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Biosynthesis of Chryseno[2,1,c]oxepin‑12‑Carboxylic Acid from Glycyrrhizic Acid in Aspergillus terreus TMZ05‑2, and Analysis of Its Anti‑inflammatory Activity
Liangliang Chen , Lin Zhao , Ju Han , Ping Xiao , Mingzhe Zhao , Sen Zhang , Jinao Duan
J. Microbiol. 2024;62(2):113-124.   Published online February 27, 2024
DOI: https://doi.org/10.1007/s12275-024-00105-4
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  • 3 Web of Science
  • 3 Crossref
AbstractAbstract
Glycyrrhizic acid, glycyrrhetinic acid, and their oxo, ester, lactone, and other derivatives, are known for their anti-inflammatory, anti-oxidant, and hypoglycemic pharmacological activities. In this study, chryseno[2,1-c]oxepin-12-carboxylic acid (MG) was first biosynthesized from glycyrrhizic acid through sequential hydrolysis, oxidation, and esterification using Aspergillus terreus TMZ05-2, providing a novel in vitro biosynthetic pathway for glycyrrhizic acid derivatives. Assessing the influence of fermentation conditions and variation of strains during culture under stress-induction strategies enhanced the final molar yield to 88.3% (5 g/L glycyrrhizic acid). CCK8 assays showed no cytotoxicity and good cell proliferation, and anti-inflammatory experiments demonstrated strong inhibition of NO release (36.3%, low-dose MG vs. model), transcriptional downregulation of classical effective cellular factors tumor necrosis factor-α (TNF-α; 72.2%, low-dose MG vs. model), interleukin-6 (IL-6; 58.3%, low-dose MG vs. model) and interleukin-1β (IL-1β; 76.4%, low-dose MG vs. model), and decreased abundance of P-IKK-α, P-IKB-α, and P-P65 proteins, thereby alleviating inflammatory responses through the NF-κB pathway in LPS-induced RAW264.7 cells. The findings provide a reference for the biosynthesis of lactone compounds from medicinal plants.

Citations

Citations to this article as recorded by  
  • Effect of different crosslinking agents on carboxymethyl chitosan-glycyrrhizic acid hydrogel: Characterization and biological activities comparison
    Yinbing Wu, Zimin Gu, Tingting Chen, Duntao Zu, Yuhui Gan, Honglin Chen, Jianni Yang, Xin Yu, Huaihong Cai, Pinghua Sun, Jianying Ning, Haibo Zhou, Junxia Zheng
    International Journal of Biological Macromolecules.2025; 298: 139977.     CrossRef
  • New oxepin and dihydrobenzofuran derivatives from Bauhinia saccocalyx roots and their anti-inflammatory, cytotoxic, and antioxidant activities
    Lueacha Tabtimmai, Thanyathon Phonchan, Natrinee Thongprik, Sutin Kaennakam, Nuttapon Yodsin, Kiattawee Choowongkomon, Chanikan Sonklin, Supachai Jadsadajerm, Awat Wisetsai
    Journal of Natural Medicines.2025;[Epub]     CrossRef
  • Efficient directional biosynthesis of isoquercitrin from quercetin by Bacillus subtilis CD-2 and its anti-inflammatory activity
    Ju Han, Jingru Ma, Ruiqi He, Fan Yang, Jingyi Meng, Jiaqi Liu, Fanxing Shi, Jinao Duan, Liangliang Chen, Sen Zhang
    Natural Product Research.2024; : 1.     CrossRef
Mutational analysis of the RNA helicase Dhh1 in Ste12 expression and yeast mating
Daehee Jung , Jihye Ahn , Boram Rhee , Jinmi Kim
J. Microbiol. 2017;55(5):373-378.   Published online April 29, 2017
DOI: https://doi.org/10.1007/s12275-017-7020-4
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  • 5 Crossref
AbstractAbstract
Dhh1 and Dhh1 homologues (RCK/p54/DDX6) are mem-bers of the DEAD-box protein family of RNA helicases. These proteins display conserved sequence motifs for ATPase and RNA binding activities. Dhh1 is a component of the P-bodies (processing bodies) of mRNA granules and functions as an mRNA decapping activator in Saccharomyces cerevisiae. Dhh1 also contributes to gene-specific regulation during yeast mating. The dhh1 deletion mutation results in a significant decrease in the expression of Ste12, a mating-specific trans-cription factor, showing severe mating defects. Here, we in-troduced amino-acid substitution mutations in the ATPase and RNA binding domains of Dhh1 and also constructed a deletion of 79 amino acids at the Q/P-rich C-terminal region. The mutations in ATPase A and B motif (K96R, D195A) and C-terminus deletion showed reduced levels of mating effi-ciency as well as Ste12 protein expression. The Q/P-rich C- terminal region of Dhh1 was dispensable for growth at non- permissive temperature 37°C but appeared to play an im-portant role in regulating the Ste12 protein expression and mating processes. The P-body accumulation induced by treatment with α-mating factor required ATPase, RNA-bind-ing and the Q/P-rich C-terminal domains of Dhh1.

Citations

Citations to this article as recorded by  
  • Fus3 and Tpk2 protein kinases regulate the phosphorylation-dependent functions of RNA helicase Dhh1 in yeast mating and Ste12 protein expression
    Jaehee Hwang, Daehee Jung, Jinmi Kim
    Journal of Microbiology.2022; 60(8): 843.     CrossRef
  • The Role of DEAD-Box ATPases in Gene Expression and the Regulation of RNA–Protein Condensates
    Karsten Weis, Maria Hondele
    Annual Review of Biochemistry.2022; 91(1): 197.     CrossRef
  • Roles of Dhh1 RNA helicase in yeast filamentous growth: Analysis of N-terminal phosphorylation residues and ATPase domains
    Eunji Lee, Daehee Jung, Jinmi Kim
    Journal of Microbiology.2020; 58(10): 853.     CrossRef
  • Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12
    Daehee Jung, Jong Seok Seo, Jayoung Nam, Jinmi Kim, Enrico Baruffini
    PLOS ONE.2019; 14(7): e0220137.     CrossRef
  • Roles of eIF4E-binding protein Caf20 in Ste12 translation and P-body formation in yeast
    Kiyoung Park, Yu-Seon Lee, Daehee Jung, Jinmi Kim
    Journal of Microbiology.2018; 56(10): 744.     CrossRef

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