scholarly journals Cellulose-containing waste recycling using fungi

2021 ◽  
Vol 17 (5) ◽  
pp. 123-133
Author(s):  
I. A. Fomenko ◽  
S. N. Tuchkova
Keyword(s):  
Renewable Energy Sources ◽  
Starter Cultures ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Enzyme ◽  
Cellulolytic Activity ◽  
Irpex Lacteus ◽  
Thermostable Enzymes ◽  
Glycosidic Bonds ◽  
Plant Waste ◽  
Simple Carbohydrates

Accumulation of plant waste is a serious environmental problem. Mushrooms with high cellulolytic activity can process it into valuable products that will be useful in solving various industries and agriculture problems. The enzymes of the cellulolytic complex include 1,4-β-D-glucan-4-glucanohydrolase, exo-1,4-β-glucosidase, cellobiohydrolase, β-glucosidase. 1,4-β-D-glucan-4-glucanohydrolases destroy β-1,4-glycosidic bonds within the chain of cellulose and lichenin polysaccharides. Exoglucanases destroy β-1,3- and β-1,4-glycosidic bonds at the end of the molecule. Cellobiohydrolases cleave β-1,4-glycosidic bonds to form cellobiose and glucose. β-glucosidase complete the process of destruction. Fungi with high cellulolytic activity include both representatives of the Ascomycota and Basidiomycota divisions. Ascomycete Chaetomium globosum produces endoglucanases of two families and 8 cellobiohydrolases. Myceliophthora thermophila also produces endoglucanases and cellobiohydrolases, the most abundant of which is Mt Cel7A. The fungus is a promising producer of thermostable enzymes. Trichoderma reesei has a long history of safe use as a source of highly active cellulolytic enzymes and other valuable metabolites. LPMOs of the cellulolytic fungus Thielavia terrestris are considered auxiliary enzymes, but can negatively affect the main enzymes of the complex. Irpex lacteus also produces LPMO and a complete cellulolytic enzyme complex. The cellulolytic activity of fungi and their ability to grow on cheap substrates can be used to bioconvert plant waste into valuable products. One of the ways to utilize them is to convert into compound feed with a high protein content through the use of starter cultures. The use of mushrooms will increase the content of protein and simple carbohydrates, enrich the feed with fats. Another method is to obtain cellulases, which are widely used in many industries. Thanks to the production of biodiesel and bioethanol from cellulose-containing raw materials it is possible to solve the problem of lack of fuel by replacing energy carriers from non-renewable energy sources with their environmentally friendly counterparts. They are less toxic than diesel and gasoline and are also made from renewable resources.

scholarly journals Cellulolytic ability of a promising Irpex lacteus (Basidiomycota: Polyporales) strain from the subtropical rainforest of Misiones province, Argentina

2018 ◽  
Vol 66 (3) ◽  
pp. 1034 ◽  
Author(s):  
Ernesto Martin Giorgio ◽  
Laura Lidia Villalba ◽  
Gerardo Lucio Robledo ◽  
Pedro Dario Zapata ◽  
Mario Carlos Saparrat
Keyword(s):  
Agar Medium ◽  
Technological Development ◽  
White Rot Fungi ◽  
White Rot ◽  
Cellulolytic Enzymes ◽  
Crystalline Cellulose ◽  
Its Sequence ◽  
Cellulolytic Activity ◽  
Irpex Lacteus ◽  
Misiones Province

The cellulolytic activity of fungi growing in the subtropical rainforest of Misiones (Argentina) represents a challenge in the technological development of the production of cellulosic bioethanol in the region using native sources. These fungi are promising to obtain sustainable enzyme cocktails using their enzymes. Cellulolytic ability of 22 white-rot fungi isolated from the subtropical rainforest of Misiones-Argentina in agar medium with two types of cellulosic substrates, carboxy-methylcellulose or crystalline cellulose, were comparatively analyzed, and the activity of two cellulolytic enzymes was evaluated in liquid medium. Although all isolates were able to grow and degrade both substrates in agar medium, and to produce total cellulase Filter paper (FPase) and endo-β-1,4-glucanase (EG) activities in broth, the isolate Irpex sp. LBM 034 showed the greatest enzymatic levels (FPase, 65.45 U L-1; EG, 221.21 U L-1). Therefore, the ITS sequence of this fungus was sequenced and analyzed through a phylogenetic analysis. These results indicate that the isolate LBM 034, corresponding to Irpex lacteus, has a promising cellulolytic ability and enzymes such as EG useful in sustainable saccharification of cellulosic materials in the region.

