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- W2321171920 abstract "Protein Z4, an abundant of serpin storage proteins of Hordeum vulgare, is one major factor that benefits the stability of beer foam. In this study, protein Z4 from Canadian malt Metcalfe was cloned and expressed in Pichia pastoris. The glycosylated 45 kDa of recombinant protein Z4 was purified by Ni-NTA affinity column. The secondary structure of recombinant protein Z4 was detected via Circular Dichroism (CD) and Fourier Transform Infrared Spectroscopy (FTIR), and β-sheets and β-turns were the main structure of recombinant protein Z4. A few structural differences between recombinant protein Z4 and protein Z4 from malt were also analyzed, that more obvious α-helical structure and more S-H contents were detected in recombinant protein Z4. Meanwhile, higher structural stability of recombinant protein Z4 was also observed after incubating the samples in a wide range of temperature, pH and ethanol. These results confirmed the positive relationship between modifications by saccharides and high structural stability of recombinant protein Z4." @default.
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- W2321171920 date "2016-07-01" @default.
- W2321171920 modified "2023-10-15" @default.
- W2321171920 title "Heterologous expression of Hordeum vulgare protein Z4 in Pichia pastoris shows increased structural stability" @default.
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- W2321171920 doi "https://doi.org/10.1016/j.procbio.2016.03.019" @default.
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