Marine industry waste is rich in the extracellular structural protein collagen, excised fragments of which are known to display numerous physiological activities. This study aims at screening waste derived collagen hydrolysates for their utility as peroxide inhibitors in lipid‐based food and cytoprotective agents via cell culture. Collagen was isolated from Pacu and Rohu waste by acid dissolution and salt precipitation. The purified collagen samples were analyzed through electrophoresis, spectral, and elution pattern and confirmed to be of Type‐I. The hydrolysates exhibited a molecular weight around 5 kDa and were found to be in random conformation. The hydrolysates substantially decreased peroxidation levels by 80–90% in linoleic acid model and were equally effective in market available products: cod liver oil and mustard oil. Cell culture assays showed that the hydrolysates were not toxic and capable of increasing cell survival rate by scavenging lipid peroxides generated in situ. Practical applications Peroxidation of lipid‐based food products leads to decreased quality, low benefit‐to‐cost ratio, and imparts harmful effects on consumption, thus requiring synthetic antioxidants to be added to the food. Synthetic oxidation inhibitors currently used carry the risk of carcinogenicity, making the search for natural, nontoxic, and biocompatible peroxide inhibitors a research hotspot. Collagen hydrolysates are bioactive, nontoxic, immune‐compatible, provide added nutritional benefits on consumption and as seen in this study, can be mass isolated from marine industrial wastes making them the perfect functional food additive to be replacing synthetic antioxidants. The utilization of waste would reduce pollution, add substantial value to a common industrial waste and remove the cost of peroxide inhibitor synthesis leading to decrease in the food price and increased shelf life.

No abstract

No abstract

No abstract

This study attempts to identify the significant role played by the secondary structure of collagen-derived peptides that are involved in lipid peroxide quenching in food products. Collagen was extracted from the skin of Perch and swim bladder of Rohu at 45-78% efficiency. It was identified as type-I based on a high molecular weight (110kDa) and its ion-exchange elution profile. The collagen samples were enzymatically hydrolyzed and collagen hydrolysate (CH) was extracted with an efficiency of 0.67-0.74g/g of collagen. The CH samples displayed a molecular weight in the range of 8.2-9.7kDa and exhibited a higher abundance of charges resulting in higher solubility. The structural studies revealed that the CH peptides existed in polyproline-II helix and formed a mimic-triple helix in a wide range of pH. In neutral and alkaline pH, the mimic helices joined to form a hierarchical quasi-fibrillar network that was smaller than collagen fibrils but also more dynamic. The CH exhibited >95% degradation in 15h through simulated digestion. The CH were able to decrease peroxide formation by 84.5-98.9% in commercially available cod liver and almond oil and increased the shelf life of soya bean oil by a factor of 5 after 6 months of storage. The addition of CH to cultured cells quenched peroxide ions generated in situ and decreased stressor activity by a factor of 12. The reason behind the high efficacy of CH was deciphered to be the proximal charge stabilization by the quasi-fibrillar network, which allowed efficient peroxide quenching and long-term stability.