Abstract
Amylolytic enzymes are only slightly inhibited by thermal treated α-glucans (10–15%). The addition of glycine to the thermolysis mixture produces no increase of the inhibition. The inhibition of the enzyme activity is probably caused by short-chain α-glucans that the secondary binding places of the active centre coat and therefore the hydrolysis is reduced. Glucoamylase and α-amylase are not inhibited by non-dialysed melanoidines from the reaction of D-glucose and glycine, but there is a strong inhibition of α-glucosidase by these melanoidines (up to 45%). Strongly coloured, low molecular compounds that are formed during the Maillard-reaction and are soluble in ethyl acetate cause no inhibition of Glucoamylase and α-amylase.
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Schumacher, D., Hirsch, D., Cämmerer, B. et al. Untersuchungen zum Abbau von Maillard-Reaktionsprodukten durch amylolytische Enzyme. Z Lebensm Unters Forch 203, 391–394 (1996). https://doi.org/10.1007/BF01231080
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DOI: https://doi.org/10.1007/BF01231080