Influence of Malting on the Protein Composition of Triticale (× Triticosecale Wittmack) ‘Trigold’

Abstract

Triticale (× Triticosecale Wittmack) is a promising cereal for malting and brewing owing to its high levels of α‐amylase and proteolytic activity and low gelatinization temperatures. However, almost no investigation about its protein modifications during malting has been conducted. In this work, triticale proteins during the malting process were separated and analyzed, first, according to their isoelectric point and molecular weight (MW) and, second, according to their solubility and MW. Moreover, the composition of free amino acids was determined. The results describe the modification changes of the different protein fractions during malting. Triticale proteins were found between 4,700 and 64,000. The majority of the proteins were characterized as having an isoelectric point between 5.08 and 6.63. The Osborne fractionation revealed an albumin band pattern of between 13,400 and 153,800, globulin from 12,700 to 152,300, gliadin from 14,500 to 230,100, and glutenin from 11,200 to 102,200. Free amino acids increased in concentration during malting except for asparagine, which decreased. Asparagine exhibited varying trends during malting. This paper contributes to the understanding of the protein modifications and metabolic changes during the malting process of triticale and indicates the potential of this cereal for the production of cereal‐based products.