Molecular imprinting of bovine serum albumin and lysozyme within the matrix of polyampholyte hydrogels based on acrylamide, sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid and (3-acrylamidopropyl)trimethyl ammonium chloride

Alexey V. Shakhvorostov, Sarkyt E. Kudaibergenov

2021

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DOI 10.15328/cb1182
Data confidence 85 high
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Abstract

Molecularly-imprinted polyampholyte (MIP) hydrogels based on nonionic monomer – acrylamide (AAm), anionic monomer – sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS) and cationic monomer – (3-acrylamidopropyl)trimethyl ammonium chloride (APTAC) were obtained by immobilization of bovine serum albumin (BSA) and lysozyme in situ polymerization conditions. It was found that the best amphoteric hydrogel for sorption of BSA is APTAC-75H while for sorption of lysozyme is AMPS-75H. The sorption capacity of APTAC-75H and AMPS-75H with respect to BSA and lysozyme is 305.7 and 64.1-74.8 mg per 1 g of hydrogel respectively. Desorption of BSA and lysozyme from MIP template performed by aqueous solution of 1M NaCl is equal to 82-88%. Separation of BSA and lysozyme from their mixture was performed on MIP templates. The results of adsorption-desorption cycles of BSA on adjusted to BSA polyampholyte hydrogel APTAC-75H and of lysozyme on adjusted to lysozyme polyampholyte hydrogel AMPS-75H show that the mixture of BSA and lysozyme can be selectively separated with the help of MIP hydrogels.