Molecular Cloning and Expression of Polyphenoloxidase Genes from the Mushroom, Agaricus bisporus

Li, Nanyi; Cai, Weiming; Qi, Jin; Qin, Qiaoping; Ran, Fulai

doi:10.1016/s1671-2927(09)60305-9

Cited by 17 publications

(9 citation statements)

References 25 publications

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“…Often isoforms of polyphenol oxidase were found during isolation and purification. Currently six amino acid sequences (PPO1 to 6) are known for a polyphenol oxidase originating from Agaricus bisporus ( Li et al, 2011 ; Mauracher et al, 2014; Weijn et al, 2013; Wichers et al, 2003; Wu et al, 2010 ). Eicken et al (1998) isolated two catechol oxidases with different amino acid sequences from sweet potato ( Ipomoea batatas) having molecular masses of 39 and 40 kDa, respectively.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of tyrosinase from walnut leaves (Juglans regia)

et al. 2014

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of tyrosinase from walnut leaves (Juglans regia)

et al. 2014

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“…The protein BLAST was performed separately using ten Mt PPO7 sequences [PDB id: 4j3p and closely related Mt PPO7s: Q2UNF9, Aspergillus oryzae (strain ATCC 42149); G2QC95, Myceliophthora thermophila (ATCC 42464); Q2H7I7, Chaetomium globosum (ATCC 6205); G0SFX8, Chaetomium thermophilum (DSM 1495); L7IAQ4, Magnaporthe oryzae (strain Y34); L7JMT9, Magnaporthe oryzae (strain P131); G4N2I5, Magnaporthe oryzae (strain 70-15); A0A084GCK1, Scedosporium apiospermum ; A0A0C4DYF2, Magnaporthiopsis poae (ATCC 64411); J3P591, Gaeumannomyces graminis var. tritici (strain R3-111a-1)], ten AA9 LPMO sequences (PDB id: 4d7u and closely related LPMOs: Q7SHI8, Neurospora crassa (strain ATCC 24698); G2QCJ3, Myceliophthora thermophila (strain ATCC 42464); F7W1P4, Sordaria macrospora (strain ATCC MYA-333); G2RB73, Thielavia terrestris (strain ATCC 38088); Q2H8N9, Chaetomium globosum (strain ATCC 6205); G0S408, Chaetomium thermophilum (strain DSM 1495); F8MLY8, N eurospora tetrasperma (strain FGSC 2508); T0L448, Colletotrichum gloeosporioides (strain Cg-14); A0A0H4K9X4 and A0A1C9CXI0, Myceliophthora thermophila C1); and four Ab PPOs ( Ab PPO1, Ab PPO2, Ab PPO3, and Ab PPO4 [55, 56]) as query sequences. Resulting sequences below E-value cut-off of 0.001 with query coverage above 60% for AA9 LPMOs, 65% for Mt PPO7s, and 85% for Ab PPOs were considered for further analysis.…”

Section: Methodsmentioning

confidence: 99%

Boosting LPMO-driven lignocellulose degradation by polyphenol oxidase-activated lignin building blocks

Frommhagen

Mutte

Westphal

et al. 2017

Biotechnol Biofuels

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BackgroundMany fungi boost the deconstruction of lignocellulosic plant biomass via oxidation using lytic polysaccharide monooxygenases (LPMOs). The application of LPMOs is expected to contribute to ecologically friendly conversion of biomass into fuels and chemicals. Moreover, applications of LPMO-modified cellulose-based products may be envisaged within the food or material industry.ResultsHere, we show an up to 75-fold improvement in LPMO-driven cellulose degradation using polyphenol oxidase-activated lignin building blocks. This concerted enzymatic process involves the initial conversion of monophenols into diphenols by the polyphenol oxidase MtPPO7 from Myceliophthora thermophila C1 and the subsequent oxidation of cellulose by MtLPMO9B. Interestingly, MtPPO7 shows preference towards lignin-derived methoxylated monophenols. Sequence analysis of genomes of 336 Ascomycota and 208 Basidiomycota reveals a high correlation between MtPPO7 and AA9 LPMO genes.ConclusionsThe activity towards methoxylated phenolic compounds distinguishes MtPPO7 from well-known PPOs, such as tyrosinases, and ensures that MtPPO7 is an excellent redox partner of LPMOs. The correlation between MtPPO7 and AA9 LPMO genes is indicative for the importance of the coupled action of different monooxygenases in the concerted degradation of lignocellulosic biomass. These results will contribute to a better understanding in both lignin deconstruction and enzymatic lignocellulose oxidation and potentially improve the exploration of eco-friendly routes for biomass utilization in a circular economy.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-017-0810-4) contains supplementary material, which is available to authorized users.

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“…Today, six tyrosinase isoforms (PPO1-6) originating from six genes located on two different (from a total of 12) chromosomes (PPO1 and 6 on chromosome 8; PPO2-5 on chromosome 12) of the common edible mushroom (A. bisporus) are known (Wichers et al, 2003;Wu et al, 2010;Weijn et al, 2013). Apart from differing abundances with respect to the tissue compartment and the fruiting-body growth stage (Hammond & Nichols, 1976), no unique function of a particular isoform has been published (Li et al, 2011;Weijn et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Latent and activeabPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal

Mauracher

Molitor

Al‐Oweini

et al. 2014

Acta Crystallogr D Biol Crystallogr

112

107

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Tyrosinases, bifunctional metalloenzymes, catalyze the oxidation of monophenols and o-diphenols to o-quinones, the precursor compounds of the brown-coloured pigment melanin. In eukaryotic organisms, tyrosinases are expressed as latent zymogens that have to be proteolytically cleaved in order to form highly active enzymes. This activation mechanism, known as the tyrosinase maturation process, has scientific and industrial significance with respect to biochemical and technical applications of the enzyme. Here, not only the first crystal structure of the mushroom tyrosinase abPPO4 is presented in its active form (Ser2-Ser383) and in its 21 kDa heavier latent form (Ser2-Thr545), but furthermore the simultaneous presence of both forms within one single-crystal structure is shown. This allows for a simple approach to investigate the transition between these two forms. Isoform abPPO4 was isolated and extensively purified from the natural source (Agaricus bisporus), which contains a total of six polyphenol oxidases (PPOs). The enzyme formed crystals (diffracting to a resolution of 2.76 Å ) owing to the employment of the 6-tungstotellurate (VI)

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Molecular Cloning and Expression of Polyphenoloxidase Genes from the Mushroom, Agaricus bisporus

Cited by 17 publications

References 25 publications

Purification and characterization of tyrosinase from walnut leaves (Juglans regia)

Purification and characterization of tyrosinase from walnut leaves (Juglans regia)

Boosting LPMO-driven lignocellulose degradation by polyphenol oxidase-activated lignin building blocks

Latent and activeabPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal

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