scholarly journals An Efficient and Improved Methodology for the Screening of Industrially Valuable Xylano-Pectino-Cellulolytic Microbes

2015 ◽  
Vol 2015 ◽  
pp. 1-7 ◽  
Author(s):  
Avtar Singh ◽  
Amanjot Kaur ◽  
Anita Dua ◽  
Ritu Mahajan
Keyword(s):  
Low Cost ◽  
Cost Effective ◽  
Industrial Sector ◽  
Agricultural Residues ◽  
High Yield ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Activity ◽  
Nutrient Media ◽  
First Report ◽  
Primary Screening

Xylano-pectino-cellulolytic enzymes are valuable enzymes of the industrial sector. In our earlier study, we have reported a novel and cost effective methodology for the qualitative screening of cellulase-free xylano-pectinolytic microorganisms by replacing the commercial, highly expensive substrates with agricultural residues, but the microorganisms with xylanolytic, pectinolytic, cellulolytic, xylano-pectinolytic, xylano-cellulolytic, pectino-cellulolytic, and xylano-pectino-cellulolytic potential were obtained. The probability of getting the desired combination was low, so efforts were made to further improve this cost effective methodology for obtaining the high yield of the microbes capable of producing desired combination of enzymes. By inclusion of multiple enrichment steps in sequence, using only practically low cost substrates and without any nutrient media till primary screening stage, this improved novel protocol for screening gave only the desired microorganisms with xylano-pectino-cellulolytic activity. Using this rapid, efficient, cost effective, and improved methodology, microbes with required combination of enzymes can be obtained and the probability of getting the desired microorganisms is cent percent. This is the first report presenting the methodology for the isolation of xylano-pectino-cellulolytic positive microorganisms at low cost and consuming less time.

scholarly journals PRODUCTION AND CHARACTERIZATION OF CELLULOLYTIC ENZYMES BY ASPERGILLUS NIGER AND RHIZOPUS SP. BY SOLID STATE FERMENTATION OF PRICKLY PEAR

2016 ◽  
Vol 29 (1) ◽  
pp. 222-233 ◽  
Author(s):  
TAMIRES CARVALHO DOS SANTOS ◽  
GEORGE ABREU FILHO ◽  
AILA RIANY DE BRITO ◽  
AURELIANO JOSÉ VIEIRA PIRES ◽  
RENATA CRISTINA FERREIRA BONOMO ◽  
...  
Keyword(s):  
Solid State ◽  
Aspergillus Niger ◽  
Water Activity ◽  
Solid State Fermentation ◽  
Cellulase Production ◽  
Cellulolytic Enzymes ◽  
Optimum Conditions ◽  
Thermostable Enzymes ◽  
Fermentation Time ◽  
Rhizopus Sp

ABSTRACT: Prickly palm cactus husk was used as a solid-state fermentation support substrate for the production of cellulolytic enzymes using Aspergillus niger and Rhizopus sp. A Box-Behnken design was used to evaluate the effects of water activity, fermentation time and temperature on endoglucanase and total cellulase production. Response Surface Methodology showed that optimum conditions for endoglucanase production were achieved at after 70.35 h of fermentation at 29.56°C and a water activity of 0.875 for Aspergillus niger and after 68.12 h at 30.41°C for Rhizopus sp. Optimum conditions for total cellulase production were achieved after 74.27 h of fermentation at 31.22°C for Aspergillus niger and after 72.48 h and 27.86°C for Rhizopus sp. Water activity had a significant effect on Aspergillus niger endoglucanase production only. In industrial applications, enzymatic characterization is important for optimizing variables such as temperature and pH. In this study we showed that endoglucanase and total cellulase had a high level of thermostability and pH stability in all the enzymatic extracts. Enzymatic deactivation kinetic experiments indicated that the enzymes remained active after the freezing of the crude extract. Based on the results, bioconversion of cactus is an excellent alternative for the production of thermostable enzymes.

