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.
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