The unique thermotolerance of hyperthermophiles, suitable as valuable sources of thermostable enzymes, is a result of various minor changes which led to the restriction of protein flexibility and modifications of nucleic acids and membrane lipids. Furthermore, all hyperthermophiles produce a number of heat shock proteins and thermoprotectants. Thermal resistance of these microorganisms is also enhanced by rapid resynthesis of thermolabile compounds and by elimination of such intermediates from cell metabolism.
Commercial processing of starch to mono-and oligosaccharides depends on the availability and properties of the applied enzymes such as -amylase, glucoamylase, -glucosidase and xylose isomerase. Each of these enzymes has a different pH and temperature optimum for use. Therefore starch processing is carried out in the stages of liquefaction, saccharification, and isomerisation. This article discusses the application of thermostable enzymes leading to higher quality products and lower production costs caused by the simplification of the processing.
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.