Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model

•Collagen hydrolysates were produced by Alcalase, Flavouzyme, and trypsin.•Transepithelial transport was studied in a Caco-2 cell line.•Alcalase-Flavourzyme (AF) treatment yielded very low molecular weight peptides.•The transepithelial transport efficiency was the greatest for the AF treatment.

Collagen was extracted from raw bovine hide and hydrolyzed by one of three enzymes - Alcalase, Flavourzyme, or trypsin - or by using a combination of two or three of these enzymes. The Alcalase-containing enzymatic hydrolysis treatments generated a greater proportion of hydrolysates with molecular weight (MW) <2 kDa (79.8-82.7%). Flavourzyme-containing hydrolysis treatments exhibited the greatest proportion of free amino acids (686-740 nmol/mg). The hydrolysates were then subjected to a simulated gastrointestinal (GI) digestion, and transport studies were conducted using a Caco-2 cell model. Due to the lower MW profile, the hydrolyzed collagen showed greater resistance to GI digestion and greater transport efficiency than the unhydrolyzed collagen control. Hydrolysates from a dual enzyme mixture - the Alcalase/Flavourzyme combination - generated the greatest transport efficiency across Caco-2 cell monolayers (21.4%), two-fold more than that of the collagen control.