@misc{keppler_functionality_of_2017, 
author={Keppler, J.K., Martin, D., Haramus, V.M., Berton-Carabin, C., Nipoti, E., Coenye, T., Schwarz, K.},
title={Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7},
year={2017},
howpublished = {journal article},
doi = {https://doi.org/10.1016/j.foodhyd.2016.11.016},
abstract = {The results showed that both whey proteins β-LG and α-lactalbumin (ALA) were modified by AITC. This modification remained stable during pH adjustment. Unbound AITC was successfully removed by the lyophilization process, which reduced the strong odor of the volatile AITC. A shift of the isoelectric point towards acidic conditions was observed. The hydrophobicity of the modified WPI increased significantly and the protein's secondary and tertiary structure was altered. In addition, a more loose protein folding was observed. These effects were less pronounced at pH 6 and 7. The relatively mild antibacterial effect of native WPI was not significantly influenced by the addition of AITC.},
note = {Online available at: \url{https://doi.org/10.1016/j.foodhyd.2016.11.016} (DOI). Keppler, J.; Martin, D.; Haramus, V.; Berton-Carabin, C.; Nipoti, E.; Coenye, T.; Schwarz, K.: Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7. Food Hydrocolloids. 2017. vol. 65, 130-143. DOI: 10.1016/j.foodhyd.2016.11.016}}