• Journal of Animal Science and Technology
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• v.47 no.6
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• pp.1033-1040
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• 2005

Protein function of ovotransferrin with various pH and temperature, and its antimicrobial characteristics were determined. Foaming ability of ovotransferrin was high in alkali condition (pH 11), then diminished as time follows. In acidic condition (pH 3.0), very little amount of foam was produced and disappeared promptly in 30min. However, neutral condition (pH 7.0) was revealed as the best area for foam production and foam stability of ovotransferrin. Temperature effect on foam stability of ovotransferrin showed that the highest foam was produced at 60℃. Ovotransferrin was shown weak antimicrobial activity against E. Coli, S .typhi, P. aerug and Candida albicans at dose of 12.5mg/ml and 25mg/ml. Anti-microbial effect of ovotransferrin with either lysozyme or albumine on pathogenic bacteria and fungi shows that the most effective dose was 25mg/ml, especially on S. typhi and C. albicans.

• Korean Chemical Engineering Research
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• v.50 no.4
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• pp.713-717
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• 2012

Approximately forty proteins in egg white have been widely studied for their functional properties. To develop a procedure of separation for pure and non-altered proteins from egg white, purification study was conducted to isolate lysozyme, ovotransferrin, and ovalbumin. Ion exchange cartridge can selectively separate proteins from egg white, and reversed-phase HPLC (RP-HPLC) could identify separated proteins. Proteins in egg white were purified by HI trap ion exchange cartridge SP and Q with buffers pH 8.0 and 5.2. C18 column (Phenomenex, USA) was used for RP-HPLC analysis and isocratic mobile phase was used with acetonitrile (ACN)/distilled water (DW)/trifluoroacetic acid (TFA) in the ratio of 50/50/0.1. Comparing the retention times of standards in RP-HPLC experiments showed that ovotransferrin, ovalbumin, and lysozyme in egg white were eluted successively in the RP-HPLC column after the pretreatment in SP and Q ion exchange cartridges.