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Updated: Jul 2, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Functional secretion of a type 1 antifreeze protein analogue by optimization of promoter, signal peptide,
Chuan-Mei Yeh1, Xin-Hui Huang, Chan-Whei Sue
1Department of Food Science and Biotechnology, National Chung-Hsing University, Taichung, Taiwan, Republic of China. cmyeh@nchu.edu.tw
Abstract:
Lactococcus lactis is a food-grade microorganism of major commercial importance. Antifreeze protein is a potent cryogenic protection agent for the cryopreservation of food and pharmaceutical materials. In this study, extracellular expression of a novel recombinant type I antifreeze protein analogue (rAFP) in L. lactis was optimized. An efficient SlpA promoter (P SlpA) was fused to various signal peptides (SPs) and propeptide sequences to examine the extracellular expression levels of rAFP. An efficient signal peptide, SP sacB, fused to prosequence AE, enabled higher extracellular rAFP production; use of the SlpA terminator (Ter SlpA) was a further improvement. The extracellularly expressed rAFP successfully inhibited ice recrystallization and is thus potentially applicable for cryogenic preservation.
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