| Autor: |
Siriatcharanon AK; Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Sutheeworapong S; Division of Bioinformatics and Systems Biology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Baramee S; Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Waeonukul R; Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand.; Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Pason P; Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand.; Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Kosugi A; Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS), 1-1 Ohwashi, Tsukuba, Ibaraki 305-8686, Japan., Uke A; Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS), 1-1 Ohwashi, Tsukuba, Ibaraki 305-8686, Japan., Ratanakhanokchai K; Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand.; Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand., Tachaapaikoon C; Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand.; Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT), Bangkok 10150, Thailand. |
| Abstrakt: |
Cellobiose dehydrogenases (CDHs) are a group of enzymes belonging to the hemoflavoenzyme group, which are mostly found in fungi. They play an important role in the production of acid sugar. In this research, CDH annotated from the actinobacterium Cellulomonas palmilytica EW123 ( Cp CDH) was cloned and characterized. The Cp CDH exhibited a domain architecture resembling class-I CDH found in Basidiomycota. The cytochrome c and flavin-containing dehydrogenase domains in Cp CDH showed an extra-long evolutionary distance compared to fungal CDH. The amino acid sequence of Cp CDH revealed conservative catalytic amino acids and a distinct flavin adenine dinucleotide region specific to CDH, setting it apart from closely related sequences. The physicochemical properties of Cp CDH displayed optimal pH conditions similar to those of CDHs but differed in terms of optimal temperature. The Cp CDH displayed excellent enzymatic activity at low temperatures (below 30°C), unlike other CDHs. Moreover, Cp CDH showed the highest substrate specificity for disaccharides such as cellobiose and lactose, which contain a glucose molecule at the non-reducing end. The catalytic efficiency of Cp CDH for cellobiose and lactose were 2.05 x 10 5 and 9.06 x 10 4 (M -1 s -1 ), respectively. The result from the Fourier-transform infrared spectroscopy (FT-IR) spectra confirmed the presence of cellobionic and lactobionic acids as the oxidative products of Cp CDH. This study establishes Cp CDH as a novel and attractive bacterial CDH, representing the first report of its kind in the Cellulomonas genus. |
