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.
Abstract: This study proposes a basic molecular formula for all
proteins. A total of 10,739 proteins belonging to 9 different protein
groups classified on the basis of their functions were selected
randomly. They included enzymes, storage proteins, hormones,
signalling proteins, structural proteins, transport proteins,
immunoglobulins or antibodies, motor proteins and receptor proteins.
After obtaining the protein molecular formula using the ProtParam
tool, the H/C, N/C, O/C, and S/C ratios were determined for each
randomly selected sample. In this case, H, N, O, and S coefficients
were specified per carbon atom. Surprisingly, the results
demonstrated that H, N, O, and S coefficients for all 10,739 proteins
are similar and highly correlated. This study demonstrates that
despite differences in the structure and function, all known proteins
have a similar basic molecular formula CnH1.58 ± 0.015nN0.28 ± 0.005nO0.30
± 0.007nS0.01 ± 0.002n. The total correlation between all coefficients was
found to be 0.9999.