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Identification of α‐amylase inhibitors in triticale grain
Author(s) -
BurgosHernández Armando,
RosasBurgos Carina,
RamírezWong Benjamín,
CarbonellBarrachina Angel A,
CincoMoroyoqui Francisco J
Publication year - 1999
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(199909)79:12<1671::aid-jsfa418>3.0.co;2-d
Subject(s) - triticale , thermostability , size exclusion chromatography , amylase , endosperm , chemistry , biochemistry , enzyme , food science , chromatography , biology , botany
Abstract In this study three complete triticales, three substituted (one gene from rye has been replaced by one gene from wheat) triticales, and parental wheat and rye were analysed for α‐amylase inhibitory activity to evaluate whether the genetic modification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