Three-phase partitioning of trypsin inhibitor from legume seeds.

@article{Wati2009ThreephasePO,
  title={Three-phase partitioning of trypsin inhibitor from legume seeds.},
  author={Richa Kusuma Wati and Theerapong Theppakorn and Soottawat Benjakul and Saroat Rawdkuen},
  journal={Process Biochemistry},
  year={2009},
  volume={44},
  pages={1307-1314}
}

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The inhibitory activities of the inhibitor from these legumes were lost when they were treated with β-mercaptoethanol, indicating the subunit of polypeptide in its composition.

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TLDR
The structure of the TPP-treated proteinase K appears that the protein exists in an excited state which might be helping the enzyme to function more rapidly than the original enzyme in aqueous media.