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Identification of ?-amylase inhibitors in triticale grain

✍ Scribed by Burgos-Hern�ndez, Armando; Rosas-Burgos, Carina; Ram�rez-Wong, Benjam�n; Carbonell-Barrachina, Angel A; Cinco-Moroyoqui, Francisco J

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
122 KB
Volume
79
Category
Article
ISSN
0022-5142

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✦ Synopsis

In this study three complete triticales, three substituted (one gene from rye has been replaced by one gene from wheat) triticales, and parental wheat and rye were analysed for a-amylase inhibitory activity to evaluate whether the genetic modi®cation in¯uenced triticale a-amylase inhibitory activity. Gel ®ltration chromatography and thermostability analyses were performed to partially isolate and characterize a-amylase inhibitors. Results demonstrated that substituted triticales and wheat had higher a-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 classi®cation, inherited the water-soluble protein patterns from their parents: wheat and rye. In a substituted triticale (Pony `S'), two peaks with a-amylase inhibitory activity were resolved by gel ®ltration 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.

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