Situs aktif CDH pada Phanerochaete chrysosporium terdiri dari dua subsites , subsite C katalitik dan B subsite yang mengikat substrat . Domain flavin pada PcCDH Phanerochaete chrysosporium yang telah bermutasi dalam residu F282 berhasil diekspresikan dalam Escherichia coli . Pergantian Phe282 ke Ala , Asp , dan His mengubah aktivitas enzimatik dan spesifisitas spesifisitas terhadap substrat. PcCDH wild-type berperan dengan efisien dalam mengoksidasi hanya selobiosa dan laktosa, sedangka tiga macam variasi Phe282 mampu menunjukkan aktivitas pada glukosa dan maltosa. Mutan mempertahankan sebagian besar aktivitasnya dengan selobiosa tetapi menunjukkan penurunan terhadap laktosa. Kemampuan untuk mengenali glukosa tersebut memberikan peluang besar untuk aplikasi di multibiosensor.

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The active site of cellobiose dehydrogenase from Phanerochaete chrysosporium is composed of two subsites, a catalytic C subsite and a substrate-binding B subsite. The soluble flavin domain of the Phanerochaete chrysosporium CDH that has mutated in residue F282 was successfully expressed in Escherichia coli. Substitution of Phe282 to Ala, Asp, and His changed 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 also showed activity to glucose and maltose. Mutant retained most of its activity with cellobiose but greatly decreased with lactose. The ability to recognize glucose provide great opportunities for the application in multibiosensor.