The lysozyme from insect (Manduca sexta) is a cold-adapted enzyme.
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 alpha-helix secondary structure compared to that of hen egg white lysozyme and a higher specific enzymatic activity in the range of 5-30 degrees 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.
Sotelo-Mundo
Rogerio R
RR
Departamento de Investigación en Polímeros y Materiales, Universidad de Sonora, Hermosillo, Sonora, México. rrs@ciad.mx
López-Zavala
Alonso A
AA
Garcia-Orozco
Karina D
KD
Arvizu-Flores
Aldo A
AA
Velázquez-Contreras
Enrique F
EF
Valenzuela-Soto
Elisa M
EM
Rojo-Dominguez
Arturo
A
Kanost
Michael R
MR
D000220:Adaptation, Biological; D000595:Amino Acid Sequence; D000818:Animals; D003080:Cold Temperature; D018402:Manduca / Q000201:enzymology*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins; D016415:Sequence Alignment; D013816:Thermodynamics
D011994:Recombinant Proteins; D009113:Muramidase