Purification and properties of an extracellular proteinase of Trichoderma koningii
โ Scribed by H.K. Manonmani; Richard Joseph
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 338 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0141-0229
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๐ SIMILAR VOLUMES
## Sumiiiary T. viride ITCC 1433 synthesizes a two component system for the hydrolysis of cellobiose and cellooligodextrins. 80% of the total activity are solubilized during growth. The large protein (A), mol. weight 98000 d, is glycosylated and slightly acidic (pH = 6.1). The smaller protein (B),
P-Glucosidase (BG) is a hydrolytic enzyme which acts on various compounds with p-D-glucosidic linkages. It has been shown to play a key role in the cellulase complex of T. reesei by hydrolyzing cellobiose to glucose.' Numerous methods have been employed to purify P-glucosidase from \* To whom all co