TY - JOUR
T1 - Fabrication of Metal Ion-BSA Chelation-Targeted Surface-Imprinted Particles for Protein Separation
AU - Wang, Ting
AU - Lyu, Yanting
AU - Yang, Zuoting
AU - Cheng, Haichuan
AU - Zhang, Qiuyu
AU - Zhang, Baoliang
N1 - Publisher Copyright:
© 2023 American Chemical Society. All rights reserved.
PY - 2023/6/14
Y1 - 2023/6/14
N2 - The development of high-performance protein-imprinted materials for adsorption and separation to obtain high-purity, high-quality biomolecules is still one of the most important techniques to promote the rapid development of the protein drug industry. In this paper, a novel highly specific bovine serum albumin (BSA) cobalt-molybdenum double-hydroxides surface-imprinted composite particles (Co-Mo LDHs@MIPs) were constructed by the surface imprinting technique combined with metal chelation. ZIF-67 was etched by molybdate ions to obtain unique MOF-derived bimetallic hydroxide particles (Co-Mo LDHs), which were used as the carrier. The rough outer surface and bimetallic ion coordination of Co-Mo LDHs enable anchoring more template proteins. The adsorption capacity of Co-Mo LDHs@MIPs was up to 423.37 mg/g for BSA in 60 min with an imprinting factor of 2.65. In addition, Co-Mo LDHs@MIPs can selectively recognize and separate BSA from mixed proteins and fetal bovine serum and exhibit high reusability stability.
AB - The development of high-performance protein-imprinted materials for adsorption and separation to obtain high-purity, high-quality biomolecules is still one of the most important techniques to promote the rapid development of the protein drug industry. In this paper, a novel highly specific bovine serum albumin (BSA) cobalt-molybdenum double-hydroxides surface-imprinted composite particles (Co-Mo LDHs@MIPs) were constructed by the surface imprinting technique combined with metal chelation. ZIF-67 was etched by molybdate ions to obtain unique MOF-derived bimetallic hydroxide particles (Co-Mo LDHs), which were used as the carrier. The rough outer surface and bimetallic ion coordination of Co-Mo LDHs enable anchoring more template proteins. The adsorption capacity of Co-Mo LDHs@MIPs was up to 423.37 mg/g for BSA in 60 min with an imprinting factor of 2.65. In addition, Co-Mo LDHs@MIPs can selectively recognize and separate BSA from mixed proteins and fetal bovine serum and exhibit high reusability stability.
UR - http://www.scopus.com/inward/record.url?scp=85163405253&partnerID=8YFLogxK
U2 - 10.1021/acs.iecr.3c00582
DO - 10.1021/acs.iecr.3c00582
M3 - 文章
AN - SCOPUS:85163405253
SN - 0888-5885
VL - 62
SP - 9290
EP - 9301
JO - Industrial and Engineering Chemistry Research
JF - Industrial and Engineering Chemistry Research
IS - 23
ER -