title: Biochemical characterisation of chymotrypsin from the midgut gland of yellowleg shrimp, Penaeus californiensis.
abstract: Chymotrypsin from shrimp, Penaeus californiensis, was compared to Bos taurus chymotrypsin, and its structure-function relationship was studied. Catalytic efficiency toward synthetic substrate is lower, but it has a broad specificity and higher activity toward protein substrates, including collagen. It is active at pH 4-10 and fully active up to 50 °C for 2 h and at least nine days at room temperature. The activation peptide is twice as long as bovine chymotrypsinogen, has less disulfide bridges, and is a single polypeptide. Only one activation step is necessary from chymotrypsinogen to the mature enzyme. Postmortem implications in muscle softening and melanisation, resistance to temperature and pH and efficiency with proteinaceous substrates make chymotrypsin useful as a biotechnological tool in food processing. This makes shrimp processing wastes useful as a material for production of fine reagents.
authors.affiliation: Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Calle IPN 195, La Paz, B.C.S. 23090, Mexico.
authors.forename: Maria A
authors.initials: MA
authors.lastname: Navarrete-del-Toro
authors.affiliation: Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Calle IPN 195, La Paz, B.C.S. 23090, Mexico. Electronic address: fgarcia@cibnor.mx.
authors.forename: Fernando L
authors.initials: FL
authors.lastname: García-Carreño
authors.affiliation: Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Calle IPN 195, La Paz, B.C.S. 23090, Mexico.
authors.forename: Patricia
authors.initials: P
authors.lastname: Hernández-Cortés
authors.affiliation: Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/C, H-1117 Budapest, Hungary.
authors.forename: Tamas
authors.initials: T
authors.lastname: Molnár
authors.affiliation: Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/C, H-1117 Budapest, Hungary; Molecular Biophysics Research Group, Hungarian Academy of Sciences-ELTE, Pázmány Péter sétány 1/C, H-1117 Budapest, Hungary.
authors.forename: Laszlo
authors.initials: L
authors.lastname: Gráf
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins / Q000737:chemistry* / Q000235:genetics; D055162:Biocatalysis; D002417:Cattle; D002918:Chymotrypsin / Q000737:chemistry* / Q000235:genetics; D004064:Digestive System / Q000737:chemistry / Q000201:enzymology; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D033561:Penaeidae / Q000737:chemistry / Q000201:enzymology*; D016415:Sequence Alignment
chemical_list: D060829:Arthropod Proteins; D002918:Chymotrypsin
keywords: Chymotrypsin; Collagenolytic activity; Crustacean proteases; Sensitivity to inhibitors; Shrimp; Substrate specificity