Extraction, purification and some partial characterization of alpha-amylase inhibitors from wheat Iapar 28-Igapó.
alpha-Amylase inhibitors from wheat (Triticum aestivum) cultivar Iapar 28-Igapó were extracted with water in a 1:10 (w:v) ratio and precipitated with ammonium sulfate between 20-50% saturation, followed by DEAE and CM-cellulose chromatography. One inhibitor was purified and designated as CMC-IB, and had electrophoretic mobilities of 0.23 and 0.54 in alkaline and acidic conditions, respectively. This inhibitor was 750 times more active on human salivary alpha-amylase (HSSA) than porcine pancreatic o-amylase (PPA). The preincubation time required for maximum complexation with HSA was 20 minutes and optimum pH of inhibition was 7.5. The inhibitor CMC-IB was stable at 0 degrees C and maintained 50% of inhibitory activity against HSA, when incubated at 98 degrees C for one hour.
Kondo
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NK
Depto. de Química, Universidade Estadual de Londrina, Brasil.
Ida
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EI
D000818:Animals; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D006801:Humans; D010179:Pancreas / Q000201:enzymology; D012469:Salivary Glands / Q000201:enzymology; D013552:Swine; D013997:Time Factors; D014908:Triticum; D000516:alpha-Amylases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification
D004791:Enzyme Inhibitors; D000516:alpha-Amylases