Increasing manganese peroxidase productivity of Phanerochaete chrysosporium by optimizing carbon sources and supplementing small molecules

Authors


Shulin Chen, Department of Biological Systems Engineering, The Bioprocessing and Bioproduct Engineering Laboratory (BBEL), Washington State University, L.J. Smith 213, Pullman, WA 99163, USA. E-mail: chens@wsu.edu.

Abstract

Aims:  To overproduce manganese peroxidase (MnP) using Phanerochaete chrysosporium. Effects of carbon sources, agricultural by-products and small molecules were tested to enhance the MnP productivity.

Methods and Results:  Various carbon sources and agricultural by-products were compared as the basal medium. A MnP activity of 4·7 ± 0·31 U ml−1 was obtained using mannose as a carbon source. The enzyme productivity further reached 7·36 ± 0·05 and 8·77 ± 0·23 U ml−1 when the mannose medium was supplemented with cyclic adenosine monophosphate (cAMP) and S-adenosylmethionine, respectively.

Conclusions:  This study revealed the highest MnP productivity obtained by optimizing the carbon sources and supplementing small molecules. It can provide insight for: (i) making high quantities of enzymes by optimizing media resources and (ii) engineering the global regulatory genes in P. chrysosporium for the onsite production of MnP.

Significance and Impact of the Study:  As MnP is an important enzyme to hydrolyse lignin polymers which protects the plant cell wall from exposing of cellulose fibres, the production of the enzyme is a current demand for biofuel biotechnology. The knowledge generated from this study can help to advance the technology for stable production of MnP.

Ancillary