scholarly journals Defining the Frontiers of Synergism between Cellulolytic Enzymes for Improved Hydrolysis of Lignocellulosic Feedstocks

Catalysts ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1343
Author(s):  
Mpho S. Mafa ◽  
Brett I. Pletschke ◽  
Samkelo Malgas
Keyword(s):  
Value Added ◽  
Product Yield ◽  
Cellulose Hydrolysis ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Enzyme ◽  
Key Factors ◽  
Cellulose Conversion ◽  
Lignocellulosic Feedstocks ◽  
Polysaccharide Monooxygenases ◽  
Hydrolysis Of

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.

Cellulosomes localise on the surface of membrane vesicles from the cellulolytic bacterium Clostridium thermocellum

2019 ◽  
Vol 366 (12) ◽  
Author(s):  
Shunsuke Ichikawa ◽  
Satoru Ogawa ◽  
Ayami Nishida ◽  
Yuzuki Kobayashi ◽  
Toshihito Kurosawa ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Cell Communication ◽  
Membrane Vesicles ◽  
Cellulolytic Enzymes ◽  
Crystalline Cellulose ◽  
Cellulolytic Bacterium ◽  
Cellulolytic Activity ◽  
Cellulolytic Bacteria ◽  
Degradation Activity ◽  
Enzyme Complexes

ABSTRACTMembrane vesicles released from bacteria contribute to cell–cell communication by carrying various cargos such as proteins, nucleic acids and signaling molecules. Cellulolytic bacteria have been isolated from many environments, yet the function of membrane vesicles for cellulolytic ability has been rarely described. Here, we show that a Gram-positive cellulolytic bacterium Clostridium thermocellum released membrane vesicles, each approximately 50–300 nm in diameter, into the broth. The observations with immunoelectron microscopy also revealed that cellulosomes, which are carbohydrate-active enzyme complexes that give C. thermocellum high cellulolytic activity, localized on the surface of the membrane vesicles. The membrane vesicles collected by ultracentrifugation maintained the cellulolytic activity. Supplementation with the biosurfactant surfactin or sonication treatment disrupted the membrane vesicles in the exoproteome of C. thermocellum and significantly decreased the degradation activity of the exoproteome for microcrystalline cellulose. However, these did not affect the degradation activity for soluble carboxymethyl cellulose. These results suggest a novel function of membrane vesicles: C. thermocellum releases cellulolytic enzymes on the surface of membrane vesicles to enhance the cellulolytic activity of C. thermocellum for crystalline cellulose.

Ultrastructural Localization of Cellulase in Diplodia Maydis and in D. Maydis-Infected Com Stalk Tissue

1977 ◽  
Vol 35 ◽  
pp. 454-455
Author(s):  
Judith A. Murphy ◽  
Mary R. Thompson ◽  
A.J. Pappelis
Keyword(s):  
Culture Medium ◽  
Cupric Oxide ◽  
Cellulase Activity ◽  
Growth Period ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Low Ph ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Activity ◽  
X Ray

BeMiller et.al.(l) found that D. maydis did not have the solubilizing enzyme C1. They reported that D- maydis exhibited cellulolytic activity constitutively, and hypothesized that the cellulolytic enzymes were attached to fungal hyphal surfaces because they found cellulase released to the culture medium only after the growth period, when available cellulose had been used up.The purpose of this study was to determine the location of cellulolytic enzymes (EC 3.2.1.4; beta-1,4-glucan glucanohydrolase) in D. maydis and D. maydis-infected corn tissue at the ultrastructural level.Cellulase activity produces glucose as an end product which will reduce cupric oxide and can be visualized with an EM because it is electron dense and the Cu component can be verified with x-ray analysis(Figs.l,2). After thorough washing, samples fixed in aldehydes are incubated in a substrate mixture at a low pH. The enzyme is activated and reducing sugar is released. The sample is then reacted with Benedict's solution at a high temperature, allowing CuO crystals to be deposited at the site of reaction.

