Thermodynamic activation and structural analysis of trypsin I from Monterey sardine (Sardinops sagax caerulea)

Autor:	Facundo M. Fernández, Aldo A. Arvizu-Flores, Rogerio R. Sotelo-Mundo, Francisco Javier Castillo-Yáñez, Idania E. Quintero-Reyes, Gloria Yepiz-Plascencia, Maria A. Islas-Osuna, Ramón Pacheco-Aguilar, Martha Felix-Lopez, Enrique F. Velazquez-Contreras, Arti T. Navare
Rok vydání:	2012
Předmět:	chemistry.chemical_classification Serine protease Protease Molecular model biology medicine.medical_treatment Sardine General Medicine Trypsin Analytical Chemistry Enzyme chemistry Biochemistry biology.protein medicine Enzyme kinetics Peptide sequence Food Science medicine.drug
Zdroj:	Food Chemistry. 133:898-904
ISSN:	0308-8146
Popis:	In this work, we report the molecular characterisation of trypsin I (Try I) from Monterey sardine (Sardinops sagax caerulea). Aspects such as thermodynamic activation parameters, molecular model and cDNA-deduced amino acid sequence allow a more in depth understanding of its activity at low temperatures. The analysis of the thermodynamic activation parameters suggests that this molecule is a cold-adapted protease. From the molecular cloning, we deduced the amino acid sequence and predicted a theoretical structural model of sardine Try I with a classical trypsin fold. Cold-adaptation of this enzyme probably comes from amino acid replacement of key residues to improve flexibility at low temperature, thus increasing kcat. The cold-adaptation of sardine Try I opens a wide range of biotechnological applications for this protease and also it is interesting from the structure function relationship point of view of serine protease proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::bb4fb32821762c9ed8176b4d955fd45c https://doi.org/10.1016/j.foodchem.2012.01.111 Zobrazit plný text záznamu Full Text from ScienceDirect