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Effects of the extraction temperatures on the protein contents, gelatin purities, physicochemical properties, and functional properties of tilapia scale gelatins. | LitMetric
Medical Food Laboratory, Shanghai Key Laboratory of Pediatric Gastroenterology and Nutrition, Shanghai Institute for Pediatric Research, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200092, China; National R&D Branch Center for Freshwater Aquatic Products Processing Technology (Shanghai), Integrated Scientific Research Base on Comprehensive Utilization Technology for By-Products of Aquatic Product Processing of Ministry of Agriculture and Rural Affairs, Shanghai Engineering Research Center of Aquatic-Product Processing and Preservation, College of Food Science & Technology, Shanghai Ocean University, Shanghai 201306, China; Department of Clinical Nutrition, College of Health Science and Technology, Shanghai Jiao Tong University School of Medicine, Shanghai 200135, China; Marine Biomedical Science and Technology Innovation Platform of Lingang Special Area, Shanghai 201306, China. Electronic address:
Published: October 2024
AI Article Synopsis
Article Abstract
Herein, the effects of the extraction temperatures (45, 55, 65, 75, and 85 °C) on the protein contents, gelatin purities, physicochemical properties, and functional properties of tilapia scale gelatins were studied. Among these temperatures, 65 °C was the best extraction temperature to obtain good production yield (16.0 % ± 0.3 %), good protein contents (excellent total amino acid composition of 94.20 ± 0.76 g/100 g of gelatin, the highest hydrophobic amino acids percentage of 32.68 ± 0.24 g/100 g of gelatin), appropriate ATR-FTIR spectra peaks (Amides A, B, I, II, and III), high β-sheet percentage (38.2 % ± 1.3 %), the highest purity of the gelatin structures (280, 140, and 125 kDa), the lowest nanoparticle sizes in atomic force microscopy results, the highest water-holding capacity (25.3 % ± 0.9 %), the highest fat-binding capacity (16.9 % ± 0.1 %), high foaming properties (foaming capacity of 151.7 % ± 7.6 % and foaming stability of 145.8 % ± 6.3 %), the lowest interfacial tension (2.1 ± 0.2 mN/m), the lowest emulsifying activity index (16.5 % ± 0.9 %), the highest emulsifying stability index (88.9 % ± 5.1 %), highest emulsion viscosity (1462 ± 17 mPa·s at the rotary speed of 6 rpm), the lowest initial droplet sizes, and lowest emulsion creaming index (6.9 % ± 0.7 %). This work provided a useful guide to choosing extraction temperature for gelatin extraction and a useful theory on the relationship between compositions and properties of a protein sample.
