Interaction between wheat alpha-amylase/trypsin bi-functional inhibitor and mammalian digestive enzymes: Kinetic, equilibrium and structural characterization of binding
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- 作者：Massimiliano Cuccioloni ; massimiliano.cuccioloni@unicam.it" class="auth_mail" title="E-mail the corresponding author ; Matteo Mozzicafreddo ; Ishtiaq Ali ; Laura Bonfili ; Valentina Cecarini ; Anna Maria Eleuteri ; Mauro Angeletti
- 关键词：Bifunctional inhibitor ; Kinetics ; Thermodynamics ; Binding mode ; Wheat ; Gluten sensitivity
- 刊名：Food Chemistry
- 出版年：2016
- 出版时间：15 December 2016
- 年：2016
- 卷：213
- 期：Complete
- 页码：571-578
- 全文大小：1312 K
文摘
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The interaction between a wheat bifunctional inhibitor and trypsin and α-amylase was studied.
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Wheat ATI targets the catalytic regions of both enzymes with independent binding sites.
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Wheat ATI inhibits trypsin and alpha-amylase with moderate-to-high potency.
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The inhibition could affect the onset/progression of gastrointestinal inflammatory disorders.