Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus

Tsukihara, Takahisa; Honda, Yoshio; Sakai, Ryota; Watanabe, Takahito; Watanabe, Takashi

doi:10.1016/j.jbiotec.2006.05.013

Cited by 60 publications

(22 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…20,21 Later, Pleurotus ostreatus was used to express the versatile peroxidase MnP2 homologously, with a yield of up to 21 mg L ¡1 . 22 However, the extensive screening required to identify mutant production strains, as well as contamination with the native enzyme, led to disappointing results. The model bacterium Escherichia coli has been extensively developed as an expression platform for fungal enzymes, and many recombinant enzymes have been isolated successfully from inclusion bodies and refolded with 1-28% efficiency [23][24][25][26][27][28][29][30] and maximum yields of 1.5-14 mg L ¡1 after in vitro activation and purification.…”

Section: Recombinant Lignin-degrading Peroxidasesmentioning

confidence: 99%

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

et al. 2016

View full text Add to dashboard Cite

Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.

show abstract

Section: Recombinant Lignin-degrading Peroxidasesmentioning

confidence: 99%

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

et al. 2016

View full text Add to dashboard Cite

show abstract

“…However, higher yield of ganoderic acids in G. lucidum mycelia is needed for commercial applications (33). Genetic engineering has been successfully used to enhance the yields of bioactive compounds (55) and some enzymes such as laccase (1,13) and versatile peroxidase MnP2 (41) in basidiomycete Agaricomycetes. However, no study reported the enhancement of terpenes accumulation through genetic manipulation of basidiomycetes.…”

mentioning

confidence: 99%

Enhancement of Ganoderic Acid Accumulation by Overexpression of an N-Terminally Truncated 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Gene in the Basidiomycete Ganoderma lucidum

Zhong

2012

Appl Environ Microbiol

View full text Add to dashboard Cite

Ganoderic acids produced by Ganoderma lucidum, a well-known traditional Chinese medicinal mushroom, exhibit antitumor and antimetastasis activities. Genetic modification of G. lucidum is difficult but critical for the enhancement of cellular accumulation of ganoderic acids. In this study, a homologous genetic transformation system for G. lucidum was developed for the first time using mutated sdhB, encoding the iron-sulfur protein subunit of succinate dehydrogenase, as a selection marker. The truncated G. lucidum gene encoding the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) was overexpressed by using the Agrobacterium tumefaciens-mediated transformation system. The results showed that the mutated sdhB successfully conferred carboxin resistance upon transformation. Most of the integrated transfer DNA (T-DNA) appeared as a single copy in the genome. Moreover, deregulated constitutive overexpression of the HMGR gene led to a 2-fold increase in ganoderic acid content. It also increased the accumulation of intermediates (squalene and lanosterol) and the upregulation of downstream genes such as those of farnesyl pyrophosphate synthase, squalene synthase, and lanosterol synthase. This study demonstrates that transgenic basidiomycete G. lucidum is a promising system to achieve metabolic engineering of the ganoderic acid pathway.

show abstract

“…The catalytic versatility with non-requirement of redox mediators projects versatile peroxidase as a potential industrial biocatalyst 40 . Until recently, this enzyme was characterized only from Pleurotus and Bjerkandera and reported in Panus, Trametes, Lepista, Dichomitous and Spongipellis 41 .…”

Section: Resultsmentioning

confidence: 99%

Insights into the Mechanism of Lignocellulose Degradation by Versatile Peroxidases

Ravichandran¹,

Sridhar²

2017

Current Science

View full text Add to dashboard Cite

Lignocelluloses are imperative structural components of plant cell wall and are profusely found in agricultural crop residues. The structural heterogeneity and recalcitrance of lignin limit the accessibility of cell wall carbohydrates for constructive exploitation. During the past decades, diverse lignin degrading enzymes were characterized to facilitate the utilization of lignocellulosic biomass for technological applications. Versatile peroxidases are unique among ligninolytic enzymes for their remarkably high redox potential and ability to oxidize lignin without the requisite of redox mediators. The hybrid structural architecture of this enzyme bearing functional features of lignin peroxidase and manganese peroxidase demonstrates its versatility in aromatics oxidation. This review summarizes the distinctive structural aspects of fungal versatile peroxidase in correlation to its oxidation of aromatic substrates besides emphasizing on the catalytic environment conducive for substrate oxidation. This review also focuses on the general strategies employed for production of this enzyme, its molecular framework, potential biotechnological applications of versatile peroxidase and prospects on enhancing the production of enzyme. Finally, the significance of this enzyme in improving the nutritive value of crop residues to promote ruminal productivity is highlighted.

show abstract

Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus

Cited by 60 publications

References 40 publications

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

Enhancement of Ganoderic Acid Accumulation by Overexpression of an N-Terminally Truncated 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Gene in the Basidiomycete Ganoderma lucidum

Insights into the Mechanism of Lignocellulose Degradation by Versatile Peroxidases

Contact Info

Product

Resources

About