Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Discovery of a Novel Cellobiose Dehydrogenase from Cellulomonas palmilytica EW123 and Its Sugar Acids Production

  • Ake-kavitch Siriatcharanon (Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Sawannee Sutheeworapong (Division of Bioinformatics and Systems Biology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Sirilak Baramee (Excellent Center of Enzyme Technology and Microbial Utilization, Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Rattiya Waeonukul (Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Patthra Pason (Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Akihiko Kosugi (Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS)) ;
  • Ayaka Uke (Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS)) ;
  • Khanok Ratanakhanokchai (Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT)) ;
  • Chakrit Tachaapaikoon (Division of Biochemical Technology, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi (KMUTT))
  • Received : 2023.07.05
  • Accepted : 2023.09.20
  • Published : 2024.02.28
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Abstract

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 (CpCDH) was cloned and characterized. The CpCDH exhibited a domain architecture resembling class-I CDH found in Basidiomycota. The cytochrome c and flavin-containing dehydrogenase domains in CpCDH showed an extra-long evolutionary distance compared to fungal CDH. The amino acid sequence of CpCDH 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 CpCDH displayed optimal pH conditions similar to those of CDHs but differed in terms of optimal temperature. The CpCDH displayed excellent enzymatic activity at low temperatures (below 30℃), unlike other CDHs. Moreover, CpCDH 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 CpCDH for cellobiose and lactose were 2.05 × 105 and 9.06 × 104 (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 CpCDH. This study establishes CpCDH as a novel and attractive bacterial CDH, representing the first report of its kind in the Cellulomonas genus.

Keywords

Acknowledgement

We would like to thank and gratefully acknowledge the financial support given by Petchra Pra Jom Klao Ph.D. Research Scholarship year 2018, King Mongkut's University of Technology Thonburi, Thailand, under financial supported number 32/2561. In addition, this research project is supported by King Mongkut's University of Technology Thonburi under "KMUTT Research Center of Excellent Project (Grant number 7601.24/4054)".

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