Collagen recovered, isolated and enzymatically hydrolyzed from tannery waste

Abstract

Collagen was isolated from rawhide waste from the leather industry, characterized by electrophoresis and compared with a commercial collagen. Subsequently, it was subjected to an enzymatic treatment using plant peptidases from Bromelia hironymi to produce hydrolyzates, since the production of bioactive peptides by enzymatic hydrolysis is a sustainable way of taking advantage of protein by-products. The hydrolyzate was characterized by mass spectrometry showing peptides in the molecular weight range of 2,000 to 5,000 Da. Further, using liquid chromatography and tandem mass spectrometry (LC−MS/MS) technique, it was possible to identify 31 peptides from the alpha 1 chain of type I collagen and another 13 belonging to the alpha 2 chain of type I collagen. The probability that the identified peptides were bioactive was predicted with Peptide Ranker software (“in silico analysis”), demonstrating that 70% of them have a high bioactivity potential. In this way, the protein recovered from the tannery residues becomes a suitable source for obtaining a product with greater added value than the original material and with multiple potential industrial applications.