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Molecular Cloning and Characterization of a Thermostable α-Amylase Exhibiting an Unusually High Activity
| Content Provider | Semantic Scholar |
|---|---|
| Author | Park, Jongtae Suwanto, Antonius Tan, Irawan Nuryanto, Tommy Lukman, Rudy Wang, Kan Jane, Jay-Lin |
| Copyright Year | 2013 |
| Abstract | An α-amylase gene was cloned from the thermophilic bacterium Bacillus subtilis isolated from Indonesian oil palm shell waste. The gene expressed an extracellular enzyme. Optimal hydrolysis conditions for the enzyme were 70C and pH 6.0. The specific activity of the enzyme was 16.0 kU per mg of protein, which was higher than for other thermostable amylases. Hydrolytic products of the enzyme using starch and glycogen were mainly maltohexaose and maltopentaose. The enzyme had a Km value of 0.099 mg/mL for amylopectin, more than 10 times lower than for amylose. The catalytic efficiency of the enzyme using amylopectin was 39,200 mL/mg·s and was 3,270 mL/mg·s using amylose. The enzyme liquefied corn starch at pH 5.0, which was successfully converted to glucose using commercial glucoamylase and pullulanase without pH adjustment. The enzyme has advantages for industrial applications. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://agron-www.agron.iastate.edu/ptf/publications/2-JT%20Park%20et%20al%20Food%20Sci%20Biotechnol%202014.pdf |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Amylopectin Amylose Clone Cells Cloning, Molecular Exhibits as Topic Glucan 1,4-alpha-Glucosidase Glucose Greater Than Starch |
| Content Type | Text |
| Resource Type | Article |
