scholarly journals Cellulolytic and xylanolytic enzyme complex of Penicillium funiculosum Thom

Author(s):  
O. M. Yurieva ◽  
A. P. Hryhanskyi ◽  
S. O. Syrchin ◽  
L. T. Nakonechna ◽  
A. K. Pavlychenko ◽  
...  

Aim. The aim of this research was a comparative study of β-glucosidase activity of endophytic and soil Penicillium funiculosum strains. Methods. β-Gucosidase activity was determined by hydrolysis of pNPG on 4th and 6th days of cultivation. Barcoding of P. funiculosum 16795 DNA was carried out with ITS1 and ITS4 primers. Results. Obtained data demonstrate the ability of endophytic and soil P. funiculosum strains to synthesize β-glucosidase activity and hydrolyze Na-CMC and wheat straw. Studied activities enhanced with increasing cultivation time of micromycetes. Endophytic isolates of P. funiculosum had higher β-glucosidase activities than soil ones. Conclusions. P. funiculosum strains, especially 16795, are promising for further research of β-glucosidase preparations as additional component to the T. reesei enzymes, as well as to create recombinant constructs for obtaining a balanced composition of cellulolytic enzyme complexes.Keywords: Penicillium funiculosum, β-glucosidase activity, endophytes, soil strains.

RSC Advances ◽  
2014 ◽  
Vol 4 (84) ◽  
pp. 44726-44732 ◽  
Author(s):  
Mukund Adsul ◽  
Bhawna Sharma ◽  
Reeta Rani Singhania ◽  
Jitendra Kumar Saini ◽  
Ankita Sharma ◽  
...  

A prepared enzyme cocktail from different fungal enzyme preparations increases the hydrolysis of avicel/wheat straw by increasing synergism between the same or different types of cellulases.


Fermentation ◽  
2021 ◽  
Vol 7 (1) ◽  
pp. 22
Author(s):  
Natalia S. Brizuela ◽  
Marina Arnez-Arancibia ◽  
Liliana Semorile ◽  
María Ángeles Pozo-Bayón ◽  
Bárbara M. Bravo-Ferrada ◽  
...  

Lactiplantibacillus plantarum strain UNQLp 11 is a lactic acid bacterium with the potential to carry out malolactic fermentation (MLF) in red wines. Recently, the complete genome of UNQLp 11 was sequenced and this strain possesses four loci of the enzyme β-glucosidase. In order to demonstrate that these glucosidase enzymes could be functional under harsh wine conditions, we evaluated the hydrolysis of p-nitrophenyl-β-D-glucopyranoside (p-NPG) in synthetic wine with different ethanol contents (0%, 12%, and 14% v/v) and at different pH values (3.2, 3.5, and 3.8). Then, the hydrolysis of precursor n-octyl β-D-glucopyranoside was analyzed in sterile Pinot Noir wine (containing 14.5% v/v of ethanol, at different pH values) by headspace sorptive extraction gas chromatography-mass spectrometry (HSSE-GC/MS). The hydrolysis of p-NPG showed that β-glucosidase activity is very susceptible to low pH but induced in the presence of high ethanol content. Furthermore, UNQLp 11 was able to release the glycosilated precursor n-octyl, during MLF to a greater extent than a commercial enzyme. In conclusion, UNQLp 11 could improve the aromatic profile of the wine by the release of volatile precursors during MLF.


2008 ◽  
Vol 153 (1-3) ◽  
pp. 116-126 ◽  
Author(s):  
Luís C. Duarte ◽  
Talita Silva-Fernandes ◽  
Florbela Carvalheiro ◽  
Francisco M. Gírio

Nahrung/Food ◽  
1997 ◽  
Vol 41 (4) ◽  
pp. 201-207 ◽  
Author(s):  
C. Legay ◽  
Y. Popineau ◽  
S. Bérot ◽  
J. Guéguen

2012 ◽  
Vol 87 (2) ◽  
pp. 1280-1285 ◽  
Author(s):  
Greta Radeva ◽  
Ivo Valchev ◽  
Stoiko Petrin ◽  
Eva Valcheva ◽  
Petya Tsekova

Catalysts ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1343
Author(s):  
Mpho S. Mafa ◽  
Brett I. Pletschke ◽  
Samkelo Malgas

Lignocellulose has economic potential as a bio-resource for the production of value-added products (VAPs) and biofuels. The commercialization of biofuels and VAPs requires efficient enzyme cocktail activities that can lower their costs. However, the basis of the synergism between enzymes that compose cellulolytic enzyme cocktails for depolymerizing lignocellulose is not understood. This review aims to address the degree of synergism (DS) thresholds between the cellulolytic enzymes and how this can be used in the formulation of effective cellulolytic enzyme cocktails. DS is a powerful tool that distinguishes between enzymes’ synergism and anti-synergism during the hydrolysis of biomass. It has been established that cellulases, or cellulases and lytic polysaccharide monooxygenases (LPMOs), always synergize during cellulose hydrolysis. However, recent evidence suggests that this is not always the case, as synergism depends on the specific mechanism of action of each enzyme in the combination. Additionally, expansins, nonenzymatic proteins responsible for loosening cell wall fibers, seem to also synergize with cellulases during biomass depolymerization. This review highlighted the following four key factors linked to DS: (1) a DS threshold at which the enzymes synergize and produce a higher product yield than their theoretical sum, (2) a DS threshold at which the enzymes display synergism, but not a higher product yield, (3) a DS threshold at which enzymes do not synergize, and (4) a DS threshold that displays anti-synergy. This review deconvolutes the DS concept for cellulolytic enzymes, to postulate an experimental design approach for achieving higher synergism and cellulose conversion yields.


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