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- W2316097129 abstract "Purified E. histolytica amylases III to VI were characterized by their hydrolytic behaviour towards 4-nitrophenyl alpha-malto-oligosaccharides, malto-oligosaccharides, amylose, amylopectin, glycogen and Y-cyclodextrin. The influence of specific inhibitors on the amylase activity of E. histolytica was examined and compared with typical alpha- and beta-amylases. Amylases III and IV showed alpha-glucosidase and glucosyltransferase activity by cleaving terminal non-reducing glucose from pNPG1 (III, IV) and pNPG2 to pNPG7 (III). Both enzymes were able to cleave malto-oligosaccharides and glucopolysaccharides to a large number of malto-oligosaccharides. Also transglucosidation reactions were observed, but maltose was not hydrolysed. Amylase V showed exoamylase-like properties by preferentially cleaving maltose units from the non-reducing end of synthetic and biogenic malto-oligosaccharides by a multiple-attack mechanism. Amylase VI was characterized as an alpha-amylase, showing great similarities with porcine pancreatic alpha-amylase in the hydrolysis pattern of 4-nitrophenyl alpha-malto-oligosaccharides and glucopolysaccharides. With biogenic malto-oligosaccharides amylase VI showed a transglucosidation reaction." @default.
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- W2316097129 date "1986-01-01" @default.
- W2316097129 modified "2023-09-27" @default.
- W2316097129 title "Separation and Characterization of Four Different Amylases ofEntamoeba histolytica.II. Characterization of Amylases" @default.
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- W2316097129 doi "https://doi.org/10.1515/bchm3.1986.367.1.169" @default.
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