M. M. Vorob'ev

TL;DR: Both spectroscopic techniques demonstrate that there are similar but less spectral changes of BSA for the trypsin attack than for α-chymotrypsin although the substrate/enzyme ratio is taken the same.

TL;DR: The unordered structure increases concomitant with a decrease in the remaining structure, thus, revealing breakdown of the intact protein into smaller fragments in an open reaction system such as the stomach.

TL;DR: Demasking of peptide bonds during proteolysis of β-casein and β-lactoglobulin by trypsin was monitored by the measurement of the overall spectral shift of intrinsic protein fluorescence, showing that the fluorescence shift can be attributed to the demasking stage.

TL;DR: In this article, it was shown that the increase of amino nitrogen can be a non-monotonous function of the hydrolysis degree or proteolysis time, which was treated as an indication of the prevalence of the hydrophobically induced masking effect for β-casein.

TL;DR: Lower peptides and amino acids in hydrolyzates of casein obtained with protosubtilin were determined using high pressure liquid chromatography (HPLC) and this result supports the assumption that the substrate proteolysis regulation is realized through the change in the ratio of the rates of peptide bond demasking to those of peptIDE bond hydrolysis.