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  1. AU="Peng, Huakang"
  2. AU="Soderquest, Katrina"
  3. AU="Da Cruz ESilva, C Beirão"
  4. AU="Khan-Chowdhury, N R"
  5. AU="Bartelt-Hunt, Shannon"
  6. AU=Singh Gurvinder Pal
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  1. Article: Metabolic Engineering of Model Microorganisms for the Production of Xanthophyll.

    Wang, Nan / Peng, Huakang / Yang, Caifeng / Guo, Wenfang / Wang, Mengqi / Li, Gangqiang / Liu, Dehu

    Microorganisms

    2023  Volume 11, Issue 5

    Abstract: Xanthophyll is an oxidated version of carotenoid. It presents significant value to the pharmaceutical, food, and cosmetic industries due to its specific antioxidant activity and variety of colors. Chemical processing and conventional extraction from ... ...

    Abstract Xanthophyll is an oxidated version of carotenoid. It presents significant value to the pharmaceutical, food, and cosmetic industries due to its specific antioxidant activity and variety of colors. Chemical processing and conventional extraction from natural organisms are still the main sources of xanthophyll. However, the current industrial production model can no longer meet the demand for human health care, reducing petrochemical energy consumption and green sustainable development. With the swift development of genetic metabolic engineering, xanthophyll synthesis by the metabolic engineering of model microorganisms shows great application potential. At present, compared to carotenes such as lycopene and β-carotene, xanthophyll has a relatively low production in engineering microorganisms due to its stronger inherent antioxidation, relatively high polarity, and longer metabolic pathway. This review comprehensively summarized the progress in xanthophyll synthesis by the metabolic engineering of model microorganisms, described strategies to improve xanthophyll production in detail, and proposed the current challenges and future efforts needed to build commercialized xanthophyll-producing microorganisms.
    Language English
    Publishing date 2023-05-09
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms11051252
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Hen Egg White Lysozyme (HEWL) Confers Resistance to Verticillium Wilt in Cotton by Inhibiting the Spread of Fungus and Generating ROS Burst.

    Guo, Wenfang / Li, Gangqiang / Wang, Nan / Yang, Caifeng / Peng, Huakang / Wang, Mengqi / Liu, Dehu

    International journal of molecular sciences

    2023  Volume 24, Issue 24

    Abstract: Verticillium wilt is a soil-borne vascular disease caused by the fungal ... ...

    Abstract Verticillium wilt is a soil-borne vascular disease caused by the fungal pathogen
    MeSH term(s) Gossypium/metabolism ; Reactive Oxygen Species/metabolism ; Verticillium/metabolism ; Muramidase/metabolism ; Egg White ; Disease Resistance/genetics ; Plant Diseases/microbiology ; Gene Expression Regulation, Plant ; Plant Proteins/genetics ; Plant Proteins/metabolism
    Chemical Substances Reactive Oxygen Species ; Muramidase (EC 3.2.1.17) ; Plant Proteins
    Language English
    Publishing date 2023-12-05
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms242417164
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The introduction of an N-glycosylation site into prochymosin greatly enhances its production and secretion by Pichia pastoris.

    Wang, Nan / Yang, Caifeng / Peng, Huakang / Guo, Wenfang / Wang, Mengqi / Li, Gangqiang / Liu, Dehu

    Microbial cell factories

    2022  Volume 21, Issue 1, Page(s) 177

    Abstract: Background: N-glycosylation is one of the most important post-translational modifications. Many studies have shown that N-glycosylation has a significant effect on the secretion level of heterologous glycoproteins in yeast cells. However, there have ... ...

    Abstract Background: N-glycosylation is one of the most important post-translational modifications. Many studies have shown that N-glycosylation has a significant effect on the secretion level of heterologous glycoproteins in yeast cells. However, there have been few studies reporting a clear and unified explanation for the intracellular mechanism that N-glycosylation affect the secretion of heterologous glycoproteins so far. Pichia pastoris is an important microbial cell factory producing heterologous protein. It is of great significance to study the effect of N-glycosylation on the secretion level of heterologous protein. Camel chymosin is a glycoprotein with higher application potential in cheese manufacturing industry. We have expressed camel prochymosin in P. pastoris GS115, but the lower secretion level limits its industrial application. This study attempts to increase the secretion level of prochymosin through N-glycosylation, and explore the molecular mechanism of N-glycosylation affecting secretion.
    Results: Adding an N-glycosylation site at the 34th amino acid of the propeptide of prochymosin significantly increased its secretion in P. pastoris. N-glycosylation improved the thermostability of prochymosin without affecting the enzymatic activity. Immunoprecipitation coupled to mass spectrometry (IP-MS) analysis showed that compared with the wild prochymosin (chy), the number of proteins interacting with N-glycosylated mutant (chy34) decreased, and all differential interacting proteins (DIPs) were down-regulated in chy34-GS115 cell. The DIPs in endoplasmic reticulum were mainly concentrated in the misfolded protein pathway. Among the five DIPs in this pathway, overexpression of BiP significantly increased the secretion of chy. The knockout of the possible misfolded protein recognition elements, UDP-glycose:glycoprotein glucosyltransferase 1 and 2 (UGGT1/2) had no effect on the growth of yeast cells and the secretion of prochymosin.
    Conclusions: In conclusion, N-glycosylation increased the secretion of prochymosin in P. pastoris trough the adjustment of intracellular interacted proteins. The results of our study may help to elucidate the molecular mechanism of N-glycosylation affecting secretion and provide a new research method to improve the secretion of heterologous glycoprotein in P. pastoris.
    MeSH term(s) Animals ; Camelus/metabolism ; Chymosin/chemistry ; Chymosin/genetics ; Enzyme Precursors ; Glycoproteins/chemistry ; Glycosylation ; Pichia/genetics ; Pichia/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomycetales
    Chemical Substances Enzyme Precursors ; Glycoproteins ; Recombinant Proteins ; prorennin (EC 3.4.23.-) ; Chymosin (EC 3.4.23.4)
    Language English
    Publishing date 2022-08-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 2091377-1
    ISSN 1475-2859 ; 1475-2859
    ISSN (online) 1475-2859
    ISSN 1475-2859
    DOI 10.1186/s12934-022-01904-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Comparison of Activity and Safety of DSPAα1 and Its N-Glycosylation Mutants.

