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PubMed1976

Production of cellulase by Trichoderma.

The cellulase complex in T. viride is inducible. For large-scale enzyme production the fungus should be cultured on media containing cellulose. The cellulase enzymes are respressible. To produce and maintain best cellulase yields cultural conditions which lead to carbohydrate consumption in excess of cellular needs should be avoided. With the present mutant (QM9414) extracellular enzyme preparations having 1.6 FP units/ml and 1.6 mg protein/ml have been obtained within four to five days in submerged fermentation. Such preparations are capable of producing a 5% sugar solution when mixed with 10% ball milled cellulose and incubated 24 hr at 50 degrees C. Further improvements of cellulase yields are being sought by continued mutagenesis and increased nutrient levels in the growth medium.

Amylases↗

PubMed2006

[Spectroscopy study of the immobilized cellulase of magnetic nanoparticles Fe3O4].

Fe3O4 magnetic nanoparticles were synthesized by chemical coprecipitation method using ammonia as the precipitator in the present paper. And then cellulase was immobilized on Fe3O4 magnetic nanoparticles via carbodiimide activation, which was testified by FTIR and lots of repeating catalysis experiments. The morphology of nanoparticles immobilized by cellulase was characterized by TEM, and the activity of cellulase was measured by DNS spectrophotometry. The optimum temperature (60 degrees C) and pH value (3.94-5.50) for the catalysis ablility of immobilized cellulose were studied. The result showed that compared with the native enzyme the cellulase immobilized on Fe3O4 magnetic nanoparticles has the advantages of thermal stability, storage stability, and more extensive optimum pH value.

Cellulase↗

PubMed1987

[Isolation of a cellulase hyperproducer Trichoderma pseudokoningii mutant].

The present study describes the production of cellulases by a native strain of Trichoderma pseudokoningii in the presence and absence of a catabolic repressor. We report a plate assay for selecting fungal mutants capable of synthesizing the cellulase enzymes under conditions of catabolite repression. This method was used for the selection of catabolite repression-resistant mutants. One mutant, B-1, secreted 3.3 times the extracellular protein and 3 times the endoglucanase and filter paper activity in submerged cultures when compared with the wild type strain. The cellobiase activity remained at similar levels in both strains. Although this mutant was isolated as i cellulase producer in the presence of 500 mM glycerol on agar plates, in liquid medium containing the repressor B-1 it exhibits only partial derepression of the cellulase complex.

Cellobiose↗

PubMed1982

[Non-steady state kinetics for action of a multienzyme cellulase system toward insoluble cellulose].

A kinetic theory for multienzyme cellulase systems in non-steady state conditions (in relation to intermediate metabolites) of hydrolysis of insoluble cellulose has been developed. To verify the kinetic regularities obtained the action of 12 different cellulases from the fungi Trichoderma, Geotrichum and Aspergillus as well as from bacterial cells Thermomonospora sp. and Rapidase preparation has been studied with respect to ball milled cotton linters and microcrystalline cellulose. The experimental data were discussed in the framework of mechanism of enzymatic hydrolysis of cellulose suggest by us recently and the main routes for glucose and cellobiose formation from insoluble cellulose have been elucidated. The effects of concentrations of cellulase preparations and the initial substrate on (i) time lags for glucose formation, (ii) stationary rate of glucose formation, and (iii) kinetics of cellulose conversion to glucose at low and high conversion degrees, were studied. A theoretical analysis of maxima and inflection points on the kinetic curves for intermediates (oligosaccharides and cellobiose) was performed. The effects and intensity of stirring on the time lag values for glucose formation were studied and the relative role of kinetic and diffusional factors in this process was evaluated. The data obtained are unequivocally indicative of the common mechanism of conversion of cellulose to glucose by cellulase complexes irrespective of their source and composition.

Actinomycetales↗

PubMed1981

[Effect of composition of multienzyme cellulase complexes on rate-limiting steps for non-soluble (native) cellulose hydrolysis].

It was shown that the kinetics of multienzyme cellulase complexes are generally characterized by the absence of any single rate-limiting step of hydrolysis, even when the rates of individual steps of the process are substantially different. This peculiarity of the kinetic behaviour of cellulases can be explained in terms of certain "shunt ways" in a series of individual steps of enzymatic degradation of cellulose into glucose. A basic kinetic scheme for the degradation of cellulose was developed and proved experimentally for hydrolysis of milled cotton linters under the action of ten various cellulase complexes from the fungi Trichoderma, Geotrichum and Aspergillus. It was found that the value of the stationary rate of glucose formation in all cases is determined by the effect of two or three cellulolytic components of the complexes. It was concluded that the mechanism of native cellulose hydrolysis is the same for all cellulase complexes under study irrespective of their composition and origin.

