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<p>The stability of digestive enzymes in macromolecular environments is critical for their performance during food processing, storage, and digestion. Here, the unfolding of porcine pancreatic lipase (PPL) in urea solutions supplemented with polyethylene glycol (PEG), dextran, Ficoll, or Pluronic were examined. By integrating fluorescence spectroscopy with stopped-flow kinetics, the unfolding progression were monitored and a quantitative model to elucidate the underlying mechanisms was developed. The results show that the unfolding pathway of PPL varies with the macromolecular medium, adopting two-, three-, or four-state models in Pluronic, PEG/dextran, and Ficoll 70, respectively, demonstrating that macromolecular crowding directs conformational transitions. A denaturant-binding model parameterized by τ (transition equilibrium constant) and m (cooperativity index) was established to quantitatively describe these processes. Together, this work offers mechanistic insight into how macromolecular surroundings shape the structural dynamics and function of digestive enzymes.</p> Graphical Abstract <p></p>

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Lipase Activity: The Effect of Macromolecules on Structural Transitions and Lipolysis Kinetics

  • 期刊论文

  • 发表日期：

    2025年12月11日

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  • Lei Wang,
  • Pan-Pan Chen,
  • Biao Wang,
  • Mi-Zhuan Li,
  • Yan Cheng,
  • Li Zhang,
  • Zhong-Xiu Chen

摘要

The stability of digestive enzymes in macromolecular environments is critical for their performance during food processing, storage, and digestion. Here, the unfolding of porcine pancreatic lipase (PPL) in urea solutions supplemented with polyethylene glycol (PEG), dextran, Ficoll, or Pluronic were examined. By integrating fluorescence spectroscopy with stopped-flow kinetics, the unfolding progression were monitored and a quantitative model to elucidate the underlying mechanisms was developed. The results show that the unfolding pathway of PPL varies with the macromolecular medium, adopting two-, three-, or four-state models in Pluronic, PEG/dextran, and Ficoll 70, respectively, demonstrating that macromolecular crowding directs conformational transitions. A denaturant-binding model parameterized by τ (transition equilibrium constant) and m (cooperativity index) was established to quantitatively describe these processes. Together, this work offers mechanistic insight into how macromolecular surroundings shape the structural dynamics and function of digestive enzymes.

Graphical Abstract