Abstract
Invertase, 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 m2/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.
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Authors performed the research equally. IPD carried out the characterization studies. GBP and IPD designed and wrote the paper.
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Baydemir Peşint, G., Eren Yüngeviş, B. & Perçin Demirçelik, I. Enhanced invertase binding from baker’s yeast via cryogels included boronic acids. World J Microbiol Biotechnol 39, 267 (2023). https://doi.org/10.1007/s11274-023-03697-y
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DOI: https://doi.org/10.1007/s11274-023-03697-y