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
