Resorcinol as Protective Agent in Thermochemical Modification of Lysozyme

Grzegorz Lesnierowski, Robert Borowiak*, Renata Cegielska-Radziejewska and Jerzy Stangierski

Department of Food Quality Management, Faculty of Food Science and Nutrition, Poznan University of Life Sciences, Wojska Polskiego 31, PL-60-624 Poznan, Poland

Article history:
Received April 27, 2012
Accepted January 9, 2013

Key words:
lysozyme, resorcinol, modification, oligomers, hydrolytic activity

Summary:
Thermochemical modification of lysozyme enables it to retain its oligomers, showing a wide spectrum of increased antibacterial activities. It also results in significant loss of hydrolytic activity of the enzyme. The objective of this study is to analyse the protective effect of resorcinol on the hydrolytic activity of modified lysozyme using a high temperature method and the oligomerization degree in the obtained preparations. Resorcinol significantly affects the enzyme’s hydrolytic activity. Samples containing resorcinol, without oxidizing agent, modified at 90 °C retained 75 % enzymatic activity of unmodified monomer, obtaining the final value of about 16 000 U/mg. The amount oflysozyme oligomers increased slightly in the samples produced under such conditions.

*Corresponding author:          boro@up.poznan.pl
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