Induction and Catabolite Repression of Cellulase Synthesis in the Thermophilic Fungus Sporotrichum thermophile

Canevascini, Giorgio; Coudray, M R; Southgate, Robert; Meier, Hans

doi:10.1099/00221287-110-2-291

Cited by 77 publications

(15 citation statements)

References 34 publications

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“…Secretion of xylanase and cellulases from fungi was induced with degradation substrate of these enzymes, and the production of substrates was regulated by the presence of glucose (Eriksson and Hamp 1978;Canevascini et al 1979;Chow et al 1994;Yagüe et al 1997;Özcan et al 1997). However, the production of enzymes from fungi was not stimulated with the polysaccharide substrates, and their degradation components have no catabolite repression with glucose (data not shown).…”

Section: Discussionmentioning

confidence: 77%

The stimulation of extracellular carbohydrases of edible mushrooms by the hot water-soluble fraction from corn fiber

et al. 2005

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Corn fiber (CNF) is an abundant by-product of the wet corn milling process in the production of cornstarch. We have shown that the hot water-soluble fraction (HWSF) from CNF has a promoting effect on the mycelial growth of various edible mushrooms, including mycorrhizal fungi. To reveal the promoting mechanisms, the effect of CNF-HWSF on the stimulation of extracellular enzymes was examined. The production of extracellular carbohydrases such as amylase, CMCase, and xylanase was markedly enhanced by the addition of low molecular weight fractions (less than MW 500) prepared from CNF-HWSF. The enzymatic stimulation and enhancement of mycelial growth appeared during 3-15 days after inoculation. Furthermore, a fraction of less than MW 500 was separated by gel filtrate chromatography into five fractions (A-E), and the effect of each fraction was investigated. Promoting effects were shown from C and D fractions; mycelial growth and enzyme production of Lentinula edodes were indicated although fraction D has no sugars and amino acids in CNF-HWSF. From these results, the promoting effect of CNF-HWSF seems to be a two-step reaction. The first step could be achieved by rich nutrients such as free amino acids and monosaccharides from CNF-HWSF. The second step (during 3-15 days) is considered to be that the marked promoting effect was caused by the stimulation of extracellular enzymes.

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Section: Discussionmentioning

confidence: 77%

The stimulation of extracellular carbohydrases of edible mushrooms by the hot water-soluble fraction from corn fiber

et al. 2005

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“…The reaction product of this polyol dehydrogenase likely is cellobiitol. This compound has not yet been reported to induce cellulase expression if used as a carbon source (4,38). However, cellobiitol has been shown to inhibit beta-glucosidase in Sporotrichum thermophile (45).…”

Section: Discussionmentioning

confidence: 99%

Dehydrogenase GRD1 Represents a Novel Component of the Cellulase Regulon in Trichoderma reesei (Hypocrea jecorina)

Schuster

Kubicek

Schmoll

2011

Appl Environ Microbiol

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Trichoderma reesei (Hypocrea jecorina) is nowadays the most important industrial producer of cellulase and hemicellulase enzymes, which are used for pretreatment of cellulosic biomass for biofuel production. In this study, we introduce a novel component, GRD1 (glucose-ribitol dehydrogenase 1), which shows enzymatic activity on cellobiose and positively influences cellulase gene transcription, expression, and extracellular endo-1,4-␤-D-glucanase activity. grd1 is differentially transcribed upon growth on cellulose and the induction of cellulase gene expression by sophorose. The transcription of grd1 is coregulated with that of cel7a (cbh1) under inducing conditions. GRD1 is further involved in carbon source utilization on several carbon sources, such as those involved in lactose and D-galactose catabolism, in several cases in a light-dependent manner. We conclude that GRD1 represents a novel enhancer of cellulase gene expression, which by coregulation with the major cellulase may act via optimization of inducing mechanisms.

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“…thermoidea (270), which produced high cellulase and xylanase activities even on hemicellulosic substrates without cellulose. In some strains of S. thermophile, the disaccharides cellobiose and lactose also induced cellulase, although less efficiently (50,189). The time course of the appearance of various cellulase components varied in different species: thus, in H. insolens (271) and T. aurantiacus (138), all three cellulase components appeared simultaneously, while in Chaetomium thermophile var.…”

Section: Cellulasementioning

confidence: 99%

Thermophilic Fungi: Their Physiology and Enzymes

Maheshwari

Bharadwaj

Bhat

2000

Microbiol Mol Biol Rev

648

380

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SUMMARY Thermophilic fungi are a small assemblage in mycota that have a minimum temperature of growth at or above 20°C and a maximum temperature of growth extending up to 60 to 62°C. As the only representatives of eukaryotic organisms that can grow at temperatures above 45°C, the thermophilic fungi are valuable experimental systems for investigations of mechanisms that allow growth at moderately high temperature yet limit their growth beyond 60 to 62°C. Although widespread in terrestrial habitats, they have remained underexplored compared to thermophilic species of eubacteria and archaea. However, thermophilic fungi are potential sources of enzymes with scientific and commercial interests. This review, for the first time, compiles information on the physiology and enzymes of thermophilic fungi. Thermophilic fungi can be grown in minimal media with metabolic rates and growth yields comparable to those of mesophilic fungi. Studies of their growth kinetics, respiration, mixed-substrate utilization, nutrient uptake, and protein breakdown rate have provided some basic information not only on thermophilic fungi but also on filamentous fungi in general. Some species have the ability to grow at ambient temperatures if cultures are initiated with germinated spores or mycelial inoculum or if a nutritionally rich medium is used. Thermophilic fungi have a powerful ability to degrade polysaccharide constituents of biomass. The properties of their enzymes show differences not only among species but also among strains of the same species. Their extracellular enzymes display temperature optima for activity that are close to or above the optimum temperature for the growth of organism and, in general, are more heat stable than those of the mesophilic fungi. Some extracellular enzymes from thermophilic fungi are being produced commercially, and a few others have commercial prospects. Genes of thermophilic fungi encoding lipase, protease, xylanase, and cellulase have been cloned and overexpressed in heterologous fungi, and pure crystalline proteins have been obtained for elucidation of the mechanisms of their intrinsic thermostability and catalysis. By contrast, the thermal stability of the few intracellular enzymes that have been purified is comparable to or, in some cases, lower than that of enzymes from the mesophilic fungi. Although rigorous data are lacking, it appears that eukaryotic thermophily involves several mechanisms of stabilization of enzymes or optimization of their activity, with different mechanisms operating for different enzymes.

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Induction and Catabolite Repression of Cellulase Synthesis in the Thermophilic Fungus Sporotrichum thermophile

Cited by 77 publications

References 34 publications

The stimulation of extracellular carbohydrases of edible mushrooms by the hot water-soluble fraction from corn fiber

The stimulation of extracellular carbohydrases of edible mushrooms by the hot water-soluble fraction from corn fiber

Dehydrogenase GRD1 Represents a Novel Component of the Cellulase Regulon in Trichoderma reesei (Hypocrea jecorina)

Thermophilic Fungi: Their Physiology and Enzymes

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