Jun Li

Prof. Dr. Jun Li

orcid

Research Focus & Metrics

Academic Career Length

17Years (2010-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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Verified
Journal Article
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ZMZilong Ma
Zilong Ma
BDBin Du
Bin Du
JLJun Li
Jun Li
YYYuedong Yang
Yuedong Yang
FZFengmei Zhu
Fengmei Zhu
Anthocyanin is a type of flavonoid pigment widely present in fruits and vegetables. It can not only be used as natural pigment, but also has a variety of health functions, for instance, anti-oxidant, anti-inflammatory, anti-tumor, and neuroprotective activities. Persistent proinflammatory status is a major factor in the development, progression, and complications of chronic diseases. Not surprisingly, there are thus many food ingredients that can potentially affect inflammation related diseases and many studies have shown that anthocyanins play an important role in inflammatory pathways. In this paper, the inflammation related diseases (such as, obesity, diabetes, cardiovascular disease, and cancer) of anthocyanins are introduced, and the anti-inflammatory effect of anthocyanins is emphatically introduced. Moreover, the anti-inflammatory mechanism of anthocyanins is elaborated from the aspects of NF-κB, toll like receptor, MAPKs, NO, and ROS and the main efficacy of anthocyanins in inflammation and related diseases is determined. In conclusion, this review aims to get a clear insight into the role of anthocyanins in inflammation related diseases.

1 August 2021 in Efood
Verified
Journal Article
Open access
FZFengmei Zhu
Fengmei Zhu
JLJiaxuan Li
Jiaxuan Li
ZMZilong Ma
Zilong Ma
JLJun Li
Jun Li
BDBin Du
Bin Du
Anthocyanins is a natural edible pigment with many health benefits. The aim of this work was the identification of anthocyanins present in Aronia melanocarpa using mass spectrometric features. The anthocyanins of the A. melanocarpa were analyzed by UVVis, HPLC‐DAD and LC‐EIS/MS methods. The four important anthocyanins were identified as follows: cyanidin‐3‐galactoside (68.68%), cyanidin‐3‐arabinoside (25.62%), cyanidin‐3‐glucoside (5.28%) and cyanidin‐3‐xyloside (0.42%). Among the four anthocyanin monomers, three anthocyanins with the highest content of A. melanocarpa were selected, and the antioxidant activity was studied with the total anthocyanins. The antioxidant capacity was cyanidin‐3‐galactoside > total anthocyanin > cyanidin‐3‐arabinoside > cyanidin‐3‐glucoside. The activity of the four anthocyanin samples was greater than ascorbic acid. The methodology described in this study will provide an effective tool for anthocyanins identification. Our results suggested that anthocyanins from A. melanocarpa exhibited effective antioxidant activity. These findings may be crucial in future research concerning chokeberry based functional food products.

27 February 2020 in Microbiologyopen
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XDXiangyu Deng
Xiangyu Deng
BDBin Du
Bin Du
FZFengmei Zhu
Fengmei Zhu
YGYanan Gao
Yanan Gao
JLJun Li
Jun Li
β‐Glucosidase production by Aspergillus niger is accompanied by an inevitable temperature increase in the industrial fermentation environment. Hence, the synthetic process of β‐glucosidase is negatively affected. However, our understanding of the heat stress response (HSR) mechanism in A. niger is still incomplete. The current study explored the intracellular proteome profile of A. niger 3.316 in group T (50°C stress) and group C (30°C control) using two proteomic approaches (isobaric tags for relative and absolute quantitation [iTRAQ] and label‐free) and examined the expression of four proteins using a parallel reaction monitoring (PRM) approach. Based on the result of the iTRAQ proteomic analysis, 1,025 proteins were differentially expressed in group T compared to group C. Using the label‐free approach, we only focused on 77 proteins with significant changes in their protein expression levels. In addition, we performed bioinformatics analysis on all these proteins and obtained detailed gene ontology (GO) enrichment and Kyoto encyclopedia of genes and genomes (KEGG) pathway results. Under heat stress conditions, the relative expression levels of proteins with protection and repair functions were upregulated in A. niger 3.316. These proteins were involved in metabolic pathways, oxidative phosphorylation, porphyrin and chlorophyll metabolism, pyruvate metabolism, and the citrate cycle (TCA cycle). The insights obtained from the presented proteomics and bioinformatics analyses can be used to further explore the HSR mechanism of A. niger.

13 May 2025 in Molecular Nutrition & Food Research
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Journal Article
Closed access
CWChenxuan Wang
Chenxuan Wang
JZJiefang Zhou
Jiefang Zhou
XLXiaojing Liu
Xiaojing Liu
FZFengmei Zhu
Fengmei Zhu
JLJun Li
Jun Li
JLJinjin Liu
Jinjin Liu

21 February 2025 in Analytical Methods
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FGFeng Guo
Feng Guo
KCKeren Chen
Keren Chen
JYJiaru Yang
Jiaru Yang
YWYifan Wu
Yifan Wu
JCJiageng Cheng
Jiageng Cheng
WXWentao Xu
Wentao Xu
The molecular recognition elements utilized for antibiotic detection are presented, along with the interactions between them. The inner circle represents the five types of intermolecular forces, while the outer circle embodies the seven molecular recognition elements and direct recognition.

4 November 2010 in Applied Biochemistry and Microbiology
Verified
Journal Article
Closed access
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FZF. -M. Zhu
F. -M. Zhu
BDB. Du
B. Du
HGH. -S. Gao
H. -S. Gao
CLC. -J. Liu
C. -J. Liu
JLJun Li
Jun Li
Protoplasts of Aspergillus oryzae 3.481 and Aspergillus niger 3.316 were prepared using cellulose and snail enzyme with 0.6 M NaCl as osmotic stabilizer. Protoplast fusion has been performed using 35% polyethylene glycol 4,000 with 0.01 mM CaCl2. The fused protoplasts have been regenerated on regeneration medium and fusants were selected for further studies. An intracellular (β-glucosidase (EC 3.2.1.21) was purified from the protoplast fusant of Aspergillus oryzae 3.481 and Aspergillus niger 3.316 and characterized. The enzyme was purified 138.85-fold by ammonium sulphate precipitation, DE-22 ion exchange and Sephadex G-150 gel filtration chromatography with a specific activity of 297.14 U/mg of protein. The molecular mass of the purified enzyme was determined to be about 125 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme had an optimum pH of 5.4 and temperature of 65°C, respectively. This enzyme showed relatively high stability against pH and temperature and was stable in the pH range of 3.0–6.6. Na+, K+, Ca2+, Mg2+ and EDTA completely inhibited the enzyme activity at a concentration of 10 mM. The enzyme activity was accelerated by Fe3+. The enzyme activity was strongly inhibited by glucose, the end product of glucoside hydrolysis. The K m and V max values against salicin as substrate were 0.035 mM and 1.7215 μmol min−1, respectively.