displayed excellent thermostability, maintained 99.40% residual activity after boiling for 10 min. Since protease K could reduce the AFB1 degradation ratio by 55.15 %, we proposed that the effective component for AFB1 degradation is a protein. The AFB1 degradation ability of Fusarium sp. WCQ3361 was further verified by feed stock detoxication and MTT test with HepG2 cells. In addition, no degradation products were detected by preliminary liquid chromatography mass spectrometry, suggesting AFB1 might be metabolized to products with different chemical characteristics from AFB1.CONCLUSIONFusarium sp. WCQ3361 was the first reported AFB1 degradation fungus belonging to genus Fusarium with broad reaction temperature range, excellent thermostability and high activity, which provides a potential highly useful solution to dealing with AFB1 contamination in human diet and animal feed.

ACS Style

Cuiqiong Wang; Zhongyuan Li; Hui Wang; Haiyan Qiu; Minghui Zhang; Shuang Li; Xuegang Luo; Yajian Song; Hao Zhou; Wenjian Ma; Tongcun Zhang. Rapid biodegradation of aflatoxin B1 by metabolites ofFusariumsp. WCQ3361 with broad working temperature range and excellent thermostability. Journal of the Science of Food and Agriculture 2016, 97, 1342 -1348.

AMA Style

Cuiqiong Wang, Zhongyuan Li, Hui Wang, Haiyan Qiu, Minghui Zhang, Shuang Li, Xuegang Luo, Yajian Song, Hao Zhou, Wenjian Ma, Tongcun Zhang. Rapid biodegradation of aflatoxin B1 by metabolites ofFusariumsp. WCQ3361 with broad working temperature range and excellent thermostability. Journal of the Science of Food and Agriculture. 2016; 97 (4):1342-1348.

Chicago/Turabian Style

Cuiqiong Wang; Zhongyuan Li; Hui Wang; Haiyan Qiu; Minghui Zhang; Shuang Li; Xuegang Luo; Yajian Song; Hao Zhou; Wenjian Ma; Tongcun Zhang. 2016. "Rapid biodegradation of aflatoxin B1 by metabolites ofFusariumsp. WCQ3361 with broad working temperature range and excellent thermostability." Journal of the Science of Food and Agriculture 97, no. 4: 1342-1348.

Book chapter
Published: 04 April 2015 in Lecture Notes in Electrical Engineering
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Pu’er Tea is a popular post-fermented tea and has a variety of health benefits. Many microorganisms, especially lactobacillus, exist and play an important role in the fermentation process of Pu’er tea. In this study, we try to screen some lactobacillus by plate method from the Pu’er tea, and strain C2 with significant cycle isolated from Pu’er tea. 16S rRNA gene sequencing results showed that strain C2 had 99 % sequence similarity to that of the type strain of three Bacillus coagulans (NR 102791.1, CP002472.1, NR 115727.1), and the results show that methyl red test and V&P test were positive. Sugar fermentation test suggested that strain C2 produced acid but not gas, which is identical to B. coagulans. This study confirmed that lactic acid bacteria play a role in Pu’er tea fermentation.

ACS Style

Cuixia Feng; Zhongyuan Li; Kun Li; Minghui Zhang; Cuiqiong Wang; Xuegang Luo. Screening, Isolation, and Identification of Bacillus coagulans C2 in Pu’er Tea. Lecture Notes in Electrical Engineering 2015, 333, 557 -562.

AMA Style

Cuixia Feng, Zhongyuan Li, Kun Li, Minghui Zhang, Cuiqiong Wang, Xuegang Luo. Screening, Isolation, and Identification of Bacillus coagulans C2 in Pu’er Tea. Lecture Notes in Electrical Engineering. 2015; 333 ():557-562.

Chicago/Turabian Style

Cuixia Feng; Zhongyuan Li; Kun Li; Minghui Zhang; Cuiqiong Wang; Xuegang Luo. 2015. "Screening, Isolation, and Identification of Bacillus coagulans C2 in Pu’er Tea." Lecture Notes in Electrical Engineering 333, no. : 557-562.