Paket Lengkap Mutation Study Of Cellobiose Dehydrogenase From Phanerocaete Crhysosporium In A Prokariotic System For Multiple Biosensor Application

Abstract: The active site of cellobiose dehydrogenase from Phanerochaete chrysosporium is composed of two subsites, catalytic C and substrate-binding B subsite. The soluble flavin domain of the Phanerochaete chrysosporium Cellobiose dehydrogenase (CDH) has been mutated in residue F282 and successfully expressed in Escherichia coli. Substitution of Phe282 to Ala, Asp, and His shown to affect its enzymatic activity and altered the enzyme’s substrate specificity. While the wild-type cellobiose dehydrogenase efficiently oxidizes only cellobiose and lactose, the three mutated Phe282 shown significant activity for glucose and maltose. For all mutants type, cellobiose has retain its maximum activity but greatly decreased with lactose. The ability of CDH to recognize glucose provide great opportunities for the application in multibiosensor.

Keywords: cellobiose dehidrogenase, Glukosa, Laktosa, Maltosa, Phanerochaete chrysosporium

Penulis: Epi Supri Wardi, Desriani Desriani, Erik Firdian

Kode Jurnal: jpfarmasidd170288

Sumber https://fisikamilenial.blogspot.com/

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