Metabolic Engineering of the 5-Aminolevulinate Biosynthetic Pathway in E. coli Improves Efficiency of Hemoprotein-Based Biocatalysis. [PDF]
Kato S +6 more
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Lignin-Degrading Enzymes and the Potential of <i>Pseudomonas putida</i> as a Cell Factory for Lignin Degradation and Valorization. [PDF]
Zhou Q, Fransen A, de Winde H.
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Intestinal Microecological Mechanisms of Aflatoxin B1 Degradation by Black Soldier Fly Larvae (<i>Hermetia illucens</i>): A Review. [PDF]
Yuan Q, Xia J, Ge C, Yao H.
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Characterization of the Coriolopsis gallica DyP for Its Potential to Biotransform Various Fluoroquinolones. [PDF]
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Characterization and optimization of azo dyes degrading microbes isolated from textile effluent. [PDF]
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Encapsulins: catalysis inside a shell. [PDF]
Fazal A, Giessen TW.
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Bitter Gourd (Momordica charantia) Peroxidase in Decolorization of Dyes from Tannery Effluent
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Characterization of dye-decolorizing peroxidase from Bacillus subtilis
Archives of Biochemistry and Biophysics, 2020The dye-decolorizing peroxidases (DyPs) belong to a unique heme peroxidase family for their biotechnological potential to detoxify synthetic dyes. In this work, we have biochemically and structurally characterized the dye-decolorizing peroxidase from Bacillus subtilis (BsDyP).
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The multihued palette of dye-decolorizing peroxidases
Archives of Biochemistry and Biophysics, 2015Dye-decolorizing peroxidases (DyPs; EC 1.11.1.19) are heme enzymes that comprise a family of the dimeric α+β barrel structural superfamily of proteins. The first DyP, identified relatively recently in the fungus Bjerkandera adusta, was characterized for its ability to catalyze the decolorization of anthraquinone-based industrial dyes. These enzymes are
Rahul Singh, Lindsay D. Eltis
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