Topic
Trichoderma reesei
About: Trichoderma reesei is a research topic. Over the lifetime, 3832 publications have been published within this topic receiving 152877 citations. The topic is also known as: Trichoderma reesi.
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TL;DR: This chapter presents method that is reproducible and no synergy or cooperation between the different enzymes exists, and the extracellular enzyme product is partially purified, concentrated, and stabilized.
Abstract: Publisher Summary Trichoderma reesei QM6a and a mutant from this strain produce very effective cellulases. The protein exocellobiohydrolas (CBH 1) is the most abundant of the enzymes from Trichoderma reesei . Trichoderma reesei also produces cellobiase activity. In the product Celluclast, this activity is very low and the addition of Aspergillus niger cellobiase is recommended for total saccharification of cellulose. The enzyme complex is commercially available from different companies. It is produced by a selected strain of Trichoderma reesei that is grown under optimum submerged fermentation conditions for production of this product. The extracellular enzyme product is partially purified, concentrated, and stabilized. Many different methods have been used to determine cellulolytic activities. This chapter presents method that is reproducible and no synergy or cooperation between the different enzymes exists.
100 citations
TL;DR: The use of a fed-batch cultivation of the fungus Trichoderma reesei allows cellulase production to occur under optimum conditions, and results in extremely high enzyme titres and productivities, compared with the values obtained in two-stage continuous cultivation.
99 citations
TL;DR: The biological function of the enzymes is discussed, and it is hypothesized that it is homologous to EG III in Trichoderma reesei and the role of the enzyme is to make the cellulose in wood more accessible to other cellulases.
Abstract: A 28-kDa endoglucanase was isolated from the culture filtrate of Phanerochaete chrysosporium strain K3 and named EG 28. It degrades carboxymethylated cellulose and amorphous cellulose, and to a lesser degree xylan and mannan but not microcrystalline cellulose (Avicel). EG 28 is unusual among cellulases from aerobic fungi, in that it appears to lack a cellulose-binding domain and does not bind to crystalline cellulose. The enzyme is efficient at releasing short fibres from filter paper and mechanical pulp, and acts synergistically with cellobiohydrolases. Its mode of degrading filter paper appears to be different to that of endoglucanase I from Trichoderma reesei. Furthermore, EG 28 releases colour from stained cellulose beads faster than any other enzyme tested. Peptide mapping suggests that it is not a fragment of another known endoglucanases from P. chrysosporium and peptide sequences indicate that it belongs to family 12 of the glycosyl hydrolases. EG 28 is glycosylated. The biological function of the enzyme is discussed, and it is hypothesized that it is homologous to EG III in Trichoderma reesei and the role of the enzyme is to make the cellulose in wood more accessible to other cellulases.
99 citations
TL;DR: Inactivation of the cellulase of Trichoderma reesei by shear, is of sufficient magnitude to merit consideration in the design of equipment for the enzymatic hydrolysis of cellulose, and the inac inactivation constant is a function of the flow rate of the enzyme solution through a fine capillary tube.
99 citations
TL;DR: A 3.43-fold synergistic effect by combining this beta-glucosidase with Trichoderma reesei cellulases was observed, indicating this enzyme could potentially be used for improving the efficiency of cellulosic bioconversion.
99 citations