Authors
Cheng Han, Huanle Gao, Zimeng Zhang, Zhuying Li, Jianxin Zhao, Shumao Cui, Yue Sun, Wenjie Li, Wenbo Liu, Hongtao Zhang
Published in
ACS synthetic biology. Jun 19, 2026. Epub Jun 19, 2026.
Abstract
N-Acetyllactosamine (LacNAc) serves as a key intermediate in the biosynthesis of 6'-sialyl-N-acetyllactosamine (6'-SLN) and 3'-sialyl-N-acetyllactosamine (3'-SLN), which are the predominant components of sialylated milk oligosaccharides (SMOs) in goat milk. Therefore, methods for high-efficiency and low-cost production of LacNAc are necessary for 6'-SLN and 3'-SLN production. In this study, a new strategy for LacNAc production through a whole-cell coupled fermentation approach using sucrose and N-acetylglucosamine (GlcNAc) as substrates was explored. First, the enzymatic activities of β-1,4-galactosyltransferase (Hpβ4GalT and HpGalT), which were involved in LacNAc biosynthesis, were evaluated; the results indicated that Hpβ4GalT exhibits a higher LacNAc synthesis capacity than HpGalT. Subsequently, LacNAc was synthesized using a whole-cell catalytic system based on multistrain coupling. Then, to further enhance the titer, Saccharomyces cerevisiae cells were introduced to enable energy regeneration, and a coexpression strategy was employed to minimize the cell density. Following the optimization of induction and coupled fermentation conditions, LacNAc production increased 6-fold. Finally, the fermentation optimization conditions were validated in a 5-L bioreactor, achieving a maximum LacNAc titer of 32.38 g/L and a substrate GlcNAc molar yield of 84.46%.
PMID:
42319757
Bibliographic data and abstract were imported from PubMed on 19 Jun 2026.
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