The news correspondents obtained a quote from the research, "A thermostable sucrose phosphorylase was cloned from a thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum JW/SL-YS485. The values of k(cat) and K-m on sucrose were 15.1 s(-1) and 20.2 mM, respectively, at 37 degrees C. The half-life time of this enzyme was 3.1 h at 70 degrees C. The yield of synthetic amylose was not significantly improved when glucose isomerase, glucose oxidase, and catalase were used to remove fructose, which was an inhibitor to sucrose phosphorylase. This result suggested that the two-enzyme system equipped with the sucrose phosphorylase with a high value of fructose dissociation constant (34.4 mM) did not require the three other enzymes to mitigate product inhibition."
According to the news reporters, the research concluded: "The number-average degree of polymerization of synthetic amylose was controlled from 33 to 262 by adjusting primer maltodextrin concentration and reaction time."
For more information on this research see: One-Pot Enzymatic Conversion of Sucrose to Synthetic Amy lose by using Enzyme Cascades. ACS Catalysis, 2014;4(5):1311-1317. ACS Catalysis can be contacted at: Amer Chemical Soc,
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