Phosphorylation modification of tilapia skin gelatin hydrolysate and identification and characterization of calcium-binding peptides

• Published in: Process biochemistry (1991) Vol. 127; pp. 1 - 9
• Main Authors: Mei, Zhang, Jinlun, He, Hongyu, Pan, Liping, Sun, Yongliang, Zhuang
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.04.2023
• Subjects: calcium; Calcium-binding capacity; chelation; electron microscopy; Fourier transform infrared spectroscopy; gelatin; hydrolysates; mass spectrometry; Peptide; phosphates; phosphopeptides; Phosphorylation; proteinases; Structural characteristics; Tilapia skin gelatin; Calcium-binding capacity; Phosphorylation; Structural characteristics; Peptide; Tilapia skin gelatin

In present study, complex protease was utilized to prepare tilapia skin gelatin hydrolysate (TSGH), and the phosphorylation conditions of TSGH were optimized using calcium-binding capacity. The phosphorylation degree of TSGH under the optimal conditions was 0.55%. The calcium-binding capacities of T...