Aspergillus niger↗

PubMed1995

A simple and rapid semiquantitative method for measuring cellulase activity in agar media.

A simple and rapid semiquantitative technique for the determination of fungal cellulytic activities in solid (agar slant) media has been developed. This method is a combination of Congo-red staining widely used for qualitative cellulase detection and common cellulase activity tests. Previous investigation on the adsorptive effect of cellulose content of media showed that the real enzyme activity values can be measured with minimum loss by means of agar discs cut from the most active zones of slants visualized by Congo-red staining. Different cellulase activity tests (FPase, CMCase and beta-glucosidase by PNPG-method) of seven cellulolytic fungal strains were investigated by this technique. Data give information on the different enzyme profiles of the species. The method can be regarded as very simple and suitable for simultaneous rapid comparison of cellulase components of greater series of fungal strains from agar slant cultures. It can also be used in the case of fungi unable to grow in liquid cultures.

Agar↗

PubMed1994

Some characteristics and partial purification of the Ganoderma lucidum cellulase system.

The extracellular cellulase system of the white-rotting basidiomycete Ganoderma lucidum was characterised while growing in cellulose-containing shaken liquid culture. The protein content of the culture filtrate reached its maximum after 36 days and cellulase activity at about 60 days. Different cellulase activities (endoglucanase, cellobiohydrolase and beta-glucosidase) were determined in a range of pH extending from 6 to 2. All of the three enzyme activities have at least three peaks between pH 6 and 2, although optimum points of the different enzymes are slightly different, showing that the enzyme complex consists of a number of enzymes and isozymes. Partial purification of the enzyme complex was carried out by DEAE-cellulose column chromatography. Using 0-3 M linear urea gradient, protein was eluted in one sharp peak corresponding mainly to beta-glucosidase activity. Comparing crude extracellular protein with that of purified by the column using PAGE indicated that this method was suitable for the separation and partial purification of one type of Ganoderma cellulases.

Basidiomycota↗

PubMed1993

Triggering of cellulase biosynthesis by cellulose in Trichoderma reesei. Involvement of a constitutive, sophorose-inducible, glucose-inhibited beta-diglucoside permease.

We prepared [U-14C]cellobiose by cultivating Acetobacter pasteurianus in the presence of [U-14C]glucose and hydrolyzing the [U-14C]cellulose formed with beta-glucosidase-free cellulase from Trichoderma reesei. This 14C-labeled cellobiose was used to investigate the presence of an uptake system for cellobiose in T. reesei. Evidence was obtained for the presence of a high affinity (Km for cellobiose 0.3 microM) but low activity (2.5 milliunits/mg fungal dry weight) cellobiose permease. The permease is formed constitutively, but higher levels are formed after addition of sophorose (glucosyl-beta-1,2-diglucoside), a reputed cellulase inducer. The permease appears to be specific for beta-diglucosides, as the uptake of [U-14C]cellobiose is inhibited by sophorose, gentiobiose (glucosyl-beta-1,3-glucoside), and cellobiose. Under these conditions, cellooligodextrines (n, 4-7; final concentration, 1 mM) are not inhibitors. Glucose, but no other monosaccharides, inhibits the permease. The hypersecretory mutant T. reesei RUT C-30 exhibits elevated permease activities, whereas in T. reesei QM 9979, a mutant strain defective in the induction of cellulases by cellulose or sophorose, strongly reduced permease activities were demonstrated. The results stress a hitherto not recognized point of control in the induction of cellulases by T. reesei at the level of uptake of cellulose oligosaccharides.

Cellulase↗

PubMed1998

Factorial optimization of a six-cellulase mixture

A factorial experimental design approach was used to optimize mixtures of six cellulases (five Thermomonospora fusca cellulases and plus/minus Trichoderma reesei CBHI along with beta-glucosidase) so as to maximize the glucose produced from filter paper. Optimized mixture A and mixture B produced glucose at 25 and 8.3 μmol glucose/μmol enzyme/min, respectively, which are 8 and 1.5 times higher than the sum of the activity of the individual cellulases. In both mixtures, the glucose yield depended on the ratio and the cellulases used. Most enzymes showed synergistic interactions that increased the glucose yield. The yield of glucose with the optimum mixtures depended on the total enzyme concentration. Copyright 1998 John Wiley & Sons, Inc.

