Abstract
The biological activity (D-value determination) of eggshell membrane (ESM) was examined to determine the membrane components and mechanisms responsible for antibacterial activity. Biological and enzymatic activities (i.e., beta-N-acetylglucosaminidase [beta-NAGase], lysozyme, and ovotransferrin) of ESM denatured with trypsin, lipases, or heat were compared with those of untreated ESM. Trypsin-treated ESM lost all biological activity (D-values at 54 degrees C were 5.12 and 5.38 min for immobilized and solubilized trypsin, respectively) but showed no significant loss of enzymatic activities. Treatments with porcine lipase and a lipase cocktail did not impact biological or enzymatic activities. Heat denaturation of ESM (at 80 and 100 degrees C for 15 min) resulted in significant decreases in biological activity (D-values of 3.99 and 4.43 min, respectively) and loss of beta-NAGase activity. Lysozyme and ovotransferrin activities remained but were significantly reduced. Purified ESM and hen egg white components (i.e., beta-NAGase, lysozyme, and ovotransferrin) were added to Salmonella Typhimurium suspensions (in 0.1% peptone water) at varying concentrations to evaluate their biological activity. D-values at 54 degrees C were 4.50 an...Continue Reading
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