期刊
SEPARATION SCIENCE AND TECHNOLOGY
卷 39, 期 12, 页码 2891-2914出版社
TAYLOR & FRANCIS INC
DOI: 10.1081/SS-200028791
关键词
downstream processing; HGMF; primary capture; purification
Different routes were screened for the preparation of superparamagnetic cation-exchange adsorbents for the capture of proteins using high-gradient magnetic fishing. Starting from a polyglutaraldehyde-coated base particle, the most successful of these involved attachment of sulphite to oligomers of epichlorohydrin formed on the particle surface. The resultant cation-exchanger had a maximum lysozyme binding capacity of 272 mg g(-1) and a dissociation constant of 0.73 muM. Using lysozyme as a model protein in small-scale studies, appropriate conditions were then selected for the capture of lactoperoxidase from sweet bovine whey. Subsequently, a high-gradient magnetic fishing process was constructed for the fractionation of whey, in which lactoperoxidase was purified 36-fold and concentrated 4.7-fold.
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