Abstract
In this study three complete triticales, three substituted (one gene from rye has been replaced by one gene from wheat) triticales, and parental wheat and rye were analysed for α-amylase inhibitory activity to evaluate whether the genetic modification influenced triticale α-amylase inhibitory activity. Gel filtration chromatography and thermostability analyses were performed to partially isolate and characterize α-amylase inhibitors. Results demonstrated that substituted triticales and wheat had higher α-amylase inhibitory activities and higher water-soluble protein contents than complete triticales and rye. Sodium dodecylsulfate-PAGE-electrophoresis showed that all triticales, irrespective of their classification, inherited the water-soluble protein patterns from their parents: wheat and rye. In a substituted triticale (Pony ‘S’), two peaks with α-amylase inhibitory activity were resolved by gel filtration chromatography; they were designated T1 and T2 according to their order of elution. T1 showed a higher inhibitory activity but a lower thermostability at 70 °C than T2; T1 apparently comes from wheat, whereas T2 presumably comes from rye. © 1999 Society of Chemical Industry
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