Difference between revisions of "Part:BBa K3196004"
 
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Versatile peroxidase, which was firstly found in Pleurotus eryngii in the 1990s<sup>[1]</sup>, is a kind of non-animal peroxide for lignin degradation. Most fungi secreting versatile peroxidase belong to Pleurotus and Bjerkandera.
 
Versatile peroxidase, which was firstly found in Pleurotus eryngii in the 1990s<sup>[1]</sup>, is a kind of non-animal peroxide for lignin degradation. Most fungi secreting versatile peroxidase belong to Pleurotus and Bjerkandera.
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<h1>''Usage and Biology''</h1>
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With the same structure and catalytic properties as manganese peroxidase and lignin peroxidase, the enzyme brings with promised prospect, attracting a number of researchers’ attention. Manganese peroxidase can oxidase Mn2+ into Mn3+, which can oxidize various monophenols and diphenols, including phenolic lignin model compound. Lignin peroxidase operates a typical peroxidase catalytic cycle, which can directly interact with lignin.<sup>[2]</sup>
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Nowadays, numerous researches such as biological bleaching, bioremediation, biofuels are developed to fully reveal its practical potential, however, mostly using physisporinu as their research object but not on the level of genes. According to Mohorcic M<sup>[1]</sup>, it is feasible to introduce VP’s coding sequence into pichia pastoris as an approach to increase the output of VP and shorten the experimental cycle. Inspired by the paper, we introduce VP into our pichia pastoris system to degrade lignin more effectively and completely together with small laccase. Besides pichia pastoris could modify VP after translation, ensuring the high expression of active VP.
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[[File:T--HUST--China--2019-PHO1-αpropelA.jpg ‎|400px|thumb|center|Figure1. T--HUST--China--2019-PHO1-αpropelA]]
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<h1>''Reference''</h1>
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[1] M. J. Martinez B B S C. MnP isoenzymes produced by two pleurotus species in liquid sulture and during wheat-straw solid-state fermentation [J]. Acs Symposium. 1996, 655; 183-196.
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[2] Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites Susana Camarero, Sovan Sarkar, Francisco Javier Ruiz-Duen˜ as, Marı´a Jesu´ s Martı´nez, and A´ ngel T. Martı´nez§  THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 15, Issue of April 9, pp. 10324–10330, 1999<!-- -->
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K3196004 parameters</partinfo>
 
<partinfo>BBa_K3196004 parameters</partinfo>
 
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<h1>'''Usage and Biology'''</h1>
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With the same structure and catalytic properties as manganese peroxidase and lignin peroxidase, the enzyme brings with promised prospect, attracting a number of researchers’ attention. Manganese peroxidase can oxidase Mn2+ into Mn3+, which can oxidize various monophenols and diphenols, including phenolic lignin model compound. Lignin peroxidase operates a typical peroxidase catalytic cycle, which can directly interact with lignin.<sup>[2]</sup>
 +
 +
Nowadays, numerous researches such as biological bleaching, bioremediation, biofuels are developed to fully reveal its practical potential, however, mostly using physisporinu as their research object but not on the level of genes. According to Mohorcic M<sup>[1]</sup>, it is feasible to introduce VP’s coding sequence into pichia pastoris as an approach to increase the output of VP and shorten the experimental cycle. Inspired by the paper, we introduce VP into our pichia pastoris system to degrade lignin more effectively and completely together with small laccase. Besides pichia pastoris could modify VP after translation, ensuring the high expression of active VP.
 +
 +
 +
<h1>'''Reference'''</h1>
 +
[1] M. J. Martinez B B S C. MnP isoenzymes produced by two pleurotus species in liquid sulture and during wheat-straw solid-state fermentation [J]. Acs Symposium. 1996, 655; 183-196.
 +
[2] Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites Susana Camarero, Sovan Sarkar, Francisco Javier Ruiz-Duen˜ as, Marı´a Jesu´ s Martı´nez, and A´ ngel T. Martı´nez§  THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 15, Issue of April 9, pp. 10324–10330, 1999

Latest revision as of 05:29, 20 October 2019


VP

Versatile peroxidase, which was firstly found in Pleurotus eryngii in the 1990s[1], is a kind of non-animal peroxide for lignin degradation. Most fungi secreting versatile peroxidase belong to Pleurotus and Bjerkandera.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

With the same structure and catalytic properties as manganese peroxidase and lignin peroxidase, the enzyme brings with promised prospect, attracting a number of researchers’ attention. Manganese peroxidase can oxidase Mn2+ into Mn3+, which can oxidize various monophenols and diphenols, including phenolic lignin model compound. Lignin peroxidase operates a typical peroxidase catalytic cycle, which can directly interact with lignin.[2]

Nowadays, numerous researches such as biological bleaching, bioremediation, biofuels are developed to fully reveal its practical potential, however, mostly using physisporinu as their research object but not on the level of genes. According to Mohorcic M[1], it is feasible to introduce VP’s coding sequence into pichia pastoris as an approach to increase the output of VP and shorten the experimental cycle. Inspired by the paper, we introduce VP into our pichia pastoris system to degrade lignin more effectively and completely together with small laccase. Besides pichia pastoris could modify VP after translation, ensuring the high expression of active VP.


Reference

[1] M. J. Martinez B B S C. MnP isoenzymes produced by two pleurotus species in liquid sulture and during wheat-straw solid-state fermentation [J]. Acs Symposium. 1996, 655; 183-196. [2] Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites Susana Camarero, Sovan Sarkar, Francisco Javier Ruiz-Duen˜ as, Marı´a Jesu´ s Martı´nez, and A´ ngel T. Martı´nez§ THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 15, Issue of April 9, pp. 10324–10330, 1999