Keyword search (4,163 papers available)

"McAllister TA" Authored Publications:

Title Authors PubMed ID
1 Identification of Genes Involved in the Degradation of Lignocellulose Using Comparative Transcriptomics Gruninger RJ; Tsang A; McAllister TA; 37149538
CSFG
2 Effect of ammonia fiber expansion-treated wheat straw and a recombinant fibrolytic enzyme on rumen microbiota and fermentation parameters, total tract digestibility, and performance of lambs. Ribeiro GO; Gruninger RJ; Jones DR; Beauchemin KA; Yang WZ; Wang Y; Abbott DW; Tsang A; McAllister TA; 32369600
CSFG
3 Effects of a recombinant fibrolytic enzyme on fiber digestion, ruminal fermentation, nitrogen balance and total tract digestibility of heifers fed a high forage diet. Ran T, Saleem AM, Shen Y, Ribeiro GO, Beauchemin KA, Tsang A, Yang W, McAllister TA 31251799
CSFG
4 The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor. Pereira EO, Tsang A, McAllister TA, Menassa R 23915965
CSFG
5 Improvement in Saccharification Yield of Mixed Rumen Enzymes by Identification of Recalcitrant Cell Wall Constituents Using Enzyme Fingerprinting. Badhan A, Wang YX, Gruninger R, Patton D, Powlowski J, Tsang A, McAllister TA 26180803
CSFG
6 Identification of Genes Involved in the Degradation of Lignocellulose Using Comparative Transcriptomics. Gruninger RJ, Reid I, Forster RJ, Tsang A, McAllister TA 28417376
CSFG
7 Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates. Jones DR, Uddin MS, Gruninger RJ, Pham TTM, Thomas D, Boraston AB, Briggs J, Pluvinage B, McAllister TA, Forster RJ, Tsang A, Selinger LB, Abbott DW 28588026
CSFG
8 Identification of novel enzymes to enhance the ruminal digestion of barley straw Badhan A; Ribeiro GO; Jones DR; Wang Y; Abbott DW; Di Falco M; Tsang A; McAllister TA; 29621684
CSFG
9 New recombinant fibrolytic enzymes for improved in vitro ruminal fiber degradability of barley straw. Ribeiro GO, Badhan A, Huang J, Beauchemin KA, Yang W, Wang Y, Tsang A, McAllister TA 30053012
CSFG

 

Title:The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor.
Authors:Pereira EO,  Tsang A,  McAllister TA,  Menassa R
Link:https://www.ncbi.nlm.nih.gov/pubmed/23915965?dopt=Abstract
DOI:10.1186/1754-6834-6-111
Publication:Biotechnology for biofuels
Keywords:Acetylxylan esterase Acremonium alcalophilum;  Heterologous expression;  Lipase;  Nicotiana benthamiana; 
PMID:23915965 Category:Biotechnol Biofuels Date Added:2019-06-07
Dept Affiliation: CSFG
1 Agriculture and Agri-Food Canada, 1391 Sandford Street, London, ON N5V 4T3, Canada ; Department of Biology, The University of Western Ontario, London, ON N6A 5B7, Canada.
2 Centre for Structural and Functional Genomics, Concordia University, Montreal, Quebec H4B 1R6, Canada.
3 Agriculture and Agri-Food Canada, Lethbridge Research Centre, Lethbridge, AB T1J 4B1, Canada.

Description:

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

Biotechnol Biofuels. 2013;6:111

Authors: Pereira EO, Tsang A, McAllister TA, Menassa R

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.

PMID: 23915965 [PubMed]




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