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• W4380182922 startingPage "105641" @default.
• W4380182922 abstract "The use of immobilized enzymes as biocatalysts in industrial bioprocesses has gained attention due to their catalytic efficiency and environmental benefits. Despite showing significant potential in numerous experiments, their practical applicability remains a challenge due to various factors such as the separation of materials after use, production costs, and resistance to stirring. In response, a polyacrylamide (PAM) bead was developed to support the enzyme utilizing the high hydrophilicity of PAM to promote enzyme activity. This study demonstrated a novel and straightforward technique for developing a PAM bead with wrinkles and a rough surface that can be filtered out easily. Instead of typical entrapment, the bead was chemically modified, achieving amine functionality at 3.8 mmol/g, then covalently coupled with xylanase, resulting in significant improvement in stability. The activity of PAM-xylanase was maintained at approximately 90% on day 30 of 30 °C incubation, which was at least 10 times more stable than the free enzyme. Moreover, the bead could be reused 5 times with a conversion of approximately 91% compared to its initial hydrolysis, making it a promising alternative to immobilized biocatalysts currently in use., making it a promising alternative to immobilized biocatalysts currently in use." @default.
• W4380182922 created "2023-06-11" @default.
• W4380182922 creator A5002041795 @default.
• W4380182922 creator A5024052846 @default.
• W4380182922 creator A5046322371 @default.
• W4380182922 date "2023-09-01" @default.
• W4380182922 modified "2023-10-16" @default.
• W4380182922 title "Novel fabrication via one-step polymerization and alginate cage-assisted shaping technique for polyacrylamide beads as a highly stable biocatalyst for xylan hydrolysis" @default.
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• W4380182922 doi "https://doi.org/10.1016/j.reactfunctpolym.2023.105641" @default.
• W4380182922 hasPublicationYear "2023" @default.
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