scholarly journals Crystallization and preliminary X-ray diffraction analysis of an endo-1,4-β-D-glucanase fromAspergillus aculeatusF-50

2015 ◽  
Vol 71 (4) ◽  
pp. 397-400 ◽  
Author(s):  
Yun Chen ◽  
Jian-Wen Huang ◽  
Chun-Chi Chen ◽  
Hui-Lin Lai ◽  
Jian Jin ◽  
...  
Keyword(s):  
Model Building ◽  
Structure Refinement ◽  
Diffusion Method ◽  
Cellulolytic Enzyme ◽  
Glycoside Hydrolase Family ◽  
X Ray Diffraction ◽  
Orthorhombic Space Group ◽  
Cell Parameters ◽  
Renewable Biomass ◽  
Glycosidic Bonds

Cellulose is the most abundant renewable biomass on earth, and its decomposition has proven to be very useful in a wide variety of industries. Endo-1,4-β-D-glucanase (EC 3.2.1.4; endoglucanase), which can catalyze the random hydrolysis of β-1,4-glycosidic bonds to cleave cellulose into smaller fragments, is a key cellulolytic enzyme. An endoglucanase isolated fromAspergillus aculeatusF-50 (FI-CMCase) that was classified into glycoside hydrolase family 12 has been found to be effectively expressed in the industrial strainPichia pastoris. Here, recombinant FI-CMCase was crystallized. Crystals belonging to the orthorhombic space groupC2221, with unit-cell parametersa= 74.2,b= 75.1,c= 188.4 Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 1.6 Å resolution. Initial phase determination by molecular replacement clearly shows that the crystal contains two protein molecules in the asymmetric unit. Further model building and structure refinement are in progress.

Carbon nutrition and hydrolytic and cellulolytic activities in the ectomycorrhizal fungus Pisolithus tinctorius

1993 ◽  
Vol 39 (5) ◽  
pp. 529-535 ◽  
Author(s):  
Weiguo Cao ◽  
Don L. Crawford
Keyword(s):  
Hydrolytic Enzymes ◽  
Ectomycorrhizal Fungus ◽  
Isozyme Pattern ◽  
Pisolithus Tinctorius ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Activity ◽  
Gradient Gel Electrophoresis ◽  
Carbon Nutrition ◽  
High Concentrations ◽  
Increased Activity

Four strains of an ectomycorrhizal fungus, Pisolithus tinctorius, were investigated for carbon nutrition, and for production of hydrolytic and cellulolytic enzymes. Glucose, mannose, and cellobiose supported rapid mycelial growth of all four strains. Fructose was utilized by two strains, SMF and S359. Of the 10 hydrolytic enzymes examined, acid phosphatase, acid α-galactosidase, acid esterase, and acid β-glucosidase were found in all four strains. β-Galactosidase was only observed in strain S359. α-Mannosidase, β-mannosidase, α-glucosidase, β-xylosidase, and proteinase were not detected in any of the four strains. Isozyme patterns of β-glucosidase and esterase in the four strains were compared by activity staining after native gradient gel electrophoresis. The isozyme pattern of β-glucosidase showed three major forms in all four strains. In addition, two more isoforms were found in strain S370. All strains shared two esterase bands, while strain S370 had three more isoforms. Study on strain SMF indicated that acid β-glucosidase was expressed constitutively, with increased activity in cellobiose-containing media. Under nitrogen-limiting conditions, a low level of endoglucanase and exoglucanase activity was observed in strains SMF and S359. Further study on S359 showed that high concentrations of nitrogen repressed the cellulolytic activity. When cellobiose served as carbon source, higher cellulolytic activity was observed. Cellulose did not induce higher activity.Key words: Pisolithus, ectomycorrhizal, β-glucosidase, hydrolytic enzymes, cellulolytic enzymes.

scholarly journals The use of lytic polysaccharide monooxygenases in anaerobic digestion of lignocellulosic materials

