The effect of pH on glucoamylase production, glycosylation and chemostat evolution of Aspergillus niger
โ Scribed by Gregg L.F Wallis; Richard J Swift; Robert Atterbury; Susanne Trappe; Ursula Rinas; Frank W Hemming; Marilyn G Wiebe; Anthony P.J Trinci; John F Peberdy
- Book ID
- 117480814
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 402 KB
- Volume
- 1527
- Category
- Article
- ISSN
- 0304-4165
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
When grown on a medium containing 5 g maltodextrin L -1 , Aspergillus niger transformant N402[pAB6-10]B1, which has an additional 20 copies of the glucoamylase (glaA) gene, produced 320 ยฑ 8 mg (mean ยฑ S.E.) glucoamylase (GAM) L -1 in batch culture and 373 ยฑ 9 mg GAM L -1 in maltodextrin-limited chem
A comparative structure-function study was performed to establish possible roles of carbohydrates in stabilization of glycoproteins, using glucoamylase (GA) as a model system. In addition to kinetic properties, stability toward elevated temperatures, extremes of pH, high salt concentrations together
Fungal cellulases are well-studied enzymes and are used in various industrial processes. Much of the knowledge of enzymatic depolymerization of cellulosic material has come from Trichoderma cellulase system. Species of Trichoderma can produce substantial amounts of endoglucanase and exoglucanase but
The response of steady state chemostat cultures of a recombinant Aspergillus niger (B1-D), secreting both a heterologous enzyme (Hen Egg White Lysozyme [HEWL]) and a native enzyme (Glucoamylase), to varying levels of O 2 enrichment of the process gas was evaluated. Formation of both the native and t