Here a versatile fusion tag composed of His-tag, intein, and elastin-like polypeptide (ELP) tag was prepared for the first time to be fused with levansucrase SacB to construct a recombinant His-ELP-intein-SacB (HEIS) protein to realize nonchromatographic purification of SacB. The efficient biomimetic mineralization of CaHPO4 and HEIS-based hybrid-hydrangea (CaHPO4-HEIS-HH) with good reusability, excellent storage stability and 254.3% improved relative levan yield was prepared with the biomimetic mineralization method. Additionally, the CaHPO4-HEIS-HH showed outstanding operation activity when catalyzing sucrose in solution and up to 75% sucrose conversion rate in fruit juices. The mechanism of biomimetic mineralization was analyzed to show that the HEIS protein might serve as a "binder" to assemble the nanoflakes during biomimetic mineralization. The CaHPO4-HEIS-HH was applicable for efficient production of the levan-type prebiotic polysaccharides, and this approach should be highly valuable for nonchromatographic purification and convenient preparation of various encapsulated enzymes for more efficient catalysis.
Keywords: Biocatalyst; Biomimetic mineralization; Elastin-like polypeptides; Levansucrase; hydrangea.
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