To the best of our knowledge, this is the first report on thermophilic fungi isolated in Korea. Three species of thermophiles were isolated from compost and were identified as Myriococcum thermophilum, Thermoascus aurantiacus, and Thermomyces lanuginosus. They can grow at temperatures above 50degrees C and produce high levels of cellulolytic and xylanolytic enzymes at high temperatures. Notably, the considerable thermostability of the endo-glucanase produced by T. aurantiacus has made the fungus an attractive source of industrial enzymes.
Cellulase ; Fungi* ; Korea ; Soil* ; Thermoascus

Dissolving pulp consists of high purity cellulose and is widely used to as raw materials for the production of regenerated cellulose fiber, cellulose ester and cellulose ether. The characteristic of dissolving pulp affects greatly the production and processing performance of subsequent products. The α-cellulose content, hemicellulose content, pulp viscosity, ash, transition metal ion content, fiber morphology, molecular weight distribution of cellulose and the reactivity are the important properties. Because of its green, mild and high efficiency, the application of enzymes in improving the properties of dissolving pulp has a promising application prospect and has been researched significantly. In this review, the main properties of dissolving pulp are presented first, followed by a recommendation of the enzymes to improve these properties. The application and current research of cellulase and xylanase in improving the properties of dissolving pulp are emphasized. The main problems and the future research areas in improving the properties of dissolving pulp by enzymes are revealed. Finally, the technology prospects in this field are proposed.
Cellulase ; Molecular Weight ; Viscosity ; Wood

Enzyme activities of Cenococcum geophilum isolates were examined on enzyme-specific solid media. Deoxyribonuclease, phosphatase, and urease were detected in all isolates, whereas cellulase was not detected in any of the isolates. Variations in enzyme activities of amylase, caseinolysis, gelatinase, lipase, and ribonuclease were observed among isolates.
Amylases ; Cellulase ; Gelatinases ; Lipase ; Ribonucleases ; Urease

The morphological optimization of Trichoderma harzianum was carried out using several surfactants to achieve increased cellulase production. Addition of the surfactants to the culture medium successfully modified the fungal morphology from an aggregated form to a dispersed form. Optimization of the fungal morphology increased cellulase activity up to 177%. The morphologically optimized conditions enhanced the accessibility of the fungus to substrates and thus promoted cellulase production.
Cellulase ; Fungi ; Surface-Active Agents ; Trichoderma*

The ability of Ganoderma to produce extracellular enzymes, including beta-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. beta-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for beta-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neo-japonicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.
Amylases ; beta-Glucosidase ; Cellulase ; Cellulases ; Ganoderma ; Oxygenases ; Polygalacturonase ; Reishi

A fungal strain producing a high level of cellulase was selected from 320 fungal isolates and identified as Aspergillus sp. This strain was further improved for cellulase production by sequential treatments by two repeated rounds of gamma-irradiation of Co60, ultraviolet treatment and four repeated rounds of treatment with N-methyl-N'-nitro-N-nitrosoguanidine. The best mutant strain, Aspergillus sp. XTG-4, was selected after screening and the activities of carboxymethyl cellulase, filter paper cellulase and beta-glucosidase of the cellulase were improved by 2.03-, 3.20-, and 1.80-fold, respectively, when compared to the wild type strain. After being subcultured 19 times, the enzyme production of the mutant Aspergillus sp. XTG-4s was stable.
Aspergillus ; beta-Glucosidase ; Cellulase ; Mass Screening ; Methylnitronitrosoguanidine ; Mutagenesis ; Sprains and Strains

