Characterization of "lettucine", a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting.

@article{Piero2002CharacterizationO,
  title={Characterization of "lettucine", a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting.},
  author={Angela Roberta Lo Piero and Ivana Puglisi and Goffredo Petrone},
  journal={Journal of agricultural and food chemistry},
  year={2002},
  volume={50 8},
  pages={2439-43}
}
In this work we focused on the characterization of a novel plant rennet purified from lettuce leaves (Lactuca sativa L. cv Romana). The lettuce protease, lettucine, showed trypsin-like, SV8-like, and caseinolytic activities. Although the enzyme did not recognize peptides having hydrophobic amino acid residues in the P(1) position of the target bond, it did show milk-clotting activity, suggesting that different bonds rather than the Phe(105)-Met(106) of the kappa-casein might be cleaved, still… CONTINUE READING

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