Abstract
Background: β-lactoglobulin hydrolysates (BLGH) have shown antioxidant, antihypertensive, antimicrobial, and opioid activity. In the current study, an innovative combination of high hydrostatic pressure and enzymatic hydrolysis (HHP–EH) was used to increase the yield of short bioactive peptides, and evaluate the anti-inflammatory and antioxidant properties of the BLGH produced by the HHP–EH process. Method: BLG was enzymatically hydrolyzed by different proteases at an enzyme-to-substrate ratio of 1:100 under HHP (100 MPa) and compared with hydrolysates obtained under atmospheric pressure (AP-EH at 0.1 MPa). The degree of hydrolysis (DH), molecular weight distribution, and the antioxidant and anti-inflammatory properties of hydrolysates in chemical and cellular models were evaluated. Results: BLGH obtained under HHP–EH showed higher DH than the hydrolysates obtained under AP-EH. Free radical scavenging and the reducing capacity were also significantly stronger in HHP-BLGH compared to AP-BLGH. The BLGH produced by alcalase (Alc) (BLG-Alc) showed significantly higher antioxidant properties among the six enzymes examined in this study. The anti-inflammatory properties of BLG-HHP-Alc were observed in lipopolysaccharide-stimulated macrophage cells by a lower level of nitric oxide production and the suppression of the synthesis of pro-inflammatory cytokines. Peptide sequencing revealed that 38% of the amino acids in BLG-HHP-Alc are hydrophobic and aromatic residues, which contribute to its anti-inflammatory properties. Conclusions: Enzymatic hydrolysis of BLG under HHP produces a higher yield of short bioactive peptides with potential antioxidant and anti-inflammatory effects.
Highlights
Whey is a byproduct of cheese manufacturing, with a broad range of applications in the food and nutraceutical industries [1]
The degree of hydrolysis (DH) of the BLG samples was determined by measuring the free amino group content of BLG hydrolysates treated under atmospheric and high hydrostatic pressure (Figure 1)
The high hydrostatic pressure enhanced the enzymatic hydrolysis of BLG by various enzymes
Summary
Whey is a byproduct of cheese manufacturing, with a broad range of applications in the food and nutraceutical industries [1]. The main protein constituents of whey are β-lactoglobulin (BLG), α-lactalbumin, and to a lesser extent immunoglobulin and bovine serum albumin [2,3]. Extensive studies have revealed the nutritional and functional properties of whey proteins [3]. Whey proteins have nutritional and functional benefits, their utilization is restricted mainly due to the Cow’s Milk Protein Allergy (CMPA), which is the most prevalent food allergy, in infants [4]. BLG is known as the main allergen in cow’s milk [5].
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