Cloning and expression of fungal Trametes Laccase gene in yeast host andcharacterization of recombinant enzyme biochemical properties and kineticparameters

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HESAMPOUR A.; Mohandesi n.

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Journal: JOURNAL OF FOOD MICROBIOLOGY Year:2018 | Volume:4 | Issue:4 Page(s): 41-54

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Title

Cloning and expression of fungal Trametes Laccase gene in yeast host andcharacterization of recombinant enzyme biochemical properties and kineticparameters

Author(s)

HESAMPOUR A. | Mohandesi n. | Issue Writer Certificate

Keywords

LaccaseQ1

Pichia PastorisQ1

TrametesQ1

yeastQ2

Abstract

Laccase have received much attention from researchers in last decades due to their ability tooxidase both phenolic and non-phenolic lignin related compounds as well as highly recalcitrantenvironmental pollutants, which makes them very useful for their application to severalbiotechnological processes. Despite of Trametes Laccase wildly application as detoxification ofindustrial effluents, its native low expression, makes it unsuitable for industrial application. In thisstudy, heterologous expression of Trametes Laccase gene in methylotrophic yeast, P. pastoris withα MF as signal peptide and Ppinkα HC expression vector under methanol induction in BMGY andBMMY media was investigated and expressed active recombinant Laccase biochemical andbiophysical properties in compare with native Trametes Laccase was studied. According to codonperformance of P. pastoris, Trametes Laccase gene sequence designed and synthetic genes undercontrol of inducible AOX1 promoter was successfully high expressed as active form in yeast host, SDS-PAGE analysis showed the recombinant Laccase in size of 65KDa with Km=140μ M. Analysisof Laccase biochemical and biophysical properties demonstrated that recombinant Laccase haswide pH profile with pH optima 4. 8 and optimum temperature of 60 ° C with high activity inP. pastoris host. We conclude that recombinant P. pastoris Laccase could fulfil a serried ofpredefined industrial quality criteria to be used in industry like, broad pH optimum, substratespecify and proper thermal stability. Therefore, studied methylotrophic yeast could be anappropriate host for expression and production of recombinant Laccase, with industrial application.

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APA: Copy

HESAMPOUR, A., & Mohandesi, n.. (2018). Cloning and expression of fungal Trametes Laccase gene in yeast host andcharacterization of recombinant enzyme biochemical properties and kineticparameters. JOURNAL OF FOOD MICROBIOLOGY, 4(4 ), 41-54. SID. https://sid.ir/paper/250748/en

Vancouver: Copy

HESAMPOUR A., Mohandesi n.. Cloning and expression of fungal Trametes Laccase gene in yeast host andcharacterization of recombinant enzyme biochemical properties and kineticparameters. JOURNAL OF FOOD MICROBIOLOGY[Internet]. 2018;4(4 ):41-54. Available from: https://sid.ir/paper/250748/en

IEEE: Copy

A. HESAMPOUR, and n. Mohandesi, “Cloning and expression of fungal Trametes Laccase gene in yeast host andcharacterization of recombinant enzyme biochemical properties and kineticparameters,” JOURNAL OF FOOD MICROBIOLOGY, vol. 4, no. 4 , pp. 41–54, 2018, [Online]. Available: https://sid.ir/paper/250748/en

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