Keyword search (4,163 papers available)

"proteome" Keyword-tagged Publications:

Title Authors PubMed ID
1 Comparative Analysis of Enzyme Production Patterns of Lignocellulose Degradation of Two White Rot Fungi: Obba rivulosa and Gelatoporia subvermispora Marinovíc M; Di Falco M; Aguilar Pontes MV; Gorzsás A; Tsang A; de Vries RP; Mäkelä MR; Hildén K; 35892327
CSFG
2 Predicted coronavirus Nsp5 protease cleavage sites in the human proteome Scott BM; Lacasse V; Blom DG; Tonner PD; Blom NS; 35379171
ENCS
3 Combination of system biology and classical approaches for developing biorefinery relevant lignocellulolytic Rasamsonia emersonii strain Raheja Y; Singh V; Kaur B; Basotra N; Di Falco M; Tsang A; Singh Chadha B; 35318142
CSFG
4 Penicillium subrubescens adapts its enzyme production to the composition of plant biomass. Dilokpimol A, Peng M, Di Falco M, Chin A Woeng T, Hegi RMW, Granchi Z, Tsang A, Hildén KS, Mäkelä MR, de Vries RP 32408196
CSFG
5 Lithocholic bile acid accumulated in yeast mitochondria orchestrates a development of an anti-aging cellular pattern by causing age-related changes in cellular proteome. Beach A, Richard VR, Bourque S, Boukh-Viner T, Kyryakov P, Gomez-Perez A, Arlia-Ciommo A, Feldman R, Leonov A, Piano A, Svistkova V, Titorenko VI 25839782
MASSSPEC
6 Evaluation of secretome of highly efficient lignocellulolytic Penicillium sp. Dal 5 isolated from rhizosphere of conifers. Rai R, Kaur B, Singh S, Di Falco M, Tsang A, Chadha BS 27341464
CSFG
7 Isolation and Preparation of Extracellular Proteins from Lignocellulose Degrading Fungi for Comparative Proteomic Studies Using Mass Spectrometry Robert J Gruninger 28417377
CSFG
8 Mass Spectrometry-Based Proteomics Marcos Rafael Di Falco 29876812
CSFG
9 The presence of trace components significantly broadens the molecular response of Aspergillus niger to guar gum. Coconi Linares N, Di Falco M, Benoit-Gelber I, Gruben BS, Peng M, Tsang A, Mäkelä MR, de Vries RP 30797054
CSFG

 

Title:The presence of trace components significantly broadens the molecular response of Aspergillus niger to guar gum.
Authors:Coconi Linares N,  Di Falco M,  Benoit-Gelber I,  Gruben BS,  Peng M,  Tsang A,  Mäkelä MR,  de Vries RP
Link:https://www.ncbi.nlm.nih.gov/pubmed/30797054?dopt=Abstract
DOI:10.1016/j.nbt.2019.02.005
Publication:New biotechnology
Keywords:Aspergillus niger;  CAZymes;  Exoproteome;  Guar gum;  Plant biomass degradation;  Transcriptome; 
PMID:30797054 Category:N Biotechnol Date Added:2019-06-07
Dept Affiliation: CSFG
1 Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT, Utrecht, the Netherlands.
2 Center for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, Quebec H4B 1R6, Canada.
3 Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT, Utrecht, the Netherlands; Center for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke Street West, Montreal, Quebec H4B 1R6, Canada; Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, the Netherlands.
4 Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT, Utrecht, the Netherlands; Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, the Netherlands.
5 Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT, Utrecht, the Netherlands; Department of Microbiology, P.O. Box 56, Viikinkaari 9, University of Helsinki, Helsinki, Finland.
6 Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, 3584 CT, Utrecht, the Netherlands; Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, the Netherlands. Electronic address: r.devries@westerdijkinstitute.nl.

Description:

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

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

Abstract

Guar gum consists mainly of galactomannan and constitutes the endosperm of guar seeds that acts as a reserve polysaccharide for germination. Due to its molecular structure and physical properties, this biopolymer has been considered as one of the most important and widely used gums in industry. However, for many of these applications this (hemi-)cellulosic structure needs to be modified or (partially) depolymerized in order to customize and improve its physicochemical properties. In this study, transcriptome, exoproteome and enzyme activity analyses were employed to decipher the complete enzymatic arsenal for guar gum depolymerization by Aspergillus niger. This multi-omic analysis revealed a set of 46 genes encoding carbohydrate-active enzymes (CAZymes) responding to the presence of guar gum, including CAZymes not only with preferred activity towards galactomannan, but also towards (arabino-)xylan, cellulose, starch and pectin, likely due to trace components in guar gum. This demonstrates that the purity of substrates has a strong effect on the resulting enzyme mixture produced by A. niger and probably by other fungi as well, which has significant implications for the commercial production of fungal enzyme cocktails.

PMID: 30797054 [PubMed - indexed for MEDLINE]




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