@misc{Żelazko_Monika_Pancreatic_2007,
 author={Żelazko, Monika and Chrzanowska, Józefa and Polanowski, Antoni},
 volume={76},
 number={1},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.76, 1 (2007)-.},
 howpublished={online},
 year={2007},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Pancreatic proteinases like trypsin, chymotrypsin and elastase are the main enzymes responsible for digestion of food proteins. In recent years, wide biochemical diversity and functional individualism of those enzymes in variety species have been affirmed. Abundance of catalytical forms as well as isoforms has been described for trypsin, chymotrypsin and elastase. They have been distinguished in e.g. amino acids composition, pi value or stability. Each form reveals individual biochemical feature like e.g. catalytical efficiency, substrate affinity or distinct interactions with protein inhibitors. The consequence can be both different sensitivity to antynutritional factors and variable properties of enzyme preparations obtained from pancreases.},
 title={Pancreatic proteinases - species diversity and the appending feeding and biotechnological implications},
 type={Text},
 URL={http://rcin.org.pl./Content/87156/PDF/POZN271_113554_biotechnologia-2007-no1-zelazko.pdf},
 keywords={biotechnology},
}