The Impact of Thermal and pH Variations on the Structure of Cathepsin D in the Hepatopancreas of Japanese Clam (Ruditapes philippinarum)
cathepsin D from <i>R. philippinarum</i> exhibited high thermostability up to 50°C and activity at pH 2-4. Its stability and characteristics are comparable to those of other species, which opens avenues in biotechnology for protein hydrolysis and peptide production.
Authors
- Francisco J. Cinco‐Moroyoqui (ORCID: https://orcid.org/0000-0001-8599-702X)
- Alonso A. López-Zavala (ORCID: https://orcid.org/0000-0001-9843-3709)
- Francisco Cadena-Cadena (ORCID: https://orcid.org/0000-0001-5409-3909)
- José Luis Cárdenas-López (ORCID: https://orcid.org/0000-0003-3265-1724)
- Ofelia Rouzaud‐Sández (ORCID: https://orcid.org/0000-0002-6541-6782)
- Ignacio Alfredo Rivero (ORCID: https://orcid.org/0000-0003-4920-6379)
- Hisila Santacruz‐Ortega (ORCID: https://orcid.org/0000-0002-7123-8791)
- Ezquerra-Brauer Josafat Marina
Institutions
- Universidad de Sonora (MX)
- Tecnológico Nacional de México (MX)
- Instituto Tecnológico de Tijuana (MX)
Publication Details
- Journal
- Current Protein and Peptide Science
- Published
- 2025-02-04
- DOI
- https://doi.org/10.2174/0113892037244173241206055736
- Primary Topic
- Protein Hydrolysis and Bioactive Peptides
- Type
- article
- Field-Weighted Citation Impact
- 0.00