4.7 Review

Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts

期刊

BIOTECHNOLOGY ADVANCES
卷 33, 期 5, 页码 435-456

出版社

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biotechadv.2015.03.006

关键词

Controlled immobilization; Enzyme stabilization; Multimeric enzymes; Chimeric proteins; Covalent attachment; Ionic exchange; IMAC

资金

  1. Spanish MINECO [CTQ2013-41507-R]
  2. COLCIENCIAS [1102-489-25428]
  3. Universidad Industrial de Santander (VIE-UIS Research Program) (Colombia)
  4. CNPq (Brazil) [403505/2013-5]
  5. Spanish MINECO for a Ramon y Cajal fellowship [RyC-2009-03813]

向作者/读者索取更多资源

In this review, we detail the efforts performed to couple the purification and the immobilization of industrial enzymes in a single step. The use of antibodies, the development of specific domains with affinity for some specific supports will be revised. Moreover, we will discuss the use of domains that increase the affinity for standard matrices (ionic exchangers, silicates). We will show how the control of the immobilization conditions may convert some unspecific supports in largely specific ones. The development of tailor-made heterofunctional supports as a tool to immobilize-stabilize-purify some proteins will be discussed in deep, using low concentration of adsorbent groups and a dense layer of groups able to give an intense multipoint covalent attachment. The final coupling of mutagenesis and tailor made supports will be the last part of the review. (C) 2015 Elsevier Inc. All rights reserved.

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