Year-end Sale % OFF 
Abstract
Alizarin is an anti-fungal compound produced by the plant, Rubia tinctorum. The parasitic fungus Bjerkandera adusta Dec 1 was cultured in potato dextrose (PD) medium with or without alizarin. Alizarin was a good substrate for the dye-decolorizing peroxidase (DyP) from B. adusta Dec 1 and hampered B. adusta growth at the early stage of plate culture. During liquid shaking culture, DyP activity in cultures supplemented with 100 μM alizarin was greater than that in controls cultured without alizarin. In particular, DyP activity per dry cell mass increased approximately 3.5-, 3.1-, and 2.9-fold at 24, 30, and 36 h after inoculation, respectively, compared with control cultures. These data suggest that alizarin stimulates the expression of DyP. Interestingly, alizarin rapidly decomposed at an early stage in culture (24–42 h) in PD medium supplemented with 100 μM alizarin. Thus, alizarin appears to induce DyP expression in B. adusta Dec 1, and this DyP, in turn, rapidly degrades alizarin. Collectively, our findings suggest that the physiological role of DyP is to degrade antifungal compounds produced by plants.
Highlights
Bjerkandera adusta, a basidiomycete belonging to the family Polyporaceae, is a white rot fungus that parasitizes certain trees, resulting in lignin degradation
We focused on the ability of dye-decolorizing peroxidase (DyP) to degrade the anti-fungal anthraquinone compound, alizarin (Manojlovic et al 2005), and further considered the possibility that DyP degrades natural anthraquinone compounds, such as some phytoalexins (Wijnsma et al 1985)
DyP degradation activity toward both alizarin and Remazol brilliant blue R (RB19) was similar as shown in Fig. 1, indicating that alizarin is a good substrate for DyP
Summary
Bjerkandera adusta, a basidiomycete belonging to the family Polyporaceae, is a white rot fungus that parasitizes certain trees, resulting in lignin degradation. Manganese peroxidase (MnP) and dye decolorizing peroxidase (DyP) have been detected during culture of B. adusta Dec 1, but lignin peroxidase (LiP) and laccase have not. Another noteworthy characteristic is that Dec 1 degrades xenobiotics such as synthetic anthraquinone dyes and secretes a versatile peroxidase (VP) in addition to DyP during culture (Kim et al 1995; Sugano et al 2000, 2006, 2009; Gomi et al 2011). DyP of B. adusta is a member of a large family of DyPtype peroxidases that is subdivided in three classes, P, I and V, according to their tertiary structural homology (Yoshida and Sugano 2015). Members of class I are intermediate in size, and some show moderate decolorizing activity toward
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
