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GrainGenes Reference Report: JFB-18-83

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Reference	JFB-18-83
Title	Purification and partial characterization of two proteinaceous alpha-amylase inhibitors from triticale
Journal	Journal of Food Biochemistry
Year	1994
Volume	18
Pages	83-102
Author	Ida E Finardi-Filho F Lajolo F
Abstract	A total of six alpha-amylase inhibitory proteins (isoinhibitors) were extracted from triticale (Triticum X Secale) seeds and two of them were purified to homogeneity The isoinhibitors were extracted by 70% ethanol and produced, by Sephadex G-100 chromatography, two peaks that exhibited alpha-amylase inhibitory activity Further purification of the most active peak by DEAE-cellulose chromatography resulted in six active fractions Two of them designated as TAI-5 and TAI-6, considered to be homogeneous by both acidic and alkaline electrophoresis, were partially characterized The isoelectric points were 480 and 470, and the molecular weights 39,200 and 29,200, respectively Under dissociating conditions the molecular weights were 13,500 and 13,000, suggesting that the isoinhibitors are composed of three and two subunits, respectively. Both isoinhibitors were stable at different pHs, relatively stable at 98C, and resistant to proteolysis by trypsin, chymotrypsin and pepsin. The optimum interaction pH for both isoinhibitors with human salivary amylase was 7.9. They exhibited specificity to human salivary and porcine pancreatic alpha-amylases, but had no inhibitory activity on Bacillus subtilis, Aspergillus oryzae and endogenous triticale alpha-amylases.
Keyword	[ Hide all but 1 of 10 ] alpha-amylase characterization chromatography enzyme-inhibitors physicochemical-properties proteinase proteolysis purification stability triticale

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