Published 1974
.
Written in English
Edition Notes
| Statement | by Aldons Jekabs Lusis. |
| The Physical Object | |
|---|---|
| Pagination | [11], 92 leaves, bound : |
| Number of Pages | 92 |
| ID Numbers | |
| Open Library | OL14239808M |
Chaetomium thermophile contains three distinct β-glucosidases. Two of the enzymes are cell bound while the third is extracellular. On the basis of rel Cited by: Chaetomium thermophile contains three distinct β-glucosidases. Two of the enzymes are cell bound while the third is extracellular. On the basis of relative substrate specificities toward p- nitrophenyl -β- d -glucoside and cellobiose, one of the cell-bound enzymes is classified as a cellobiase while the other two enzymes are classified as aryl-β- d by: Abstract Graduation date: The thermophilic fungus Chaetomium thermophile was shown to contain three major β-glucosidases, a cell-bound cellobiase, a cellbound aryl-β-glucosidase and an extracellular aryl-β-glucosidase. Here, the crystal structure of a family GH3 β-glucosidase from the thermophilic fungus Chaetomium thermophilum (Ct BGL) was determined at a resolution of Å. The structure showed the three-domain architecture found in other β-glucosidases .
The thermophilic fungus Chaetomium thermophilum var. coprophilum produced large amounts of extracellular and intracellular beta-glucosidase activity when grown on cellulose or cellobiose as . Thermophilic Chaetomium (Chaetomium thermophilum) is one of the most extreme eukaryotic thermophiles that has revolutionized the biotechnological production of versatile enzymes with . Lusis, A.D. and Becker, R.R. () The β-glucosidase system of the thermophilic fungus Chaetomium thermophile var. coprophile N. var. Biochim. Biophys. Acta , 5– PubMed . Laccase from culture filtrates of a thermophilic fungus reported as Chaetomium thermophilium was purified by ultrafiltration, anion-exchange chromatography, and affinity chromatography. The enzyme was a glycoprotein of 77 kDa.
Chaetomium thermophile contains three distinct β-glucosidases. Two of the enzymes are cell bound while the third is extracellular. The aim of the present investigation was to study the /3-glucosidase system of Sporotrichum thermophile for its possible implications in cellulolysis. As will be shown, no evidence was found for a mul- tiple /3-glucosidase system in this fungus. Abstract Multiple forms of beta-glucosidase (EC ) of Sporotrichum thermophile were produced when the fungus was grown in a cellulose medium. One beta-glucosidase was purified . (endo-1,4-D-glucanase,EC ) was produced from a thermostable fungus Chaetomium thermophile. It was grownon Vogel's medium with different carbon sources like xylan, .
