Production of Low Molecular Weight Biopeptides with High Biological Activity from Animal Protein Sources by A Multi-Enzyme Mixture
DOI:
https://doi.org/10.24925/turjaf.v14i5.1350-1362.8528Keywords:
bioactive peptides, Enzymatic hydrolysis, Collagen, whey protein, protein hydrolisateAbstract
In this study, the bioactive peptide contents, ADE inhibition activities, antioxidant properties, and degrees of hydrolysis of hydrolysates obtained from the enzymatic hydrolysis of bovine collagen, fish collagen, and whey (PAS) protein sources were investigated. The results demonstrated that hydrolysis facilitated by a complex enzyme mixture of alcalase, neutrase, collagenase, and flavourzyme (1:1:1:1 v/v) (1 g enzyme mixture/100 g protein source) significantly increased bioactive peptide production and total protein content. Bovine collagen achieved the highest degree of hydrolysis (30.4%) and bioactive peptide content (868.74 mg/ml), while fish collagen and PAS were at lower levels. Fish collagen hydrolysates stood out with the highest reactive carboxyl group content (20.43 mmol KOH/g) and low molecular weight (979.22 Mn(mol.equivalent/L)). PAS hydrolysates, with their high molecular weights (4308.32 Mn(mol.equivalent/L)), were prominent in technological applications. In ADE inhibition activities, the highest values were observed in fish and bovine collagen hydrolysates (93.3% and 93.6%, respectively), while PAS hydrolysates exhibited lower inhibition activity (87.5%). In antioxidant activity tests (ABTS and DPPH), fish collagen demonstrated the highest antioxidant activity (45.70 TEAC/g and 14.30% inhibition), whereas bovine collagen exhibited lower activity (33.38 TEAC/g and 8.17% inhibition). These findings suggest that the multi-enzyme mixture used can be applied to all animal-derived protein sources for the production of highly bioactive peptides. In conclusion, bovine and fish collagen, in particular, offer significant potential for use as functional food additives and in health-related applications. This study is original in that, unlike previous studies, collagen molecules were subjected to an advanced degree of hydrolysis using a multi-enzyme system.
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