文献类型：期刊文献

英文题名：Synergistic multi-enzyme system of Sphingobacterium sp. for enhanced penicillin G degradation: Pathways, proteomics, and binding dynamics analysis

作者：Zhang, Sinan[1,2,3];Wang, Zejian[3];Huang, Sheng[1,2];Sun, Huijie[3];Wu, Shiyong[1,2]

机构：[1]East China Univ Sci & Technol, Engn Res Ctr Resource Utilizat Carbon Containing W, Minist Educ, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, State Key Lab Coal Liquificat Gasificat & Utilizat, Shanghai 200237, Peoples R China;[3]East China Univ Sci & Technol, Dept Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2025

卷号：320

外文期刊名：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录：;EI(收录号：20252818761713);WOS:【SCI-EXPANDED(收录号:WOS:001537029000001)】；

基金：This work was supported by the financial support of research projects from the National Key Research and Development Program of China (No.2021YFC2101000) , Shanghai Scientific and Technological Innova-tion Action Plans-Scientific Instrument Development, China (grant No. 21142201300, 22142201000) , National Natural Science Foundation of China (No. 32071471)

语种：英文

外文关键词：Degradation products; Proteomics; Molecular docking

摘要：The persistent contamination of penicillin G sodium (PGNa) in pharmaceutical fermentation residues poses critical environmental and public health risks, demanding urgent global remediation strategies. While microbial degradation represents a promising solution, the enzymatic mechanisms governing PGNa detoxification remain poorly elucidated. This study demonstrates the exceptional PGNa degradation capacity of a multi-enzyme system derived from Sphingobacterium sp. SQW1. Notably, meropenem induction enhanced degradation enzyme activity by 13-fold compared to baseline levels. Furthermore, the effects of various mediators on the enzymatic catalysis of PGNa were systematically investigated. The degradation enzyme demonstrated robust thermal stability and broad pH adaptability, with particularly notable activity observed at 55 degrees C (1,585.32 U/mL). Through proteomics and binding analysis, AmpC was identified as the pivotal enzyme among 43 differentially expressed candidates, demonstrating strong PGNa affinity and catalytic stability. LC-MS-based pathway analysis identified three primary degradation routes: (3-lactam ring hydrolysis, penicillin acylase-mediated side chain cleavage, and oxidative decarboxylation/demethylation cascades. Our findings provide the first molecular-level characterization of PGNa degradation by bacterial enzyme complexes, establishing a groundbreaking framework for enzymatic bioremediation of (3-lactam antibiotic residues. This work advances both fundamental understanding and practical applications in waste fermentation residue management, offering an eco-efficient alternative to conventional antibiotic elimination technologies.