Chemical modification of oxalate decarboxylase to improve adsorption capacity

•Chemical modification of Oxdc with EDTAD was investigated.•SDS-PAGE and LC/MS results demonstrated that the modification reaction occurred at the N-terminus of the peptides.•The adsorption capacity of EDTAD-modified Oxdc onto calcium oxalate monohydrate crystals was higher than native Oxdc. In orde...

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Veröffentlicht in:International journal of biological macromolecules 2017-05, Vol.98, p.495-501
Hauptverfasser: Lin, Rihui, He, Junbin, Wu, Jia, Cai, Xinghua, Long, Han, Chen, Shengfeng, Liu, Haiqian
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Sprache:eng
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Zusammenfassung:•Chemical modification of Oxdc with EDTAD was investigated.•SDS-PAGE and LC/MS results demonstrated that the modification reaction occurred at the N-terminus of the peptides.•The adsorption capacity of EDTAD-modified Oxdc onto calcium oxalate monohydrate crystals was higher than native Oxdc. In order to enhance the adsorption capacity of oxalate decarboxylase (Oxdc) on calcium oxalate monohydrate crystals and improve the application performance of Oxdc, chemical modification of Oxdc with ethylenediaminetetraacetic dianhydride (EDTAD) was investigated in this work. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography tandem mass spectrometry (LC/MS) analysis results demonstrated that Oxdc and EDTAD have been covalently bound, and suggested that the chemical modification occurred at the free amino of the side chain and the α-amine of the N-terminus of Oxdc. Fluorescene and circular dichroic measurement showed that the structure and conformation of Oxdc were tinily altered after modification by EDTAD. The optimum pH of EDTAD-modified Oxdc was shifted to the alkaline side about 1.5 unit and it has a higher thermostability. The analysis of kinetic parameters indicated that the EDTAD-modified Oxdc showed a higher affinity towards the substrate. Through modification the adsorption capacity of Oxdc onto CaOx monohydrate crystals was increased by 42.42%.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2017.02.009