Egg white lysozyme purification with a chitin-silica based affinity chromatographic matrix

FEDERICO J. WOLMAN,; GUILLERMO J. COPELLO; ANDREA M. MEBERT; ALEXANDRA M. TARGOVNIK; MARÍA V. MIRANDA; AGUSTÍN A. NAVARRO DEL CAÑIZO; LUIS E. DÍAZ; OSVALDO CASCONE

EUROPEAN FOOD RESEARCH AND TECHNOLOGY

Springer, Life Sciences Editorial

Lugar: Nueva York; Año: 2010 vol. 231 p. 181 - 188

1438-2377

Abstract A composite biosorbent retaining noncovalentlybound chitin in between layers of a silicon oxidematrix was assessed for lysozyme purification from undilutedegg white. The matrix can be shaped with big size andhigh density, thus allowing its effcient separation from theegg white after the adsorption step. The lysozyme-depletedegg white can follow its usual commercialisation route.A surface area of 142 m2/g and a total pore volume of0.295 cm3/g were calculated from the nitrogen sorption isotherms.Its water content was 78.3%. The matrix structureis the result of the polysaccharide addition to the polymerisationmixture, which is known to inXuence the condensationprocess, leading to a material with characteristicproperties. A maximum capacity of 117.1 +/- 9 mg lysozyme/g and a dissociation constant of 0.73 +/- 0.15 mg/mLwere calculated from the Langmuir isotherm. A lysozymepurification batch process from undiluted egg white wasdeveloped, where 87% of the lysozyme was removed fromthe egg white and the matrix was easily recovered by a simplefiltration through a strainer. The overall yield of the processwas 64% with a purification factor of 20.