Marked difference in efficiency of the digestive enzymes pepsin, trypsin, chymotrypsin, and pancreatic elastase to cleave tightly folded proteins

Abstract In order for the intestinal mucosa to absorb dietary proteins they have be digested into single amino acids or very short peptides of a length not more than four acids. study efficiency digestive endopeptidases digest folded we analyzed several target under different conditions, native proteins, heat denatured and acid treated. The three pancreatic serine proteases, trypsin, chymotrypsin, elastase, were found remarkable inefficient in cleaving whereas pepsin, which acts at low pH (pH 1.2) was much efficient, possibly due denaturing conditions thereby better accessibility internal cleavage sites pH. Heat treatment improved considerably by all enzymes, but followed return neutral did any major effect. Cleavage when protein is state, apparently efficient. This indicates that pepsin prime enzyme properly enzymes primarily are involved generating efficient uptake mucosa.