Journal
CATALYSIS LETTERS
Volume 148, Issue 9, Pages 2665-2674Publisher
SPRINGER
DOI: 10.1007/s10562-018-2493-2
Keywords
Amylase; Haloalkaliphilic; Thermophilic; Entrapment; Wadi An Natrun
Categories
Funding
- US-Egypt Science and Technology Joint Fund
- Suez Canal University (Egypt) [1841]
- University of Georgia (USA) [NSF-OISE-1132412]
Ask authors/readers for more resources
An extremophilic amylase from Alkalilimnicola sp. NM-DCM-1 was expressed and purified. The amylase, AmyD8, was extremophilic, with maximal activity at 55 A degrees C, pH 10.5 and 2.4 M NaCl. AmyD8 had a broad substrate utilization spectrum, hydrolyzing branched and linear substrates. AmyD8 was stable and active in nonionic and anionic surfactants. AmyD8 was organic solvent resistant, retaining activity after incubation in benzene, methanol, ethanol and isopropanol. AmyD8 was entrapped in an agar-agar matrix with 89% entrapment yield and no loss in relative activity. Entrapped AmyD8 retained its extremophilic properties. Entrapment enhanced AmyD8's thermal stability, the half-life of the entrapped enzyme nearly doubled after incubation at 50-65 A degrees C. Entrapped AmyD8 had excellent recyclability, retaining 58% of initial activity after 16 hydrolysis cycles. These extreme properties give AmyD8 great economic feasibility. [GRAPHICS] .
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available