β-Lactamases and extended-spectrum β-lactamases (ESBLs) producing pathogenic bacteria were widely studied previously in China, but were seldom focused on foodborne Salmonella. In this study, an investigation concerning β-lactamases and ESBLs producing Salmonella recovered from retail raw chickens was performed. Sixty of 699 foodborne Salmonella isolates were detected as β-lactamases and ESBLs-producing ones that covered 12 Salmonella serotypes and exhibited different pulsed-field gel electrophoresis genotypes. Forty-four of 60 β-lactamases and ESBLs-producing strains were simultaneously resistant to ampicillin, amoxicillin/clavulanic acid, ceftiofur, ceftriaxone, and cefoxitin. The most commonly detected β-lactamases and ESBLs-encoding gene was blaTEM-1 (n=44), followed by blaOXA-1 (n=38), blaCMY-2 (n=29), blaPSE-1-like (n=1), blaCTX-M-3 (n=16), and blaCTX-M-15 (n=1), respectively. Fourteen, 24, 21, and 1 isolates were detected simultaneously positive for 1, 2, 3, and 4 of the detected β-lactamases and ESBLs-encoding genes, respectively. A Salmonella strain simultaneously co-carrying blaTEM-1, blaOXA-1, blaCMY-2, and blaCTX-M-3 was first reported in the present study. Amino acid substitution of Trp244Cys/His247Leu was detected in PSE-1, Val218Asp in CMY-2, and Asp242Gly in CTX-M-15 enzymes, respectively. A difference was found among the amino acid sequences of the detected OXA-1, CMY-2, CTX-M, PSE-1, and TEM-1. The results demonstrated that β-lactamases and ESBLs were emerging and prevalent in foodborne Salmonella.