Affinity chromatography by Sameh Magdeldin

By Sameh Magdeldin

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2010; Turková, 1999). Fig. 6. g. exoglucanase and endoglucanase from Cellulomonas fimi or cellulase from Trichoderma harzianum, are able to specifically bind cellulose thanks to their cellulose-binding domain. These domains may be exploited as affinity tags for fusion proteins immobilization on cellulose supports, which are inert and exhibit only low non-specific affinity and are readily available. g. , Zymomonas mobilis extracellular invertase or Bacillus stearothermophilus L1 lipase. Alternative method using chemical coupling by glutaraldehyde was utilized for preparation of a conjugate containing glucose oxidase and cellulose-binding domain.

Affinity immobilization techniques exploit the selectivity of specific interactions, which occur in almost all important biological processes in living organisms. , 1997; Roy & Gupta, 2006; Saleemuddin, 1999). As mentioned earlier the major advantage of utilization of affinity interactions for enzyme immobilization lies in the selectivity of the method. Also the possibility to control the Affinity Interactions as a Tool for Protein Immobilization 35 orientation of immobilized enzyme and minimal conformational changes caused by this type of binding resulting in high retention of the immobilized molecule activity represent an important benefit.

Proc Natl Acad Sci U S A 39: 232-236 Lowe CR (1996) Analytical biotechnology. Curr Opin Biotechnol 7: 1-3 Lowe CR, Burton SJ, Burton NP, Alderton WK, Pitts JM, Thomas JA (1992) Designer dyes: 'biomimetic' ligands for the purification of pharmaceutical proteins by affinity chromatography. Trends Biotechnol 10: 442-448 Mattiasson B, (1999) Expanded bed chromatography (special issue), 8, 1-271. Morag E, Bayer EA, Wilchek M (1996) Reversibility of biotin-binding by selective modification of tyrosine in avidin.

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