Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
Braz. arch. biol. technol
; Braz. arch. biol. technol;59: e16160346, 2016. tab, graf
Article
in En
| LILACS
| ID: biblio-951342
Responsible library:
BR1.1
ABSTRACT
ABSTRACT α-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 °C and pH 5.5-10.5. A4 amylase was extremely stable at +4 °C, and the enzyme retained over 65% of its original α-amylase activity at 70 °C and 43% at 90 °C. The enzyme's Km values for soluble starch, amylopectin and amylose substrates were obtained as 0.9, 1.3 and 0.5 mg/mL, respectively. EDTA, Hg2+, B4O7 2-, OH-, CN- , and urea exhibited different inhibition effects; their IC50 values were identified as 8.0, 5.75, 16.5, 15.2, 8.2 and 10.9 mM, respectively. A4 amylase exhibited extreme stability toward some surfactants and perfect match for a wide variety of commercial solid and liquid detergents at 55 °C. So, it may be considered to be potential applications for detergent and other industrial uses.
Full text:
1
Collection:
01-internacional
Database:
LILACS
Language:
En
Journal:
Braz. arch. biol. technol
Journal subject:
BIOLOGIA
Year:
2016
Document type:
Article
Affiliation country:
Turkey
Country of publication:
Brazil