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Research Conducted by P. Qi and Co-Authors Has Provided New Information about Enzymes and Coenzymes

June 3, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Enzymes and Coenzymes. According to news reporting from Blacksburg, Virginia, by NewsRx journalists, research stated, "Synthetic amylose could be a very important compound as a precursor of low-oxygen diffusion biodegradable plastic films, a healthy food additive, and a potential high-density hydrogen carrier. In this study, one-pot reactions composed of sucrose phosphorylase and potato alpha-glucan phosphorylase or supplemented with the three other enzymes (i.e., glucose isomerase, glucose oxidase, and catalase) were carried out to convert cheap sucrose to synthetic amylose, whereas one glucose unit from sucrose was added into the nonreducing end of the primer maltodextrin."

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, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; ACS Catalysis - www.pubs.acs.org/journal/accacs)

Our news journalists report that additional information may be obtained by contacting P. Qi, Cell Free Bioinnovat Inc, Blacksburg, VA 24060, United States. Additional authors for this research include C. You and Y.H.P. Zhang (see also Enzymes and Coenzymes).

Keywords for this news article include: Virginia, Blacksburg, United States, Enzymes and Coenzymes, North and Central America

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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