Proteolysis of β-Lactoglobulin Assisted by High Hydrostatic Pressure Treatment for Development of Polysaccharides-Peptides Based Coatings and Films

Abstract

Peptides usually have many bioactive functions. The variety of peptide binding and the modularity of the components allow for their application to additional tissues and materials; hence broadening the range of possible coatings and films. β-lactoglobulin (b-LG) forms spherical microgels or can be used in the formation of coated particles, with the core formed by aggregated b-LG and the coat by polysaccharides. The enzymatic proteolysis of b-LG assisted by high hydrostatic pressure (HHP) treatment was studied. Pretreatment of HHP enhanced the hydrolysis degree (DH) of b-LG. The highest value of DH without pretreatment was 24.81% at 400 MPa, which increased to 27.53% at 200 MPa with pretreatment, suggesting a difference in the DH of b-LG caused by the processing strategy of HHP. Molecular simulation suggested that the flexible regions of b-LG, e.g., Leu140-Ala142 and Asp33-Arg40, might contribute to enzymatic proteolysis. The b-LG hydrolysate exhibited the highest capacity of scavenging free DPPH and OH radicals at 200 MPa. In addition, the 1–2 kDa and 500–1000 Da peptides fractions significantly increased from 10.53% and 9.78% (under 0.1 MPa) to 12.37% and 14.95% under 200 MPa, respectively. The higher yield of short peptides under HHP contributed to the antioxidant capacity of b-LG hydrolysates. Enzymatic hydrolysis also largely reduced the immunoreactivity of b-LG, which is of high importance in the practical application of b-LG in the field of coatings and films in regard to biocompatibility. Hydrolysis of b-LG assisted by high-pressure treatment showed promising potential in the preparation of bioactive peptides for further development of polysaccharide-peptide-based coatings and films.