Pesint, Gozde BaydemirYungevis, Burcu ErenDemircelik, Isik Percin2025-01-062025-01-0620230959-39931573-097210.1007/s11274-023-03697-y2-s2.0-85166045519https://doi.org/10.1007/s11274-023-03697-yhttps://hdl.handle.net/20.500.14669/2629Invertase, an industrially significant glycoenzyme, was purified from baker's yeast using poly (2-Hydroxyethyl methacrylate) [PHema-Pba] cryogels functionalized with boronic acid. At subzero temperatures, PHema-Pba cryogels were synthesized and characterized using swelling tests, scanning electron microscopy, and Fourier-transform infrared spectroscopy. The surface area of the PHema- Pba cryogels was 14 m(2)/g with a swelling ratio of 88.3% and macroporosity of 72%. The interconnected macropores of PHema-Pba cryogels were shown via scanning electron microscopy. Invertase binding capacity of PHema-Pba cryogel was evaluated by binding studies in different pH, temperature, and interaction time conditions and the maximum Invertase binding of PHema-Pba cryogel was found as 15.2 mg/g. and 23.7 fold Invertase purification was achieved from baker's yeast using PHema-Pba cryogels. The results show that PHema-Pba cryogels have high Invertase binding capacity and may be used as an alternative method for enzyme purification via boronate affinity systems. [GRAPHICS] .eninfo:eu-repo/semantics/closedAccessInvertaseCryogelEnzyme purificationBaker's yeastSaccharomyces cerevisiaeArticle1037528302Q239WOS:001041358900002Q2