Recycling fish skin for utilization in food industry as an effective emulsifier and foam stabilizing agent

Abstract

Background Indian fish industry produces a staggering amount of waste every year part of which is dumped as landfill leading to pollution. Objective This study aims to extract collagen from fish skin, a major component of this waste, hydrolyze it and use the hydrolysate as emulsifiers to increase the shelf life of food products. Materials and methods Collagen was purified from the skin of Catfish, Mullet and Indian Salmon were characterized through infrared and diffraction studies. The samples were hydrolyzed enzymatically. The hydrolysates were assayed for emulsifying, foam stabilizing and hemolytic properties. Results The samples displayed an electrophoretic and infrared spectral profile corresponding to that of collagen type I. X-ray diffraction patterns revealed the presence of triple helix and traces of phosphate. The hydrolysates (6 kDa) exhibited the highest emulsion at 2.74±0.20 m2/g (for 57.00±0.50 min) and foam stability in the range of 75–78%, respectively. The hydrolysates were able to stabilize drug and food formulations successfully and two of the samples exhibited less than 3% toxicity as determined through hemolytic assay. Conclusion Collagen hydrolysates from fish skin, a common fish industry waste, were found to be bioactive and non-toxic making them suitable replacements for synthetic emulsifiers.

Preparation and Characterization of Fish Skin Collagen Material Modified with β-Glucan as Potential Wound Dressing

“…The use of by-products from a local fish industry may decrease collagen cost and it allows to mitigate environmental problems [ 6 ]. On average, solid waste from fish processing comprises 50% of raw original material (depending on the level of processing and type of fish) [ 7 ]. The skin and bones comprise 30% of these wastes [ 8 ].…”

Characterization and Evaluation of Proteolysis Products during the Fermentation of Acid Whey and Fish Waste and Potential Applications

“…The concentration of peptides increased four times by the end of the experiment, contrary to the decrease of the total soluble protein, suggesting a highly active proteolytic environment . Researchers have also reported activity from endogenous and exogenous enzymes in similar mixtures and meat fermentation practices. , Endogenous enzymes such as trypsin, cathepsins, and calpains start the degradation process by hydrolyzing sarcoplasmic and myofibrillar proteins. , …”

“…38 Researchers have also reported activity from endogenous and exogenous enzymes in similar mixtures and meat fermentation practices. 48,49 Endogenous enzymes such as trypsin, cathepsins, and calpains start the degradation process by hydrolyzing sarcoplasmic and myofibrillar proteins. 46,50 The peptides produced by the endogenous enzyme system are further hydrolyzed by the bacteria, either as an energy source or as a substrate for the bacterial enzymes.…”

Antioxidant cuttlefish collagen hydrolysate against ethyl carbamate-induced oxidative damage

“…18 Unlike polyphenols, collagen hydrolysate that have drawn dramatic attention of researchers is more stable in application due to its special sequence and amphiphilic structure. 19,20 The collagen hydrolysate has been widely applied in the food industry due to its high emulsication stability. [20][21][22][23][24] Collagen hydrolysate, which is benet for human health, is rich in amino acids.…”

“…19,20 The collagen hydrolysate has been widely applied in the food industry due to its high emulsication stability. [20][21][22][23][24] Collagen hydrolysate, which is benet for human health, is rich in amino acids. The diversity of amino acid composition and amino acid sequence endows collagen hydrolysate with a variety of biological activities.…”