Mixed-mode resins: taking shortcut in downstream processing of raw-starch digesting α-amylases
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.
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BACKGROUND Starch is one of the most abundant organic polysaccharides available for the production of bio-ethanol as an alternative transport fuel. Cost-effective utilisation of starch requires consolidated bioprocessing (CBP) where a single microorganism can produce the enzymes required for hydrolysis of starch, and also convert the glucose monomers to ethanol. RESULTS The Aspergillus tubing...
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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 ...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2015
ISSN: 2045-2322
DOI: 10.1038/srep15772