proteolysis - how to determine the partial or completeness of the cleavage reaction?

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.](https://www.liverpool.ac.uk/~agmclen/Medpracs/practical_3/theory_3.html)


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.


[![enter image description here](https://i.stack.imgur.com/knEuk.jpg)](https://i.stack.imgur.com/knEuk.jpg)


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? 


Arg-Leu-Ser-Ala-Tyr


