Keyword search (4,163 papers available)

"Carbohydrate active enzyme" Keyword-tagged Publications:

Title Authors PubMed ID
1 Identification of Genes Involved in the Degradation of Lignocellulose Using Comparative Transcriptomics. Gruninger RJ, Reid I, Forster RJ, Tsang A, McAllister TA 28417376
CSFG
2 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
3 Saccharification efficiencies of multi-enzyme complexes produced by aerobic fungi. Badhan A, Huang J, Wang Y, Abbott DW, Di Falco M, Tsang A, McAllister T 29803771
CSFG
4 Application of Transcriptomics to Compare the Carbohydrate Active Enzymes That Are Expressed by Diverse Genera of Anaerobic Fungi to Degrade Plant Cell Wall Carbohydrates. Gruninger RJ, Nguyen TTM, Reid ID, Yanke JL, Wang P, Abbott DW, Tsang A, McAllister T 30061875
CSFG

 

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
Publication:New biotechnology
Keywords:Aerobic fungi;  Barley straw;  Blue native PAGE;  Carbohydrate active enzymes;  Glycosyl hydrolase;  Multi-enzyme complex; 
PMID:29803771 Category:N Biotechnol Date Added:2019-06-07
Dept Affiliation: CSFG
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]




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