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

Title:

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

Pereira, Eridan, Tsang, Adrian, McAllister, Tim A and Menassa, Rima (2013) The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor. Biotechnology for Biofuels, 6 (1). p. 111. ISSN 1754-6834

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

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.

Divisions:Concordia University > Faculty of Arts and Science > Biology
Item Type:Article
Refereed:Yes
Authors:Pereira, Eridan and Tsang, Adrian and McAllister, Tim A and Menassa, Rima
Journal or Publication:Biotechnology for Biofuels
Date:2013
Digital Object Identifier (DOI):10.1186/1754-6834-6-111
ID Code:978151
Deposited By: DAVID MACAULAY
Deposited On:10 Jan 2014 21:04
Last Modified:18 Jan 2018 17:46
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