This study illustrated the texture changes of -inoculated during refrigerated storage with the exogenous addition of SS-128. The group inoculated with SS-128 had an improved texture compared with that inoculated with the -mutant group (Δ). Proteomics were conducted to analyze the protein alterations in and supernatant, respectively. During storage, many texture-related proteins, including myosin heavy chain and beta-actin, were maintained due to . Some endogenous enzymes related to the energy metabolism and hydrolysis of were downregulated. The -induced interaction with showed significant changes in the expression of some critical enzymes and pathways. The ATP-dependent zinc metalloprotease FtsH and protease subunit HslV were downregulated, and the oxidative phosphorylation and glycosaminoglycan degradation pathways in were inhibited, resulting in the slow deterioration of . By exploring the mechanism underlying SS-128-led manipulation of the metabolism of spoilage bacteria, we clarified the texture maintenance mechanism of in SS-128, providing theoretical evidence for SS-128 application in food preservation.
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| http://dx.doi.org/10.3389/fmicb.2022.892788 | DOI Listing |
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