Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition

Ertan, Haluk; Siddiqui, Khawar Sohail; Muenchhoff, Julia; Charlton, Tim; Cavicchioli, Ricardo

doi:10.1016/j.biochi.2012.02.012

Cited by 44 publications

(31 citation statements)

References 41 publications

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“…reaction occurred at a very low pH, when Mn 2ϩ oxidation was undetectable. Similar results were demonstrated with VP from Bjerkandera adjusta (28). OII was found to inhibit the oxidation of Mn 2ϩ and RB5, while RB5 acts as an activator in the oxidation of OII and Mn 2ϩ .…”

Section: Discussionsupporting

confidence: 84%

Limits of Versatility of Versatile Peroxidase

Knop

Levinson

Makovitzki

et al. 2016

Appl Environ Microbiol

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Although Mn2؉ is the most abundant substrate of versatile peroxidases (VPs), repression of Pleurotus ostreatus vp1 expression occurred in Mn 2؉ -sufficient medium. This seems to be a biological contradiction. The aim of this study was to explore the mechanism of direct oxidation by VP1 under Mn 2؉ -deficient conditions, as it was found to be the predominant enzyme during fungal growth in the presence of synthetic and natural substrates. The native VP1 was purified and characterized using three substrates, Mn 2؉ , Orange II (OII), and Reactive Black 5 (RB5), each oxidized by a different active site in the enzyme. While the pH optimum for Mn 2؉ oxidation is 5, the optimum pH for direct oxidation of both dyes was found to be 3. Indeed, effective in vivo decolorization occurred in media without addition of Mn 2؉ only under acidic conditions. We have determined that Mn 2؉ inhibits in vitro the direct oxidation of both OII and RB5 while RB5 stabilizes both Mn 2؉ and OII oxidation. Furthermore, OII was found to inhibit the oxidation of both Mn 2؉ and RB5. In addition, we could demonstrate that VP1 can cleave OII in two different modes. Under Mn 2؉ -mediated oxidation conditions, VP1 was able to cleave the azo bond only in asymmetric mode, while under the optimum conditions for direct oxidation (absence of Mn 2؉ at pH 3) both symmetric and asymmetric cleavages occurred. We concluded that the oxidation mechanism of aromatic compounds by VP1 is controlled by Mn 2؉ and pH levels both in the growth medium and in the reaction mixture. IMPORTANCEVP1 is a member of the ligninolytic heme peroxidase gene family of the white rot fungus Pleurotus ostreatus and plays a fundamental role in biodegradation. This enzyme exhibits a versatile nature, as it can oxidize different substrates under altered environmental conditions. VPs are highly interesting enzymes due to the fact that they contain unique active sites that are responsible for direct oxidation of various aromatic compounds, including lignin, in addition to the well-known Mn 2؉ binding active site. This study demonstrates the limits of versatility of P. ostreatus VP1, which harbors multiple active sites, exhibiting a broad range of enzymatic activities, but they perform differently under distinct conditions. The versatility of P. ostreatus and its enzymes is an advantageous factor in the fungal ability to adapt to changing environments. This trait expands the possibilities for the potential utilization of P. ostreatus and other white rot fungi.

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Section: Discussionsupporting

confidence: 84%

Limits of Versatility of Versatile Peroxidase

Knop

Levinson

Makovitzki

et al. 2016

Appl Environ Microbiol

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“…The bacterial and fungal sources of LiP are listed in Table 3. LiPs have a high redox potential (1.2 V at pH 3.0) [56] as compared with other peroxidases and can oxidize phenolic and nonphenolic structures of lignin directly without a mediator. The bacterial and fungal sources of LiP are listed in Table 3.…”

