The purification of lactoferrin from human whey by batch extraction |
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| Authors: | A A Foley G W Bates |
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| Affiliation: | 1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843 USA;2. Department of Animal Science, Texas A&M University, College Station, Texas 77843 USA;1. Department of Molecular Medicine, Sapienza University of Rome, Italy;2. Department of Paediatrics, Sapienza University of Rome, Italy;1. Department of Biology and Chemistry, College of Liberal Arts and Sciences, National University of Defense Technology, Changsha, Hunan, 410073, China;2. College of Life Science and Biotechnology, Shihezi University, Shihezi, 832000, China;1. Department of Dairy Technology, Faculty of Agriculture, Ankara University, Turkey;2. Department of Chemistry, Faculty of Science, Hacettepe University, Turkey |
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| Abstract: | The isolation of lactoferrin from human whey has been accomplished using a rapid two-step procedure. The lactoferrin is directly adsorbed to cellulose phosphate by batch extraction and eluted by a stepped salt and pH gradient. The major impurity, a low-molecular-weight fraction, is quickly removed by gel filtration. The recovered lactoferrin has a purity of about 96%. The yield of lactoferrin averaged 80%. This method of lactoferrin purification greatly reduces the labor and time required, and the procedure is easily scaled to any volume of starting material. |
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