Ultrasound-assisted extraction of emodin from Rheum officinale Baill and its antibacterial mechanism against Streptococcus suis based on CcpA

• Published in: Ultrasonics sonochemistry 2024-01, Vol.102, p.106733-106733, Article 106733
• Main Authors: Bai, Jingwen, Xie, Yu, Li, Miao, Huang, Xianjun, Guo, Yujia, Sun, Jingwen, Tang, Yang, Liu, Xuantong, Wei, Chi, Li, Jianqiang, Yang, Yu
• Format: Article
• Language: English
• Subjects: Antibacterial mechanism; Catabolite control protein A; Emodin; Original; Streptococcus suis; Ultrasound-assisted extraction
• ISSN: 1350-4177; 1873-2828
• DOI: 10.1016/j.ultsonch.2023.106733

Emodin was extracted from Rheum officinale Baill by ultrasound-assisted extraction (UAE), and ethanol was chosen as the suitable solvent through SEM and molecular dynamic simulation. Under the optimum conditions (power 541 W, time 23 min, liquid to material ratio 13:1 mL/g, ethanol concentration 83 %) predicted by RSM, the yield of emodin was 2.18 ± 0.11 mg/g. Moreover, ultrasound power and time displayed the significant effects on the extraction process. Extracting dynamics analysis indicated that the extraction process of emodin by UAE conformed to Fick's second diffusion law. The results of antibacterial experiments suggested that emodin can damage cell membrane and inhibit the expression of cps2A, sao, mrp, epf, neu and the hemolytic activity of S. suis. Biolayer interferometry and FT-IR multi-peak fitting assays demonstrated that emodin induced a secondary conformational shift in CcpA. Molecular docking and molecular dynamics confirmed that emodin bound to CcpA through hydrogen bonding (ALA248, GLU249, GLY129 and ASN196) and π-π T-shaped interaction (TYR225 and TYR130), and the mutation of amino acid residues affected the affinity of CcpA to emodin. Therefore, emodin inhibited the sugar utilization of S. suis through binding to CcpA, and CcpA may be a potential target to inhibit the growth of S. suis.