Light Regulation of Two New Manganese Peroxidase-Encoding Genes in Trametes polyzona KU-RNW027

Abstract

To better understand the light regulation of ligninolytic systems in Trametes polyzona KU-RNW027, ligninolytic enzymes-encoding genes were identified and analyzed to determine their transcriptional regulatory elements. Elements of light regulation were investigated in submerged culture. Three ligninolytic enzyme-encoding genes, mnp1, mnp2, and lac1, were found. Cloning of the genes encoding MnP1 and MnP2 revealed distinct deduced amino acid sequences with 90% and 86% similarity to MnPs in Lenzites gibbosa, respectively. These were classified as new members of short-type hybrid MnPs in subfamily A.2 class II fungal secretion heme peroxidase. A light responsive element (LRE), composed of a 5′-CCRCCC-3′ motif in both mnp promoters, is reported. Light enhanced MnP activity 1.5 times but not laccase activity. The mnp gene expressions under light condition increased 6.5- and 3.8-fold, respectively. Regulation of laccase gene expression by light was inconsistent with the absence of LREs in their promoter. Blue light did not affect gene expressions but impacted their stability. Reductions of MnP and laccase production under blue light were observed. The details of the molecular mechanisms underlying enzyme production in this white-rot fungus provide useful knowledge for wood degradation relative to illumination condition. These novel observations demonstrate the potential of enhancing ligninolytic enzyme production by this fungus for applications with an eco-friendly approach to bioremediation.

Effect of Fungal Solid-State Fermentation on the Profile of Phenolic Compounds and on the Nutritional Properties of Grape Pomace

“…The activity of xylanase (endo-1,4-β-xylanase) and cellulose (endoglucanases and exoglucanases) was determined by the DNS method [20,21], β-glucosidase activity was determined according to the study of [22], and invertase activity was determined by the method of [23]. The activities of MnP and laccase were determined by monitoring the oxidation of the substrate 2,6dimethoxyphenol (DMP) at 469 nm for 120 s according to the method of [24].…”

Bioconversion of Grape Pomace with Rhizopus oryzae under Solid-State Conditions: Changes in the Chemical Composition and Profile of Phenolic Compounds

“…The activities of the lignolytic enzymes MnP and laccase were determined by monitoring oxidation of the substrate 2,6-dimethoxyphenol (DMP) at 469 nm for 120 s according to the method of Lueangjaroenkit et al [41]. The assay for LiP was performed according to the method described by Field et al [42] and Linko and Haapala [43] by monitoring the oxidation of the substrate veratryl alcohol at 310 nm.…”