Purification and Characterization of two Extracellular β-Glucosidases from Trichoderma viride ITCC 1433

✍ Scribed by M. Wilhelm; H. Sahm

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 464 KB
• Volume: 6
• Category: Article
• ISSN: 0138-4988
• DOI: 10.1002/abio.370060203

✦ Synopsis

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), mol. weight 70000 d, is unglycosylated and neutral (pH = 7.2). Both proteins form a two-step system where P-glucosidase A is active a t low substrate concentrations (KSlf = 2.3 x M cellobiose) while P-glucosidase B covers the range of 10-fold higher cellobiose concentrations (KJf = 1.8

x 31). The enzymes are fiiirly stable with a residual activity of 70% a t 50°C after 24 h.