{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T11:28:26Z","timestamp":1773055706036,"version":"3.50.1"},"reference-count":17,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2007,8,17]],"date-time":"2007-08-17T00:00:00Z","timestamp":1187308800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biotech &amp; Bioengineering"],"published-print":{"date-parts":[[2008,2,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Hyperimmune equine IgG is widely used as antivenom and anti\u2010rabies agents. This article discusses a membrane based enhanced hybrid bioseparation technique for efficient and scalable purification of equine immunoglobulin G (IgG) from horse serum. This technique is an improved version of a standard hybrid bioseparation technique developed within our group earlier for fractionation of human plasma proteins (Ghosh. 2004. J Membr Sci 237: 109\u2013117). In the presence of a high antichaotropic salt concentration, equine IgG is selectively and reversibly captured within a stirred cell membrane module from horse serum, partly due to precipitation and microfiltration, and partly due to hydrophobic interaction based membrane adsorption, while the impurities are washed out from the device. The reversibly sequestered IgG is then released by lowering the salt concentration which favor both dissolution of the precipitated IgG and desorption of the membrane bound IgG. The enhanced hybrid bioseparation technique improves the IgG recovery from the membrane module by switching from a stirring to non\u2010stirring mode during the IgG release phase. It also reduces membrane fouling by an appropriate pH switch. The effects of operating conditions on equine IgG capture were first systematically studied. The enhanced hybrid bioseparation technique was followed by an ultrafiltration step to remove ammonium sulfate and low molecular weight impurities. The equine IgG purity obtained under optimized conditions was 88% and its recovery was over 90%, both being significantly higher than corresponding values obtained using currently used purification techniques. Biotechnol. Bioeng. 2008;99: 625\u2013633. \u00a9 2007 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/bit.21614","type":"journal-article","created":{"date-parts":[[2007,8,17]],"date-time":"2007-08-17T13:20:06Z","timestamp":1187356806000},"page":"625-633","source":"Crossref","is-referenced-by-count":12,"title":["Purification of equine IgG using membrane based enhanced hybrid bioseparation technique: A potential method for manufacturing hyperimmune antibody"],"prefix":"10.1002","volume":"99","author":[{"given":"Lu","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinghua","family":"Sun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Raja","family":"Ghosh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2007,8,17]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(99)00177-4"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1006\/biol.2002.0329"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0376-7388(00)00397-5"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.memsci.2004.03.006"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.memsci.2006.04.023"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1086\/500470"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2005.08.004"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.chroma.2003.09.060"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1081\/CLT-120021113"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.4269\/ajtmh.2000.63.298"},{"key":"e_1_2_1_12_1","first-page":"132","article-title":"The action of proteolytic enzymes on the antitoxins and proteins in immune sera","volume":"20","author":"Pope CG","year":"1939","journal-title":"Br J Exp Pathol"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(94)90087-6"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jim.2003.07.014"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(91)90002-9"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(05)74319-1"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(02)00393-8"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jim.2006.05.002"}],"container-title":["Biotechnology and Bioengineering"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fbit.21614","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/analyticalsciencejournals.onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/bit.21614","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:06:40Z","timestamp":1760058400000},"score":1,"resource":{"primary":{"URL":"https:\/\/analyticalsciencejournals.onlinelibrary.wiley.com\/doi\/10.1002\/bit.21614"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,8,17]]},"references-count":17,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2008,2,15]]}},"alternative-id":["10.1002\/bit.21614"],"URL":"https:\/\/doi.org\/10.1002\/bit.21614","archive":["Portico"],"relation":{},"ISSN":["0006-3592","1097-0290"],"issn-type":[{"value":"0006-3592","type":"print"},{"value":"1097-0290","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,8,17]]}}}