Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

The Lysozyme from Insect (Manduca sexta) Is a Cold-Adapted Enzyme

Author(s): Rogerio R. Sotelo-Mundo, Alonso A. Lopez-Zavala, Karina D. Garcia-Orozco, Aldo A. Arvizu-Flores, Enrique F. Velazquez-Contreras, Elisa M. Valenzuela-Soto, Arturo Rojo-Dominguez and Michael R. Kanost

Volume 14, Issue 8, 2007

Page: [774 - 778] Pages: 5

DOI: 10.2174/092986607781483688

Price: $65

Abstract

Enzymatic activity is dependent on temperature, although some proteins have evolved to retain activity at low temperatures at the expense of stability. Cold adapted enzymes are present in a variety of organisms and there is ample interest in their structure-function relationships. Lysozyme (E.C. 3.2.1.17) is one of the most studied enzymes due to its antibacterial activity against Gram positive bacteria and is also a cold adapted protein. In this work the characterization of lysozyme from the insect Manduca sexta and its activity at low temperatures is presented. Both M. sexta lysozymes natural and recombinant showed a higher content of α-helix secondary structure compared to that of hen egg white lysozyme and a higher specific enzymatic activity in the range of 5-30 °C. These results together with measured thermodynamic activation parameters support the designation of M. sexta lysozyme as a cold adapted enzyme. Therefore, the insect recombinant lysozyme is feasible as a model for structure-function studies for cold-adapted proteins.

Keywords: Lysozyme, insect, Manduca sexta, cold adapted, glycohydrolase


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy