Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
نویسندگان
چکیده
منابع مشابه
Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain
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 a...
متن کاملPurification and Characterization of Extracellular, Polyextremophilic α-amylase Obtained from Halophilic Engyodontium album
Background: a-Amylases (EC 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries. Objectives: The first ever detailed characterization of amylase from any halophilic Engyodontium album is presented. Materials and Methods: An extracellular α-amylase was studied from halophilic E. album TISTR 3645. The enzyme was e...
متن کاملPurification and characterization of an acidic, thermophilic phytase from a newly isolated Geobacillus stearothermophilus strain DM12
Microbial phytases were applied mainly to animal and human foodstuffs in order to improvemineral bioavailability and food processing. In addition, phytases have potentialbiotechnological application in various other fields, such as environmental protection,aquaculture and agriculture. Bacillus sp. DM12, an isolate from a hot spring, produces phytase,which catalyzes the hydrolysis of phytic acid...
متن کاملPurification and Characterization of Thermostable and Detergent-Stable α-Amylase from Anoxybacillus sp. AH1.
A thermostable and detergent-stable α-amylase from a newly isolated Anoxybacillus sp. AH1 was purified and characterized. Maximum enzyme production (1874.8 U/mL) was obtained at 24 h of incubation. The amylase was purified by using Sephadex G-75 gel filtration, after which an 18-fold increase in specific activity and a yield of 9% were achieved. The molecular mass of the purified enzyme was est...
متن کاملpurification and characterization of extracellular, polyextremophilic α-amylase obtained from halophilic engyodontium album
background: a-amylases (ec 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries.objectives: the first ever detailed characterization of amylase from any halophilic engyodontium album is presented. materials and methods: an extracellular α-amylase was studied from halophilic e. album tistr 3645. the enzyme was ext...
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: Brazilian Archives of Biology and Technology
سال: 2016
ISSN: 1678-4324,1516-8913
DOI: 10.1590/1678-4324-2016160346