Molecular imprinted particles for lysozyme purification


Odabasi M., Say R., Denizli A.

MATERIALS SCIENCE & ENGINEERING C-BIOMIMETIC AND SUPRAMOLECULAR SYSTEMS, cilt.27, sa.1, ss.90-99, 2007 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 27 Sayı: 1
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1016/j.msec.2006.03.002
  • Dergi Adı: MATERIALS SCIENCE & ENGINEERING C-BIOMIMETIC AND SUPRAMOLECULAR SYSTEMS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.90-99
  • Anahtar Kelimeler: molecular imprinting, molecular recognition, lysozyme purification, protein adsorption, affinity binding, SOLID-PHASE EXTRACTION, IMMUNOGLOBULIN-G, SEPARATION, PRECONCENTRATION, POLYMERS, BEADS, ADSORPTION, REMOVAL
  • Anadolu Üniversitesi Adresli: Hayır

Özet

Molecular recognition-based separation techniques have received much attention in chemistry and biology because of their high selectivity for target molecules. The aim of this study is to prepare lysozyme-imprinted polymers which can be used for the purification of lysozyme from aqueous solutions and egg white. N-methacryloyl-(L)-histidinemethylester (MAH) was chosen as the metal-complexing monomer. In the first step, Cu2+ was complexed with MAH and the lysozyme-imprinted poly(HEMA-MAH) [Lys-MIP] particles were synthesized by UV-initiated bulk polymerization. After that, the template (i.e., lysozyme) were removed using 0.1 M NaCl solution. The specific surface area of the Lys-MIP particles was found to be 22.9 m(2)/g with a size range of 20-63 mu m in diameter and the swelling ratio was 57%. According to the elemental analysis results, the particles contained 421 mu mol MAH/g polymer. The maximum lysozyme adsorption capacity was 12.1 mg/g polymer. The relative selectivity coefficients of imprinted particles for lysozyme/human serum albumin and lysozyme/cytochrome c were 3.6 and 4.1 times greater than NIP particles, respectively. Purification of lysozyme from egg-white was also monitored by determining the lysozyme activity using Micrococcus lysodeikticus as substrate. The purity of the desorbed lysozyme was about 89% with recovery about 84%. The Lys-MIP particles could be used many times without decreasing their adsorption capacities significantly. (c) 2006 Elsevier B.V. All rights reserved.