Influence of Malting on the Protein Composition of Spelt (Triticum spelta L.) ‘Frankenkorn’

Abstract

Although spelt has promising aptitudes for beer and beverage production, almost no investigation about its protein modifications during malting has been conducted. Spelt proteins during the malting process were separated and analyzed, first, according to the isoelectric point and molecular weight (MW) and, second, according to solubility and MW. Moreover, the composition of the free amino acid was determined. Spelt proteins could be divided into a total of 13 zones according to their isoelectric point and MW. Most of the present proteins (90%) had a MW between 35,000 and 60,000 and an isoelectric point between 5.84 and 9.52. The most prominent protein fraction was defined by an isoelectric point between 5.84 and 6.89 and a MW between 35,000 and 55,000. Generally, a protein degradation process during malting was found. The Osborne fractionation revealed an albumin band pattern between 14,000 and 131,700, globulin ranging from 13,400 to 130,500, gliadin from 14,500 to 220,800, and glutenin from 19,800 to 215,300. The free amino acid composition increased in concentration except for asparagine, which decreased during malting. This paper contributes to the understanding of the protein modifications and metabolic changes during the malting process of spelt and facilitates the determination of the potential of this cereal for the production of cereal‐based products.