IJAIR NAAS Score : 3.99 ,ISSN : 2319-1473

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    The Effect of Fusion Tags on Enzyme Specificity and Protein Purification Efficiency

    Sercan Karav; Ebru Talak; Melis Tuncer; Adem Ozleyen
    Recombinant proteins are produced from recombinant DNA by using molecular technologies, and used in many working areas such as biotechnology, biomedical field and industry. However, purification of the recombinant protein is one of the most challenging steps of this process. Affinity tags are highly efficient tools to obtain the recombinant proteins with high yield and purity. They are used to facilitate the purification and detection of proteins, alongside the separation of protein complexes. Moreover, these tags might alter the enzymes specificity allowing the manipulation of the desired enzymatic reactions. Especially milk glycoproteins contain glycosidically attached a wide variety of conjugated glycans that have different biological functions. These bioactive glycans are isolated by the application of various glycosidases. Recent studies suggest that specific glycan types can be produced by affinity tag- enzyme complexes that alter the enzymes target glycan type. Such a manipulation on glycan production enables further studies on individual glycan structures and their contribution to the function of glycoproteins. In this review, we discuss various affinity tags; poly his, glutathione S-transferase (GST), maltose- binding protein (MBP), FLAG tag and other tags in the terms of their purification efficiency and substrate specificity
    Select Volume / Issue:
    Year:
    2017
    Type of Publication:
    Article
    Keywords:
    Affinity Tags; Enzyme Specificity; Glycans; Protein Purification; Recombinant Protein
    Journal:
    IJAIR
    Volume:
    6
    Number:
    3
    Pages:
    460-466
    Month:
    November
    ISSN:
    2319-1473
    Hits: 2835

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