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Saccharification efficiencies of multi-enzyme complexes produced by aerobic fungi.

Author(s): Badhan A, Huang J, Wang Y, Abbott DW, Di Falco M, Tsang A, McAllister T

N Biotechnol. 2018 Nov 25;46:1-6 Authors: Badhan A, Huang J, Wang Y, Abbott DW, Di Falco M, Tsang A, McAllister T

Article GUID: 29803771
The presence of trace components significantly broadens the molecular response of Aspergillus niger to guar gum.

Author(s): Coconi Linares N, Di Falco M, Benoit-Gelber I, Gruben BS, Peng M, Tsang A, Mäkelä MR, de Vries RP

N Biotechnol. 2019 Jul 25;51:57-66 Authors: Coconi Linares N, Di Falco M, Benoit-Gelber I, Gruben BS, Peng M, Tsang A, Mäkelä MR, de Vries RP

Article GUID: 30797054
Title:Saccharification efficiencies of multi-enzyme complexes produced by aerobic fungi.
Authors:Badhan A,  Huang J,  Wang Y,  Abbott DW,  Di Falco M,  Tsang A,  McAllister T
Link:https://www.ncbi.nlm.nih.gov/pubmed/29803771?dopt=Abstract
DOI:10.1016/j.nbt.2018.05.003
Category:N Biotechnol
PMID:29803771
Dept Affiliation: GENOMICS
1 Agriculture and Agri-Food Canada, Lethbridge Research Centre, Lethbridge, Alberta, Canada.
2 Institute of Biological Resources, Jiangxi Academy of Sciences, Nanchang, 330096, China.
3 Centre for Structural and Functional Genomics, Concordia University, Montreal, Quebec, H4B 1R6, Canada.
4 Agriculture and Agri-Food Canada, Lethbridge Research Centre, Lethbridge, Alberta, Canada. Electronic address: tim.mcallister@agr.gc.ca.

Description:

Saccharification efficiencies of multi-enzyme complexes produced by aerobic fungi.

N Biotechnol. 2018 Nov 25;46:1-6

Authors: Badhan A, Huang J, Wang Y, Abbott DW, Di Falco M, Tsang A, McAllister T

Abstract

In the present study, we have characterized high molecular weight multi-enzyme complexes in two commercial enzymes produced by Trichoderma reesei (Spezyme CP) and Penicillium funiculosum (Accellerase XC). We successfully identified 146-1000?kDa complexes using Blue native polyacrylamide gel electrophoresis (BN-PAGE) to fractionate the protein profile in both preparations. Identified complexes dissociated into lower molecular weight constituents when loaded on SDS PAGE. Unfolding of the secondary structure of multi-enzyme complexes with trimethylamine (pH >10) suggested that they were not a result of unspecific protein aggregation. Cellulase (CMCase) profiles of extracts of BN-PAGE fractionated protein bands confirmed cellulase activity within the multi-enzyme complexes. A microassay was used to identify protein bands that promoted high levels of glucose release from barley straw. Those with high saccharification yield were subjected to LC-MS analysis to identify the principal enzymatic activities responsible. The results suggest that secretion of proteins by aerobic fungi leads to the formation of high molecular weight multi-enzyme complexes that display activity against carboxymethyl cellulose and barley straw.

PMID: 29803771 [PubMed - indexed for MEDLINE]