Characterization and immobilization of Pycnoporus cinnabarinus carboxylic acid reductase, PcCAR2

Masethabela Maphatsoe, Chiam Hashem, Jonathan Guyang Ling, Melissa Horvat, Karl Rumbold, Farah Diba Abu Bakar, Margit Winkler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Carboxylic acid reductases (CARs) are well-known for their eminent selective one-step synthesis of carboxylic acids to aldehydes. To date, however, few CARs have been identified and characterized, especially from fungal sources. In this study, the CAR from the white rot fungus Pycnoporus cinnabarinus (PcCAR2) was expressed in Escherichia coli. PcCAR2′s biochemical properties were explored in vitro after purification, revealing a melting temperature of 53 °C, while the reaction temperature optimum was at 35 °C. In the tested buffers, the enzyme showed a pH optimum of 6.0 and notably, a similar activity up to pH 7.5. PcCAR2 was immobilized to explore its potential as a recyclable biocatalyst. PcCAR2 showed no critical loss of activity after six cycles, with an average conversion to benzaldehyde of more than 85% per cycle. Immobilization yield and efficiency were 82% and 76%, respectively, on Ni-sepharose. Overall, our findings contribute to the characterization of a thermotolerant fungal CAR, and established a more sustainable use of the valuable biocatalyst.

Original languageEnglish
Pages (from-to)47-54
Number of pages8
JournalJournal of Biotechnology
Publication statusPublished - 10 Feb 2022


  • Biocatalysis
  • Carboxylic acid reductase
  • Fungi
  • Immobilization
  • Pycnoporus cinnabarinus
  • Sequence similarity network

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Bioengineering
  • Biotechnology

Fields of Expertise

  • Human- & Biotechnology


Dive into the research topics of 'Characterization and immobilization of Pycnoporus cinnabarinus carboxylic acid reductase, PcCAR2'. Together they form a unique fingerprint.

Cite this