Abstract
This study was conducted to prepare calcium chelate of low-molecular-weight tuna bone collagen peptides (TBCP(LMW)) with a high chelation rate and to identify its structural characteristics and stability. The optimum conditions for calcium chelation of TBCP(LMW) (TBCP(LMW)-Ca) were determined through single-factor experiments and response surface methodology, and the calcium-chelating capacity reached over 90% under the optimal conditions. The amino acid compositions implied that Asp and Glu played important roles in the formation of TBCP(LMW)-Ca. Structural characterizations determined via spectroscopic analyses revealed that functional groups such as -COO(-), N-H, C=O, and C-O were involved in forming TBCP(LMW)-Ca. The particle size distributions and scanning electron microscopy results revealed that folding and aggregation of peptides were found in the chelate. Stability studies showed that TBCP(LMW)-Ca was relatively stable under thermal processing and more pronounced changes have been observed in simulated gastric digestion, presumably the acidic environment was the main factor causing the dissociation of the TBCP(LMW)-Ca. The results of this study provide a scientific basis for the preparation of a novel calcium supplement and is beneficial for comprehensive utilization of tuna bones.