Journal Article↗

PubMed2001

Animal cellulases.

Previous dogma has maintained that cellulose, ingested by xylophagous or herbivorous animals, is digested by cellulolytic symbiotes. The first evidence in conflict with this contention involved the demonstration of cellulolytic activities in symbiote-free secreting organs (e.g., the salivary glands of termites) or defaunated guts. Following these demonstrations, possible endogenous cellulase components were purified from several cellulose-digesting invertebrates, but this research did little to change the general view concerning animal cellulose digestion. Thanks to recent developments in molecular biology, the existence of cellulases of animal origin has been firmly established. To date, cellulase genes have been reported from arthropods (insects and a crayfish) and nematodes. This paper describes and discusses the presence and nature of endogenous cellulases in higher animals.

Amino Acid Sequence↗

PubMed2001

Stabilization of Penicillium occitanis cellulases by spray drying in presence of Maltodextrin.

The stabilization of fungal cellulases by spray drying, the thermal stability of Penicillium occitanis cellulases and the effect of some additives were studied. We observed that CMCase activity presents a good stability at 50 degrees C, even after 60 h of incubation. On the other hand, beta-glucosidase activity was more sensitive (loss of 50%) and reacts on total cellulases activities (Filter paper activities). The addition of hydrophilic agents such as ethylene glycol, polyethylene glycol (PEG6000) enhanced enzyme activity. The effect of PEG and Maltodextrin, another water activity decreasing agent, were then tested during the spray drying of Pol6 cellulases. The presence of 1% PEG allowed the best recovery but had a negative effect on enzyme stability while 1% Maltodextrin showed a negative effect on enzyme recovery but a very positive effect on enzyme stabilization.

Journal Article↗

PubMed1999

Occurrence of neutral and alkaline cellulases among alkali-tolerant micromycetes

600 different natural strains of alkali-tolerant micromycetes belonging to 4 classes, 38 genera and 119 species were tested on their ability to produce neutral and alkaline cellulases. Frequency of occurrence of neutral and alkaline cellulases producers among the studied strains was estimated. It is concluded that 72% of all tested strains produce cellulases at neutral and alkaline pH values. But the largest number of neutral and alkaline cellulases producers belong to the following classes which are tolerant to extreme environmental factors: namely Hyphomycetes (genera Acremonium, Alternaria, Cylindrocarpon, Fuzarium, Penicillium, Verticillium, Myrothecium, Ulocladium, Gliocladium), Ascomycetes (genus Chaetomium) and Coelomycetes (genera Phoma, Microsphaeropsis, Aposphaeria).

Journal Article↗

PubMed2000

Cellulases and related enzymes in biotechnology.

Basic and applied research on microbial cellulases, hemicellulases and pectinases has not only generated significant scientific knowledge but has also revealed their enormous potential in biotechnology. At present, cellulases and related enzymes are used in food, brewery and wine, animal feed, textile and laundry, pulp and paper industries, as well as in agriculture and for research purposes. Indeed, the demand for these enzymes is growing more rapidly than ever before, and this demand has become the driving force for research on cellulases and related enzymes. The present article is an overview of the biotechnological state-of-the-art for cellulases and related enzymes.

Journal Article↗

PubMed1999

Improvements in the hygroscopic properties of cotton cellulose by treatment with an endo-type cellulase from Streptomyces sp. KSM-26.

The effect of enzymatic cellulolysis on the moisture-adsorbing properties of cotton cellulose was investigated, using a highly purified endo-type cellulase from Streptomyces sp. KSM-26. The time course of changes in the hygroscopicity of cotton reflected the time course of changes in the extent of the amorphous state of cotton, which was estimated from the amount of water that could bind to cotton, as determined by differential scanning calorimetry, during the hydrolytic process. The endo-type cellulase increased the degree of freedom of cellulose chains in the amorphous regions of cotton at the initial stage of the hydrolytic reaction, leading to major improvements in the moisture-adsorbing properties of cotton. The cellulase then caused the rapid decrease in the size of the amorphous regions with the release of reducing sugars as endo-cleavages in the amorphous regions increased, which reduced the hygroscopicity. The decrease in the hygroscopicity of cotton during enzymatic hydrolysis was followed by a second increase, as the cotton became more amorphous as a consequence of further hydrolysis of the crystalline regions of cotton. The effect of cellulase on the apparent degree of polymerization and the physical strength of cotton became detectable at the later stage of cellulolysis.

