ArticleJournal of biological engineering2025
Enhanced enzyme activity and stability through immobilization of recombinant chitinase on sodium alginate-modified rice husk beads for efficient decolorization of synthetic dyes.
Article in Journal of biological engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
- Effect of high hydrostatic pressure on D-amino acid oxidase activity and stability.Journal of biological engineering · 2026Article
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3 authors.
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Abstract
backgroundThe energy efficiency and environmental friendliness of recombinant chitinase A make it a promising candidate for industrial applications as a sustainable catalyst. For the first time, a very stable and an efficient biocatalyst was developed to decolorize synthetic dyes by immobilizing Serratia marcescens chitinase A (SmChiA) onto beads comprised of sodium alginate (SA) and modified rice husk powder (mRHP). The mRHP was produced by treating rice husk powder with citric acid, which was then combined with SA at three different concentrations (25, 50 and 100% of SA weight) and cross-linked with calcium chloride to form the beads. 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide facilitates the formation of amide bonds that covalently bind SmChiA to the beads. The effectiveness of the synthesis and immobilization processes was confirmed using characterization methods (scanning electron microscopy, SEM and Fourier transform infrared spectroscopy, FTIR).
resultsBeads with 50% mRHP and 1.75 UmL
conclusionA variety of dyes could be safely removed from the environment using our bioremediation procedures. To the best of our knowledge, no studies had been conducted on the application of immobilized chitinase for dye removal.
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