Raw-starch-digesting activity and kinetic properties of glucoamylases.
نویسندگان
چکیده
منابع مشابه
Thermostable, Raw-Starch-Digesting Amylase from Bacillus stearothermophilus.
An endospore-forming thermophilic bacterium, which produced amylase and was identified as Bacillus stearothermophilus, was isolated from soil. The amylase had an optimum temperature of 70 degrees C and strongly degraded wheat starch granules (93%) and potato starch granules (80%) at 60 degrees C.
متن کاملEfficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum
BACKGROUND Starch is a very abundant and renewable carbohydrate and is an important feedstock for industrial applications. The conventional starch liquefaction and saccharification processes are energy-intensive, complicated, and not environmentally friendly. Raw starch-digesting glucoamylases are capable of directly hydrolyzing raw starch to glucose at low temperatures, which significantly sim...
متن کاملProduction and Characteristics of Raw-Starch-Digesting alpha-Amylase from a Protease-Negative Aspergillus ficum Mutant.
Mutational experiments were carried out to decrease the protease productivity of Aspergillus ficum IFO 4320 by using N-methyl-N'-nitro-N-nitrosoguanidine. A protease-negative mutant, M-33, exhibited higher alpha-amylaseactivity than the parent strain under submerged culture at 30 degrees C for 24 h. About 70% of the total alpha-amylase activity in the M-33 culture filtrate was adsorbed onto sta...
متن کاملImproving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis.
A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65 degrees C, the half-life of this mutant RSDA, which, compared with the wild-type RSDA, lacks amino acids R178 and G179, was increased 20-fold. While the wild type was inactivated completely at pH 3.0, the mutant RSDA still retained 41% of its enzymatic activity. The enhancement of ...
متن کاملStabilization of a raw-starch-digesting amylase by multipoint covalent attachment on glutaraldehyde-activated amberlite beads.
Raw-starch-digesting enzyme (RSDA) was immobilized on Amberlite beads by conjugation of glutaraldehyde/ polyglutaraldehyde (PG)-activated beads or by crosslinking. The effect of immobilization on enzyme stability and catalytic efficiency was evaluated. Immobilization conditions greatly influenced the immobilization efficiency. Optimum pH values shifted from pH 5 to 6 for spontaneous crosslinkin...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of the Japanese Society of Starch Science
سال: 1987
ISSN: 1884-488X,0021-5406
DOI: 10.5458/jag1972.34.98