Solid Phase Extraction (SPE)
Scientists review enzymes for industrial prebiotic applications
May 19 2011
The study, published in Biotechnology for Biofuels, stated that a prerequisite to these applications is normally high-level expression of enzymes in recombinant hosts.
During hydrolysis of lignocellulosic materials, thermostable enzymes reduce the amount of enzyme needed due to higher specific activity and become more stable, lengthening the hydrolysis time.
The main aim of the study was to study enzymes and substrates to compare the properties of two thermostable recombinant glycosyl hydrolase families 10 and 11 (GH10 and GH11) xylanases, with a view towards their potential applications.
They found that T.aurantiacus xylanase was ideal for applications involving total hydrolysis of lignocellulosic materials for platform sugars due to its high catalytic activity and good thermostability.
N. flexuosa xylanase, meanwhile, was found to have a much greater potential for the production of xylooligosaccharides.
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