Egg White Lysozyme Purification by Ultrafiltration and Affinity Chromatography |
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| Authors: | B H CHIANG C K SU G J TSAI G T TSAO |
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| Affiliation: | Authors Chiang and Su are with the Graduate Institute of Food Science &Technology, National Taiwan Univ. Taipei, Taiwan. Authors Tsai and Tsao are with the Laboratory of Renewable Resources Engineering, Purdue Univ., West Lafayette, IN. Address inquiries to Dr. B.H. Chiang. |
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| Abstract: | Isolation and purification of lysozyme from hen egg white was studied using a two-step procedure. The egg white was diluted 5- to 9-fold with sodium phosphate buffer, and then processed by sequential dilution diafiltration using a UF membrane (molecular weight cut-off 300,000 dalton). The membrane process increased the specific activity of lysozyme 6-fold, and recovered 96% of lysozyme activity. The permeate from diafiltration was further purified by affinity chromatography using chitin as adsorbent. The second step of the process yielded a product of specific activity of 70,400 units/mg protein. The overall lysozyme recovery was 79%. |
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| Keywords: | egg whites lysozyrne purification affinity chromotography |
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