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• W4313560219 abstract "SpyTag and SpyCatcher can rapidly conjugate covalently to form an irreversible covalent bond. Fusing SpyTag and SpyCatcher to the termini of a protein of interest enables the generation of SpyRing structure, which is often helpful for the stability of protein. In this paper, green fluorescent protein (GFP), L-phenylserine aldolase (LPA) and SRGFP, SRLPA (their SpyRing cyclized form) were covalently bound to glyoxyl-agarose (Gx) beads to prepare immobilized enzymes (Gx-GFP, Gx-LPA, Gx-SRGFP and Gx-SRLPA) with different protein loadings, and the effects of the SpyRing structure on solid-phase refolding were investigated. When the immobilized enzyme was inactivated in high concentrations of N, N-dimethylformamide (DMF) and 9 M guanidine hydrochloride, then reactivated with refolding buffer, the results showed that proteins with the SpyRing structure had a higher renaturation yield than their wild-type counterparts in all three replication cycles. The highest renaturation yields of Gx-SRGFP and Gx-SRLPA were over 90 % and 70 % respectively, which were approximately 15 % and 30 % higher than those of Gx-GFP and Gx-LPA. It suggests that the introduction of the SpyRing structure facilitates the reactivation of immobilized biocatalysts and provides a reference for the regeneration and recycling of industrial biocatalysts." @default.
• W4313560219 created "2023-01-06" @default.
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• W4313560219 date "2023-03-01" @default.
• W4313560219 modified "2023-10-14" @default.
• W4313560219 title "Effect of SpyTag/SpyCatcher cyclization on reactivation of covalently immobilized biocatalysts" @default.
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• W4313560219 doi "https://doi.org/10.1016/j.procbio.2023.01.005" @default.
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