Chiang B.H.SU C.K.TSAI G.J.TSAO G.T.2019-07-112019-07-11199300221147https://scholars.lib.ntu.edu.tw/handle/123456789/413342Isolation 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%. Copyright ? 1993, Wiley Blackwell. All rights reservedaffinity chromotographyegg whiteslysozyrnepurificationjournal article10.1111/j.1365-2621.1993.tb04261.x2-s2.0-0342656403https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342656403&doi=10.1111%2fj.1365-2621.1993.tb04261.x&partnerID=40&md5=5f6df4da0103a2acd52c7ef93a7add79