ArticleBiotechnology reports (Amsterdam, Netherlands)2020
Enhanced enzymatic activity and stability by in situ entrapment of α-Glucosidase within super porous p(HEMA) cryogels during synthesis.
Article in Biotechnology reports (Amsterdam, Netherlands), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Smart responsive hydrogels combined with AI design for tumor therapy.Acta pharmaceutica Sinica. B · 2026Review
- Combining bioaffinity-ultrafiltration withFood chemistry: X · 2026Article
- Synthesis and Characterization of a New Cryogel Matrix for Covalent Immobilization of Catalase.Gels (Basel, Switzerland) · 2022Article
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5 authors.
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Abstract
Here, poly(2-hydroxyethyl methacrylate) (p(HEMA)) cryogel were prepared in the presence 0.48, 0.96, and 1.92 mL of α-Glucosidase enzyme (0.06 Units/mL) solutions to obtain enzyme entrapped superporous p(HEMA) cryogels, donated as α-Glucosidase@p(HEMA)-1, α-Glucosidase@p(HEMA)-2, and α-Glucosidase@p(HEMA)-3, respectively. The enzyme entrapped p(HEMA) cryogels revealed no interruption for hemolysis and coagulation of blood rendering viable biomedical application in blood contacting applications. The α-Glucosidase@p(HEMA)-1 was found to preserve its' activity% 92.3 ± 1.4 % and higher activity% against free α-Glucosidase enzymes in 15-60℃ temperature, and 4-9 pH range. The K
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