MBAA TQ https://doi.org/10.1094/TQ-59-2-0728-01 | 
VIEW ARTICLE
Andrew Marcus (1), Gabriela Grigorean (2), and Glen Fox (1). 1. Food Science & Technology Department, University of California, Davis, CA, USA. 2. UC Davis Genome Center, Proteomics Core, University of California, Davis, CA, USA
Abstract
In addition to industry standard methods applied to analyze grains, malt, and wort, modern mass spectrometry-based proteomics methods offer a new paradigm to evaluate changes to the protein makeup of grains during the stages of malting. In this study, the recently domesticated perennial grain Kernza (Thinopyrum intermedium) was sampled during malting and kilning processes, and the proteome was evaluated against a barley reference that was malted similarly. In the finished Kernza malt, numerous proteins important for brewing were identified, including mash-active enzymes such as α- and β-amylases, carboxypeptidase, and foam-positive proteins such as serpins and lipid transfer proteins. Structural prolamin proteins were identified in the Kernza grains before malting and were reduced in abundance during malting at rates similar to the hordeins in the well-modified barley reference. These analyses show that Kernza may potentially be able to replace 100% of the barley malt in the grist. Additionally, insights gleaned from the Kernza malt proteome may support future breeding of this grain to encourage its wider acceptance as malt by focusing on increasing the production of the diverse hydrolyzing enzymes utilized in the mash and reducing the abundance of storage proteins.
Keywords: amylase, Kernza, malt, novel grains, proteases, proteomics
