The intensive use of antibiotics as growth-promoting agents in animal production has resulted in the spread of animal antibiotic resistance and possibly human antibiotic resistance. Based on this premise, it is significant to explore an alternative approach to preventing infectious diseases and promoting animal growth and health. Yeast as the main natural growth promoter in livestock nutrition has been extensively studied for decades. Numerous yeasts and yeast-containing products are produced, marketed, and used in animal feed as providers of nutrient sources, probiotics, and nutrients or serve distinct nutritional functions. A large amount of scientific research suggests that yeasts and their derivatives may be good for animal growth performance and health, especially when animals are housed in poor sanitation or are suffering from disease. However, when yeasts are used as a surrogate for livestock antibiotics, the results vary according to several factors, including yeast species, yeast product components, feed ingredients, animal category, type of symptoms, and differences in the rearing environment. In this review, the effects of different yeasts on different animals will be reviewed. The types of widely used yeast products, their functional characteristics, and application effects will be discussed in order to provide a reference for the development and application of yeast feed products.

Listeria monocytogenes is a food-borne pathogen. Pediocin is a group IIα bacteriocin with anti-listeria activity that is naturally produced by Pediococcus acidilactic and Lactobacillus plantarum. The pedA/papA gene encodes pediocin/plantaricin. In native hosts, the expression and secretion of active PedA/PapA protein rely on the accessory protein PedC/PapC and ABC transporter PedD/PapD on the same operon. The excretion machines were also necessary for pediocin protein expression in heterologous hosts of E. coli, Lactobacillus lactis, and Corynebacterium glutamicum. In this study, two vectors carrying the codon sequence of the mature PapA peptide were constructed, one with and one without a His tag. Both fragments were inserted into the plasmid pHT43 and transformed into Bacillus subtilis WB800N. The strains were induced with IPTG to secrete the fused proteins PA1 and PA2. Supernatants from both recombinant strains can inhibit Listeria monocytogenes ATCC54003 directly. The fused protein possesses inhibition activity as a whole dispense with removal of the leading peptide. This is the first report of active pediocin/PapA expression without the assistance of PedCD/PapCD in heterogeneous hosts. In addition, the PA1 protein can be purified by nickel-nitrilotriacetic acid (Ni-NTA) metal affinity chromatography.