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Title: The Lysozyme from Insect (Manduca sexta) is a Cold-Adapted Enzyme

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 {alpha}-helix secondary structure compared to that of hen egg white lysozyme and a higher specific enzymatic activity in the range of 5-30 {sup o}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.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930049
Report Number(s):
BNL-80674-2008-JA
TRN: US200822%%1278
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Protein and Peptide Letters; Journal Volume: 14; Journal Issue: 8
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BACTERIA; CHICKENS; EGGS; ENZYME ACTIVITY; ENZYMES; INSECTS; LYSOZYME; PROTEINS; STABILITY; TEMPERATURE DEPENDENCE; TEMPERATURE RANGE 0065-0273 K; THERMODYNAMICS; national synchrotron light source

Citation Formats

Sotelo-Mundo,R., Lopez-Zavala, A., Garcia-Orozco, K., Arvizu-Flores, A., Velazquez-Contreras, E., Valenzuela-Soto, E., Rojo-Dominguez, A., and Kanost, M.. The Lysozyme from Insect (Manduca sexta) is a Cold-Adapted Enzyme. United States: N. p., 2007. Web. doi:10.2174/092986607781483688.
Sotelo-Mundo,R., Lopez-Zavala, A., Garcia-Orozco, K., Arvizu-Flores, A., Velazquez-Contreras, E., Valenzuela-Soto, E., Rojo-Dominguez, A., & Kanost, M.. The Lysozyme from Insect (Manduca sexta) is a Cold-Adapted Enzyme. United States. doi:10.2174/092986607781483688.
Sotelo-Mundo,R., Lopez-Zavala, A., Garcia-Orozco, K., Arvizu-Flores, A., Velazquez-Contreras, E., Valenzuela-Soto, E., Rojo-Dominguez, A., and Kanost, M.. Mon . "The Lysozyme from Insect (Manduca sexta) is a Cold-Adapted Enzyme". United States. doi:10.2174/092986607781483688.
@article{osti_930049,
title = {The Lysozyme from Insect (Manduca sexta) is a Cold-Adapted Enzyme},
author = {Sotelo-Mundo,R. and Lopez-Zavala, A. and Garcia-Orozco, K. and Arvizu-Flores, A. and Velazquez-Contreras, E. and Valenzuela-Soto, E. and Rojo-Dominguez, A. and Kanost, M.},
abstractNote = {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 {sup o}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.},
doi = {10.2174/092986607781483688},
journal = {Protein and Peptide Letters},
number = 8,
volume = 14,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}