Abstract: Nonspecific protein adsorption generally occurs on
any solid surfaces and usually has adverse consequences. Adsorption
of proteins onto a solid surface is believed to be the initial and
controlling step in biofouling. Surfaces modified with end-tethered
poly(ethylene glycol) (PEG) have been shown to be protein-resistant
to some degree. In this study, the adsorption of β-casein and
lysozyme was performed on 6 different types of surfaces where PEG
was tethered onto stainless steel by polyethylene imine (PEI) through
either OH or NHS end groups. Protein adsorption was also performed
on the bare stainless steel surface as a control. The adsorption was
conducted at 23 °C and pH 7.2. In situ QCM-D was used to
determine PEG adsorption kinetics, plateau PEG chain densities,
protein adsorption kinetics and plateau protein adsorbed quantities.
PEG grafting density was the highest for a NHS coupled chain,
around 0.5 chains / nm2. Interestingly, lysozyme which has smaller
size than β-casein, appeared to adsorb much less mass than that of β-
casein. Overall, the surface with high PEG grafting density exhibited
a good protein rejection.
Abstract: the obligatory step during immunoglobulin and lysozyme concentration process is thermal treatment. The combination of temperature and time used in processing can affect the structure of the proteins and involve unfolding and aggregation. The aim of the present study was to evaluate the heat stability of total Igs, the particular immunoglobulin classes and lysozyme in milk. Milk samples were obtained from conventional dairy herd in Latvia. Raw milk samples were pasteurized in different regimes: 63 °C 30 min, 72 °C 15-20 s, 78 °C 15-20 s, 85 °C 15-20 s, 95 °C 15-20 s. The concentrations of Igs (IgA, IgG, IgM) and lysozyme were determined by turbodimetric method. During research was established, that activity of antimicrobial proteins decreases differently. Less concentration reduce was established in a case of lysozyme.