Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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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, Michael R. Kanost.

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

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Article Details

VOLUME: 14
ISSUE: 8
Year: 2007
Page: [774 - 778]
Pages: 5
DOI: 10.2174/092986607781483688
Price: $58