Though the question is about biomolecules, we agree the underlying functions, formation, degradation etc come down to chemistry, (then physics and maths). I am posting it here to receive an understanding from chemistry perspective. I am referring this info here to grasp the concept.
e.g. Trypsin is a protease that regulates specific hydrolysis/proteolysis by cleaving at the c terminus side of Arg and Lys.
Similarly, given two catalysts: (proteases) papain and bromelain. Both are said to regulate selective peptide cleavage reactions (specificity of proteolysis) - breaking peptide (amide) bond from C-terminal analysis (enzymatic hydrolysis). This is clear to me.
These enzymes only break c-terminus peptide bonds of specific amino acids. e.g. Papain for Arg and Leu. Bromelain for Ala, Leu, Ser, Gly, Tyr.
How to determine if papain or bromelain hydrolyse a given polypeptide chain completely or partially? And what's the resulting residue and chain? I am not expecting an one-liner, I want to understand the reaction mechanism and concept clearly for further application.
e.g. what's the resulting fragments of this after Papain act on it?