The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor View Full Text


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Article Info

DATE

2013-12

AUTHORS

Eridan Orlando Pereira, Adrian Tsang, Tim A McAllister, Rima Menassa

ABSTRACT

BACKGROUND: Microorganisms are the most proficient decomposers in nature, using secreted enzymes in the hydrolysis of lignocellulose. As such, they present the most abundant source for discovery of new enzymes. Acremonium alcalophilum is the only known cellulolytic fungus that thrives in alkaline conditions and can be cultured readily in the laboratory. Its optimal conditions for growth are 30°C and pH 9.0-9.2. The genome sequence of Acremonium alcalophilum has revealed a large number of genes encoding biomass-degrading enzymes. Among these enzymes, lipases are interesting because of several industrial applications including biofuels, detergent, food processing and textile industries. RESULTS: We identified a lipA gene in the genome sequence of Acremonium alcalophilum, encoding a protein with a predicted lipase domain with weak sequence identity to characterized enzymes. Unusually, the predicted lipase displays ≈ 30% amino acid sequence identity to both feruloyl esterase and lipase of Aspergillus niger. LipA, when transiently produced in Nicotiana benthamiana, accumulated to over 9% of total soluble protein. Plant-produced recombinant LipA is active towards p-nitrophenol esters of various carbon chain lengths with peak activity on medium-chain fatty acid (C8). The enzyme is also highly active on xylose tetra-acetate and oat spelt xylan. These results suggests that LipA is a novel lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. We determined that LipA is a glycoprotein with pH and temperature optima at 8.0 and 40°C, respectively. CONCLUSION: Besides being the first heterologous expression and characterization of a gene coding for a lipase from A. alcalophilum, this report shows that LipA is very versatile exhibiting both acetylxylan esterase and lipase activities potentially useful for diverse industry sectors, and that tobacco is a suitable bioreactor for producing fungal proteins. More... »

PAGES

111

References to SciGraph publications

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  • 2011-12. The role of acetyl xylan esterase in the solubilization of xylan and enzymatic hydrolysis of wheat straw and giant reed in BIOTECHNOLOGY FOR BIOFUELS
  • 2011-09-21. Transient Expression Using Agroinfiltration and Its Applications in Molecular Farming in MOLECULAR FARMING IN PLANTS: RECENT ADVANCES AND FUTURE PROSPECTS
  • 2001-07. Enhancers and core promoter elements are essential for the activity of a cryptic gene activation sequence from tobacco, tCUP in MOLECULAR GENETICS AND GENOMICS
  • 2011-10. Expression and Characterization of a Novel Lipase from Aspergillus fumigatus with High Specific Activity in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • 1989-01. The role of ester groups in resistance of plant cell wall polysaccharides to enzymatic hydrolysis in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • 2012-01. Overview of Fungal Lipase: A Review in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • 2013-10. A Cold-Adapted and Organic Solvent-Tolerant Lipase from a Psychrotrophic Bacterium Pseudomonas sp. Strain YY31: Identification, Cloning, and Characterization in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • 2002. Industrial Proteins Produced from Transgenic Plants in PLANTS AS FACTORIES FOR PROTEIN PRODUCTION
  • 2011-12. In planta expression of A. cellulolyticus Cel5A endocellulase reduces cell wall recalcitrance in tobacco and maize in BIOTECHNOLOGY FOR BIOFUELS
  • 2008-12. Welcome to Biotechnology for Biofuels in BIOTECHNOLOGY FOR BIOFUELS
  • 2006-12. Analysis of and function predictions for previously conserved hypothetical or putative proteins in Blochmannia floridanus in BMC MICROBIOLOGY
  • 2006-12. Generation, annotation, and analysis of an extensive Aspergillus niger EST collection in BMC MICROBIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1186/1754-6834-6-111

    DOI

    http://dx.doi.org/10.1186/1754-6834-6-111

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/23915965


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        "description": "BACKGROUND: Microorganisms are the most proficient decomposers in nature, using secreted enzymes in the hydrolysis of lignocellulose. As such, they present the most abundant source for discovery of new enzymes. Acremonium alcalophilum is the only known cellulolytic fungus that thrives in alkaline conditions and can be cultured readily in the laboratory. Its optimal conditions for growth are 30\u00b0C and pH\u00a09.0-9.2. The genome sequence of Acremonium alcalophilum has revealed a large number of genes encoding biomass-degrading enzymes. Among these enzymes, lipases are interesting because of several industrial applications including biofuels, detergent, food processing and textile industries.\nRESULTS: We identified a lipA gene in the genome sequence of Acremonium alcalophilum, encoding a protein with a predicted lipase domain with weak sequence identity to characterized enzymes. Unusually, the predicted lipase displays\u2009\u2248\u200930% amino acid sequence identity to both feruloyl esterase and lipase of Aspergillus niger. LipA, when transiently produced in Nicotiana benthamiana, accumulated to over 9% of total soluble protein. Plant-produced recombinant LipA is active towards p-nitrophenol esters of various carbon chain lengths with peak activity on medium-chain fatty acid (C8). The enzyme is also highly active on xylose tetra-acetate and oat spelt xylan. These results suggests that LipA is a novel lipolytic enzyme that possesses both lipase and acetylxylan esterase activity. We determined that LipA is a glycoprotein with pH and temperature optima at 8.0 and 40\u00b0C, respectively.\nCONCLUSION: Besides being the first heterologous expression and characterization of a gene coding for a lipase from A. alcalophilum, this report shows that LipA is very versatile exhibiting both acetylxylan esterase and lipase activities potentially useful for diverse industry sectors, and that tobacco is a suitable bioreactor for producing fungal proteins.", 
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