Browsing by Subject "serpiinit"

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  • Riuttala, Mari (Helsingin yliopisto, 2015)
    In humans, various allergies and intolerances have increased in recent years. Many people think that they have a variety of symptoms from eating grain products. Cereal protease inhibitors are believed to be possibly one of the factors that can cause these reactions. The aim of the experimental part of the study was to isolate serine peptidase inhibitors serpins from barley and study different hydrolysis to it. Serpins are very stable at hydrolyse. The literature review deals characteristics of serine protease inhibitors serpins and other allergens from cereals. And examine the celiac harmful proteins and their cleavage, gluten sensitivity and celiac disease. Cereals proteins can trigger variety hypersensitivity or immunological symptoms for humans. Many of cereal inhibitor proteins are allergens and storage proteins prolamins cause immunological inflammation in the coeliac patient’s intestines. Cereal serpins are very strong binding inhibitors that behave like substrates and reactive centre cleaved during inhibition. After serpins reactive centre degraded, they become very stable to heat and subsequent degradation. Serpins are almost the only protein in beer. It remains hydrolysed and undenatured through the malting and brewing process. The aim of this study was to isolate serpins from barley and eliminate them from gluten-free beer using the Aspergillus niger- fungus produced prolyl endopeptidase AN-PEP, Tritirachium album- fungus produced serine endopeptidase Protease K and hydrogen peroxide oxidation. Serpin cleavage was monitored by SDS-gel electrophoresis and size exclusion chromatography (SEC). In this study, it was shown that AN-PEP and protease K made it possible to degrade serpins from gluten-free beer. Serpins from gluten-free beer did not degrade with oxidation. AN-PEP makes it possible to eliminate the majority of beer serpins. AN-PEP can be used to make beer suitable for allergy sufferers in the future.