Activity‐based protein profiling of hydrolytic enzymes induced by gibberellic acid in isolated aleurone layers of malting barley. Issue 17 (4th August 2016)

• Record Type: Journal Article
• Authors: Daneri‐Castro, Sergio N.; Chandrasekar, Balakumaran; Grosse‐Holz, Friederike M.; van der Hoorn, Renier A. L.; Roberts, Thomas H.
• Is Part Of: FEBS letters. Volume 590:Issue 17(2016)
• Page Start: 2956
• Page End: 2962
• Publication Date: 2016-08-04
• Subjects: activity‐based protein profiling -- aleurone layer -- barley; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12320
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : 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. Abstract :