Section: Humificationmentioning

confidence: 99%

Enzymatic Degradation of Lignin in Soil: A Review

et al. 2017

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Lignin is a major component of soil organic matter and also a rich source of carbon dioxide in soils. However, because of its complex structure and recalcitrant nature, lignin degradation is a major challenge. Efforts have been made from time to time to understand the lignin polymeric structure better and develop simpler, economical, and bio-friendly methods of degradation. Certain enzymes from specialized bacteria and fungi have been identified by researchers that can metabolize lignin and enable utilization of lignin-derived carbon sources. In this review, we attempt to provide an overview of the complexity of lignin's polymeric structure, its distribution in forest soils, and its chemical nature. Herein, we focus on lignin biodegradation by various microorganism, fungi and bacteria present in plant biomass and soils that are capable of producing ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), versatile peroxidase (VP), and dye-decolorizing peroxidase (DyP). The relevant and recent reports have been included in this review.

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“…This may have resulted in partial depolymerization of up to 60% of the lignin and the release of different aromatic compounds of lower molecular weight and further degradation by MnP and LAC [Guerriero et al, 2016;Martins et al, 2011]. Because the constitutive overexpression of the ligninolytic enzymes was successful in the same fungal strain, it is possible that the production or hybrid activities of various ligninolytic enzymes, as well as the genetic background of the host, had complementary effects in the lignocellulose depolymerization [Ertan et al, 2012;Fonseca-Maldonado et al, 2014;Lima et al, 2015;Verma et al, 2002;Yang et al, 2013]. These observations and our results reinforce the hypothesis that the cooperation of different ligninolytic enzymes can improve the degradation of lignocellulosic biomass.…”

Section: Discussionmentioning

confidence: 99%

“…Although VP activity is a hybrid between MnP and LiP activities, recent findings have demonstrated that there is a synergy of VP activity on ligninolytic substrates when both LiP and MnP are active simultaneously [Siddiqui et al, 2014]. Possibly, the degradation of SB and WB lignin was initiated by LiP, VP, and accessory enzymes, since they have a high redox potential that allows cleaving of C-C and C-O-C linkages present in lignin [Ertan et al, 2012;Guerriero et al, 2016]. This may have resulted in partial depolymerization of up to 60% of the lignin and the release of different aromatic compounds of lower molecular weight and further degradation by MnP and LAC [Guerriero et al, 2016;Martins et al, 2011].…”

Section: Discussionmentioning

confidence: 99%

Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus <b><i>Phanerochaete chrysosporium</i></b> Overexpressing Laccases and Peroxidases

et al. 2018

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Ligninolytic enzyme production and lignin degradation are typically the rate-limiting steps in the biofuel industry. To improve the efficiency of simultaneous bio-delignification and enzyme production, Phanerochaete chrysosporium was transformed by shock wave-induced acoustic cavitation to co-overexpress 3 peroxidases and 1 laccase and test it on the degradation of sugarcane bagasse and wheat bran. Lignin depolymerization was enhanced by up to 25% in the presence of recombinant fungi in comparison with the wild-type strain. Sugar release on lignocellulose was 2- to 6-fold higher by recombinant fungi as compared with the control. Wheat bran ostensibly stimulated the production of ligninolytic enzymes. The highest peroxidase activity from the recombinant strains was 2.6-fold higher, whereas the increase in laccase activity was 4-fold higher in comparison to the control. The improvement of lignin degradation was directly proportional to the highest peroxidase and laccase activity. Because various phenolic compounds released during lignocellulose degradation have proven to be toxic to cells and to inhibit enzyme activity, a significant reduction (over 40%) of the total phenolic content in the samples treated with recombinant strains was observed. To our knowledge, this is the first report that engineering P. chrysosporium enhances biodegradation of lignocellulosic biomass.

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Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition

Cited by 44 publications

References 41 publications

Limits of Versatility of Versatile Peroxidase

Limits of Versatility of Versatile Peroxidase

Enzymatic Degradation of Lignin in Soil: A Review

Enhanced Delignification of Lignocellulosic Biomass by Recombinant Fungus <b><i>Phanerochaete chrysosporium</i></b> Overexpressing Laccases and Peroxidases

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