ArticleApplied biochemistry and biotechnology2026
Enhancing Enzymatic Activity and Stability of Crude Laccase Through Encapsulation in Gelatin/Chitosan Hydrogel.
Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
Laccase is an environmentally friendly catalyst characterized by a wide substrate spectrum and clean reaction processes. It demonstrates the ability to efficiently oxidize various pollutants, with water being the sole by-product. Consequently, laccase holds significant potential for applications in diverse fields such as papermaking, environmental protection, food processing, and bioenergy production. In this study, crude laccase produced by Schizophyllum commune was immobilized within a composite material through chemical cross-linking to enhance the enzyme's activity and stability. Free laccase was immobilized using a gelatin/chitosan (GEL/CS) hydrogel, and the conditions for this process were optimized. Enzymatic properties of immobilized laccase (GEL/CS-laccase) were investigated to assess its potential applications. Results indicated that the maximum laccase activity by Schizophyllum commune reached 343.9 U·mL
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