@misc{Sinkiewicz_Izabela_Evaluation_2009,
 author={Sinkiewicz, Izabela and Synowiecki, Józef},
 volume={85},
 number={2},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.85, 2 (2009)-.},
 howpublished={online},
 year={2009},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Thermus ruber produces a-glucosidase detected in the crude extract of cell proteins. This enzyme exhibits optimum activity at 65°C and pH 6,0. The enzyme was stable within a range of pH 5.5 to 8.0 and in 65°C for 60 min. The rate of p-nitrophenol-a-D-glucopyranoside cleavage was higher than that for maltose. With maltotetraose, maltopentaose and maltohexaose, the hydrolysis rate decreased with increasing the molecular weight of the substrate. Our data suggest that the starch converting process could be improved using a-glucosidase from Thermus ruber.},
 title={Evaluation of Thermus ruher as a source of thermostable a-glucosidase useful for production of glucose syrups},
 type={Text},
 URL={http://rcin.org.pl/Content/72129/PDF/POZN271_94533_biotechnologia-2009-no2-sinkiewicz.pdf},
 keywords={biotechnology},
}