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• W2892337048 abstract "Uricase as an important healthcare-related protein is extensively used in the treatment of tumor lysis syndrome and in the manufacture of serum uric-acid diagnostic kits. In this study, a gene of a new thermostable uricase (KmUOX) was cloned from thermotolerant yeast Kluyveromyces marxianus. The uricase was fused with a self-cleaving intein and cellulose-binding affinity tag and expressed in Escherichia coli BL21 (DE3). Through the binding to inexpensive cellulose and in situ intein cleavage induced by a pH change, tag-free uricase (KmUOX) was efficiently purified with a 77.11% yield via a single-step column purification strategy. This tag-free uricase showed Km, Vmax, and Kcat values of 67.60 µM, 56.35 µM/(min mg), and 32.74 S−1, respectively. Furthermore, this pure uricase was relatively thermostable and retained 79.75% of activity when incubated at 40 °C for 90 h. Thus, this pH-induced self-cleavable intein system combined with a cellulose matrix for affinity chromatography is proven here to be an effective and low-cost method for recombinant-uricase purification. Moreover, the stability of KmUOX makes it useful for clinical applications." @default.
• W2892337048 created "2018-09-27" @default.
• W2892337048 creator A5000134126 @default.
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• W2892337048 date "2018-09-01" @default.
• W2892337048 modified "2023-10-11" @default.
• W2892337048 title "Efficient purification of a recombinant tag-free thermostable Kluyveromyces marxianus uricase by pH-induced self-cleavage of intein and expression in Escherichia coli" @default.
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• W2892337048 doi "https://doi.org/10.1007/s13205-018-1422-9" @default.
• W2892337048 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6128813" @default.
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