title: Enhanced catalytic and conformational stability of Atlantic cod trypsin upon neoglycosylation.
abstract: The applicability of psychrophilic enzymes is limited because of their lower thermodynamic stability in spite of their higher catalytic rate. In this study, we have shown that the thermodynamic stability of the psychrophilic Atlantic cod trypsin could be enhanced appreciably by covalent chemical modification with oxidized sucrose polymer without affecting its hydrolytic activity. The acquired stability of cod trypsin was found to be on par with the mesophilic porcine trypsin.
authors.affiliation: Centre for Protein Engineering and Biomedical Research, The Voluntary Health Services, Adayar, Chennai--600 113, India.
authors.forename: R
authors.initials: R
authors.lastname: Venkatesh
authors.forename: S
authors.initials: S
authors.lastname: Srimathi
authors.forename: A
authors.initials: A
authors.lastname: Yamuna
authors.forename: G
authors.initials: G
authors.lastname: Jayaraman
mesh_terms: D000818:Animals; D004795:Enzyme Stability; D048389:Gadus morhua / Q000378:metabolism*; D006031:Glycosylation; D019791:Guanidine; D007700:Kinetics; D011489:Protein Denaturation; D013816:Thermodynamics; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D014357:Trypsin; D019791:Guanidine