2019 ◽  
Vol 12 (1) ◽  
Author(s):  
Thales H. F. Costa ◽  
Vincent G. H. Eijsink ◽  
Svein Jarle Horn
Keyword(s):  
Anaerobic Digestion ◽  
Methane Production ◽  
Biogas Production ◽  
Process Efficiency ◽  
Cellulolytic Enzymes ◽  
Cellulolytic Enzyme ◽  
Lignocellulosic Materials ◽  
Active Components ◽  
Enzyme Preparations ◽  
The Impact

Abstract Background The recent discovery that LPMOs can work under anaerobic conditions when supplied with low amounts H2O2 opens the possibility of using LPMOs as enzyme aids in biogas reactors to increase methane yields from lignocellulosic materials. We have explored this possibility by studying anaerobic digestion of various lignocellulosic materials: Avicel, milled spruce and birch wood, and a lignin-rich hydrolysis residue from steam-exploded birch. The digestions were added LPMOs and various cellulolytic enzyme cocktails and were carried out with or without addition of H2O2. Results In several cases, enzyme addition had a beneficial effect on methane production, which was partly due to components present in the enzyme preparations. It was possible to detect LPMO activity during the initial phases of the anaerobic digestions of Avicel, and in some cases LPMO activity could be correlated with improved methane production from lignocellulosic materials. However, a positive effect on methane production was only seen when LPMOs were added together with cellulases, and never upon addition of LPMOs only. Generally, the experimental outcomes showed substrate-dependent variations in process efficiency and the importance of LPMOs and added H2O2. These differences could relate to variations in the type and content of lignin, which again will affect the activity of the LPMO, the fate of the added H2O2 and the generation of potentially damaging reactive-oxygen species. The observed effects showed that the interplay between cellulases and LPMOs is important for the overall efficiency of the process. Conclusion This study shows that it may be possible to harness the power of LPMOs in anaerobic digestion processes and improve biogas production, but also highlight the complexity of the reaction systems at hand. One complicating factor was that the enzymes themselves and other organic components in the enzyme preparations acted as substrates for biogas production, meaning that good control reactions were essential to detect effects caused by enzyme activity. As also observed during regular aerobic enzymatic digestion of lignocellulosic biomass, the type and contents of lignin in the substrates likely plays a major role in determining the impact of LPMOs and of cellulolytic enzymes in general. More work is needed to unravel the interplay between LPMOs, O2, H2O2, and the multitude of redox-active components found in anaerobic bioreactors degrading lignocellulosic substrates.

Location of cellulolytic enzyme activity in the marine fungus Trichocladium achrasporum

1985 ◽  
Vol 31 (2) ◽  
pp. 145-148 ◽  
Author(s):  
Malcolm J. MacDonald ◽  
Donna L. Hartley ◽  
Marilyn K. Speedie
Keyword(s):  
Cellulase Activity ◽  
Marine Fungus ◽  
Particulate Fraction ◽  
Cellulolytic Enzymes ◽  
Crystalline Cellulose ◽  
Cellulolytic Enzyme ◽  
Active Growth ◽  
Endoglucanase Activity ◽  
Produce Cell ◽  
Soluble Cell

Cellulase activity in Trichocladium achrasporum was demonstrated by its ability to produce cell-associated and extracellular cellulolytic enzymes when grown on a crystalline cellulose substrate. In addition, azure dye was solubilized from dyed crystalline cellulose, appearing in the growth medium during the phase of cell lysis. Exoglucanase activity was highest in the culture filtrate, with slight activity in the cell fractions, while endoglucanase was associated only with the mycelium. No desorbable exoglucanase nor endoglucanase activity could be released by sonication of residual cellulose particles removed from actively growing cultures. β-Glucosidase activity was located only in the cell-associated fractions during active growth. All enzymes had optimal activity at 50 °C; in the particulate fraction β-glucosidase exhibited a second optimum at 30 °C. In the filtrate, soluble intracellular and particulate fractions optimal exoglucanase activity occurred at pH 6.4, 7.0, and 5.8, respectively. Endoglucanase activity was optimal at pH 5.8 in the soluble cell fraction, and at pH 5.4 in the particulate fraction.

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