Thirty seven species of Fusarium were evaluated for their ability of producing extracellular enzymes using chromogenic medium containing substrates such as starch, cellobiose, CM-cellulose, xylan, and pectin. Among the tested species Fusarium mesoamericanum, F. graminearum, F. asiaticum, and F. acuminatum showed high beta-glucosidase acitivity. Xylanase activity was strongly detected in F. proliferatum and F. oxysporum. Strong pectinase activity was also found in F. oxysporum and F. proliferatum. Amylase activity was apparent in F. oxysporum. No clear activity in cellulase was found from all the Fusarium species tested.
Amylases ; beta-Glucosidase ; Cellobiose ; Cellulase ; Fusarium* ; Polygalacturonase ; Starch

Natural lignocellulosic materials contain cellulose, hemicellulose, and lignin. Cellulose hydrolysis to glucose requires a series of lignocellulases. Recently, the research on the synergistic effect of lignocellulases has become a new research focus. Here, four lignocellulase genes encoding β-glucosidase, endo-1,4-β-glucanase, xylanase and laccase from termite and their endosymbionts were cloned into pETDuet-1 and pRSFDuet-1 and expressed in Escherichia coli. After SDS-PAGE analysis, the corresponding protein bands consistent with the theoretical values were observed and all the proteins showed enzyme activities. We used phosphoric acid swollen cellulose (PASC) as substrate to measure the synergistic effect of crude extracts of co-expressing enzymes and the mixture of single enzyme. The co-expressed enzymes increased the degradation efficiency of PASC by 44% compared with the single enzyme mixture; while the degradation rate increased by 34% and 20%, respectively when using filter paper and corn cob pretreated with phosphoric acid as substrates. The degradation efficiency of the co-expressed enzymes was higher than the total efficiency of the single enzyme mixture.
Animals ; Cellulase ; Cellulose ; Hydrolysis ; Isoptera ; Lignin ; Symbiosis ; beta-Glucosidase

Trichoderma reesei Rut-C30 is widely used in industrial cellulase production, and development of cellulase hyper-producer is of great importance for economic lignocellulosic biorefinery. In this study, T. reesei Rut-C30 was engineered with an artificial zinc finger proteins (AZFPs) library. Two mutants T. reesei M1 and M2 with improved cellulase production were obtained. Compared to the parent strain, the filter paper activity (FPase) of T. reesei M1 and M2 increased 100% and 53%, respectively. In addition, the total amount of extracellular protein from the M1 mutant increased 69%, whereas the endo-β-glucanase (CMCase) activity of the M2 mutant is 64% higher compared to the parental strain. Furthermore, RT-qPCR analysis showed that the major cellulase genes exhibited significantly increased expression in both mutants, but different patterns were observed in the two mutants. On the other hand, the cellulase transcriptional repressor ace1 was down-regulated in both mutants, but the transcription level of the activator xyr1 was only up-regulated in the strain M1. These results demonstrated that different AZFPs exert diverse regulatory mechanisms on cellulase production in T. reesei. Analysis of the target genes of AZFPs from T. reesei M1 and M2 will not only benefit further exploration of the regulatory mechanisms of cellulase biosynthesis in T. reesei, but also enable development of cellulase hyper-producing strains by metabolic engineering.
Cellulase ; Gene Library ; Transcription Factors ; Trichoderma ; Zinc Fingers

In order to learn the enzymatic hydrolysis characteristics of steam-explosion pretreated corn straw by cellulase, the effects of substrate concentration, cellulase concentration and temperature were determined. The kinetics of the hydrolysis reaction could be described with the Michealis-Menten equation, and the hydrolysis reaction obeyed the classical first-order reaction rate in the first three hours. In the condition of 45 degrees C and pH 5.0 and the stirring rate 120 r/min, the Michealis constant (Km) and maximum rate (Vm) for 1.2 FPU/mL of cellulase were 11.71 g/L and 1.5 g/(L x h). The kinetic model, including the parameters such as substrate concentration, enzymatic concentration and temperature, was suit for the hydrolysis reaction under the temperature range from 30 degrees C-50 degrees C.
Catalysis ; Cellulase ; chemistry ; Hydrolysis ; Kinetics ; Plant Stems ; Steam ; Zea mays