Journal Article↗

PubMed1999

Purification, characterization and gene analysis of exo-cellulase II (Ex-2) from the white rot basidiomycete Irpex lacteus.

A new exo-type cellulase, named exo-cellulase II (Ex-2), was purified from the crude enzyme preparation of Irpex lacteus. Ex-2 was very similar to the previously characterized exo-cellulase I (Ex-1) with respect to enzymatic features such as optimal pH, temperature, heat stability, and catalytic activity. However, Ex-2 exhibited greater pH stability than Ex-1. The molecular mass and carbohydrate content of Ex-2 (56,000, 4.0%) were different from those of Ex-1 (53,000, 2.0%). A cellulase gene (named cel2) encoding both Ex-2 and Ex-1 was isolated from an I. lacteus genomic library. The cel2 gene was found to consist of 1569 bp with an open reading frame encoding 523 amino acids, interrupted by two introns. The deduced amino acid sequences revealed that cel2 ORF has a modular structure consisting of a catalytic domain and a fungal-type cellulose-binding domain (CBD) separated by a serine-rich linker region. The catalytic domain was homologous to those of fungal cellobiohydrolases belonging to family 7 of the glycosyl hydrolases. Northern blot analysis showed that expression of the cel2 gene was induced by various cellulosic substrates and repressed by glucose, fructose, and lactose.

Journal Article↗

PubMed2005

Ancient origin of glycosyl hydrolase family 9 cellulase genes.

While it is widely accepted that most animals (Metazoa) do not have endogenous cellulases, relying instead on intestinal symbionts for cellulose digestion, the glycosyl hydrolase family 9 (GHF9) cellulases found in the genomes of termites, abalone, and sea squirts could be an exception. Using information from expressed sequence tags, we show that GHF9 genes (subgroup E2) are widespread in Metazoa because at least 11 classes in five phyla have expressed GHF9 cellulases. We also demonstrate that eukaryotic GHF9 gene families are ancient, forming distinct monophyletic groups in plants and animals. As several intron positions are also conserved between four metazoan phyla then, contrary to the still widespread belief that cellulases were horizontally transferred to animals relatively recently, GHF9 genes must derive from an ancient ancestor. We also found that sequences isolated from the same animal phylum tend to group together, and in some deuterostomes, GHF9 genes are characterized by substitutions in catalytically important sites. Several paralogous subfamilies of GHF9 can be identified in plants, and genes from primitive species tend to arise basally to angiosperm representatives. In contrast, GHF9 subgroup E2 genes are relatively rare in bacteria.

Amino Acid Sequence↗

PubMed1976

Association of latent cellulase activity with plasma membranes from kidney bean abscission zones.

Membranes isolated from abscission zones of Phaseolus vulgaris L., cv. Red Kidney, contained cellulase activity. This particulate activity was enhanced 10- to 20-fold by treatment with Triton X-100. Sucrose density gradient analyses of cell fractions showed that the membranes with which cellulase was associated had a peak equilibrium density of 1.16 to 1.17 g/cm(3) which coincided with that of ion-activated ATPase, a marker for plasma membranes. The membrane fraction having the highest cellulase activity also contained a high proportion of plasma membranes as shown by electron microscopy of sucrose density gradient fractions after staining by periodic acid-chromic acid-phosphotungstic acid. It was concluded that the particulate cellulase was associated with the plasma membrane.

Journal Article↗

PubMed1979

Postharvest Variation in Cellulase, Polygalacturonase, and Pectinmethylesterase in Avocado (Persea americana Mill, cv. Fuerte) Fruits in Relation to Respiration and Ethylene Production.

Cellulase, polygalacturonase (PG), pectinmethylesterase (PME), respiration, and ethylene production were determined in single "Fuerte" avocado fruits from the day of harvest through the start of fruit breakdown. PME declined from its maximum value at the time of picking to a low level early in the climacteric. PG activity was not detectable in the preclimacteric stage, increased during the climacteric, and continued to increase during the postclimacteric phase to a level three times greater than when the fruit reached the edible soft stage. Cellulase activity was low in the preclimacteric fruit, started to increase just as respiration increased, and reached a level two times greater than at the edible soft stage. Cellulase activity started to increase 3 days before PG activity could be detected. Increased production of ethylene followed the increase in respiration and cellulase activity by about 1.5 days. These results indicate that a close relation exists between the rapid increase in the cell wall-depolymerizing enzymes and the rise in respiration and ethylene production and refocused attention on the role of the cell wall and the associated plasma membrane in the early events of fruit ripening.

Journal Article↗