Linjiang Zhu (1), Yupeng Han (1), Qi Li (1), Jinjing Wang (1); (1) Jiangnan University, Wu xi, China
Technical Session 20: Mashing, Boiling, & Wort
Wednesday, August 17 • 8:15–9:30 a.m.
Plaza Building, Concourse Level, Governor’s Square 14
In beer brewing, protein Z was supposed to be beneficial to beer
foam. Few investigations have revealed the relationships between
conformational alteration of protein Z and beer foam. In this work,
protein Z was purified and identified during mashing and boiling
processes. Circular dichroism (CD) and Fourier transform infrared
spectroscopy (FTIR) were used to monitor the structural characteristics.
The results showed that the contents of alpha-helices and beta-sheets
of protein Z decreased and the contents of beta-turns and random coils
increased. The complex environment rich in polysaccharides might lead to
the conformational alteration and modifications. Meanwhile, the
extended structural features of protein Z provided more amino acid
residues for modifications and exposed more intra-hydrophobic regions.
Analyzing the structural transformations of protein Z provides a deeper
understanding of the mechanism of protein Z in maintaining beer foam.
