PURIFICATION AND CHARACTERIZATION OF A GLUCOAMYLASE FROM HUMICOLA-GRISEA

Authors
CAMPOS L FELIX CR
Citation
L. Campos et Cr. Felix, PURIFICATION AND CHARACTERIZATION OF A GLUCOAMYLASE FROM HUMICOLA-GRISEA, Applied and environmental microbiology, 61(6), 1995, pp. 2436-2438
Citations number
30
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
Journal title
Applied and environmental microbiology → ACNP
ISSN journal
00992240
Volume
61
Issue
6
Year of publication
1995
Pages
2436 - 2438
Database
ISI
SICI code
0099-2240(1995)61:6<2436:PACOAG>2.0.ZU;2-I
Abstract
A thermostable extracellular glucoamylase from the thermophilic fungus Humicola grisea was purified to homogeneity. Its molecular mass and i soelectric point were 74 kDa and 8.4, respectively. The enzyme contain ed 5% carbohydrate, showed maximal activities at pH 6.0 and 60 degrees C, and was stable at 55 degrees C and pH 6.0 for 2 h. The K-m of solu ble starch hydrolysis at 50 degrees C and pH 6.0 was 0.14 mg/ml. The p urified enzyme was remarkably insensitive to glucose.