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FEBS Lett. 2016 Sep;590(17):2956-62. doi: 10.1002/1873-3468.12320. Epub 2016 Aug 4.

Activity-based protein profiling of hydrolytic enzymes induced by gibberellic acid in isolated aleurone layers of malting barley.

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Faculty of Agriculture and Environment, Plant Breeding Institute, University of Sydney, Eveleigh, Australia.
The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, UK.


During barley germination, the aleurone layer secretes most of the enzymes required to degrade the endosperm, many of which are yet to be characterized. We used activity-based protein profiling (ABPP) to detect a range of active enzymes extracted from aleurone layers isolated from grains of a commercial malting barley variety incubated with or without gibberellic acid (GA). Enzymes found to be induced by GA were putative aleurains, cathepsin-B-like proteases and serine hydrolases. By using an inhibitory sugar panel, a specific active retaining β-glycosidase in the barley aleurone was identified as a putative xylanase. Our results show that ABPP can be used rapidly to identify a variety of active enzyme isoforms in cereal aleurone without the need for enzyme purification.


activity-based protein profiling; aleurone layer; barley

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