    Peng, Huakang / Wang, Nan / Wang, Mengqi / Yang, Caifeng / Guo, Wenfang / Li, Gangqiang / Huang, Sumei / Wei, Di / Liu, Dehu

    Life (Basel, Switzerland)

    2023  Volume 13, Issue 4

    Abstract: DSPAα1 is a potent rude thrombolytic protein with high medicative value. DSPAα1 has two natural N-glycan sites (N153Q-S154-S155, N398Q-K399-T400) that may lead to immune responses when administered in vivo. We aimed to study the effect of its N- ... ...

    Abstract DSPAα1 is a potent rude thrombolytic protein with high medicative value. DSPAα1 has two natural N-glycan sites (N153Q-S154-S155, N398Q-K399-T400) that may lead to immune responses when administered in vivo. We aimed to study the effect of its N-glycosylation sites on DSPAα1 in vitro and in vivo by mutating these N-glycosylation sites. In this experiment, four single mutants and one double mutant were predicted and expressed in
    Language English
    Publishing date 2023-04-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662250-6
    ISSN 2075-1729
    ISSN 2075-1729
    DOI 10.3390/life13040985
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Different N-Glycosylation Sites Reduce the Activity of Recombinant DSPAα2.

    Peng, Huakang / Wang, Mengqi / Wang, Nan / Yang, Caifeng / Guo, Wenfang / Li, Gangqiang / Huang, Sumei / Wei, Di / Liu, Dehu

    Current issues in molecular biology

    2022  Volume 44, Issue 9, Page(s) 3930–3947

    Abstract: Bat plasminogen activators α2 (DSPAα2) has extremely high medicinal value as a powerful natural thrombolytic protein. However, wild-type DSPAα2 has two N-glycosylation sites (N185 and N398) and its non-human classes of high-mannose-type N-glycans may ... ...

    Abstract Bat plasminogen activators α2 (DSPAα2) has extremely high medicinal value as a powerful natural thrombolytic protein. However, wild-type DSPAα2 has two N-glycosylation sites (N185 and N398) and its non-human classes of high-mannose-type N-glycans may cause immune responses in vivo. By mutating the N-glycosylation sites, we aimed to study the effect of its N-glycan chain on plasminogen activation, fibrin sensitivity, and to observe the physicochemical properties of DSPAα2. A logical structure design was performed in this study. Four single mutants and one double mutant were constructed and expressed in
    Language English
    Publishing date 2022-08-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2000024-8
    ISSN 1467-3045 ; 1467-3037
    ISSN (online) 1467-3045
    ISSN 1467-3037
    DOI 10.3390/cimb44090270
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5122: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: A Na

    Guo, Wenfang / Li, Gangqiang / Wang, Nan / Yang, Caifeng / Zhao, Yanan / Peng, Huakang / Liu, Dehu / Chen, Sanfeng

    Plant molecular biology

    2020  Volume 102, Issue 4-5, Page(s) 553–567

    Abstract: Key message: Overexpression of K2-NhaD in transgenic cotton resulted in phenotypes with strong salinity and drought tolerance in greenhouse and field experiments, increased expression of stress-related genes, and improved regulation of metabolic ... ...

    Abstract Key message: Overexpression of K2-NhaD in transgenic cotton resulted in phenotypes with strong salinity and drought tolerance in greenhouse and field experiments, increased expression of stress-related genes, and improved regulation of metabolic pathways, such as the SOS pathway. Drought and salinity are major abiotic stressors which negatively impact cotton yield under field conditions. Here, a plasma membrane Na
    MeSH term(s) Droughts ; Gossypium/genetics ; Gossypium/metabolism ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Plant Proteins/physiology ; Plants, Genetically Modified/metabolism ; Salt Tolerance/genetics ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism ; Sodium-Hydrogen Exchangers/physiology ; Stress, Physiological ; Water/metabolism
    Chemical Substances Plant Proteins ; Sodium-Hydrogen Exchangers ; Water (059QF0KO0R)
    Language English
    Publishing date 2020-01-27
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 778032-1
    ISSN 1573-5028 ; 0167-4412
    ISSN (online) 1573-5028
    ISSN 0167-4412
    DOI 10.1007/s11103-020-00969-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3458: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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