Zhong Yaqi, Zhou Yufang, Ma Mingzhu, Zhao Yadong, Xiang Xingwei, Shu Conghan, Zheng Bin
School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316000, China.
Zhejiang Marine Development Research Institute, Zhoushan 316000, China.
Foods. 2023 Sep 12;12(18):3403. doi: 10.3390/foods12183403.
This study was conducted to prepare calcium chelate of low-molecular-weight tuna bone collagen peptides (TBCP) with a high chelation rate and to identify its structural characteristics and stability. The optimum conditions for calcium chelation of TBCP (TBCP-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-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-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-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-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.
本研究旨在制备具有高螯合率的低分子量金枪鱼骨胶原蛋白肽（TBCP）钙螯合物，并鉴定其结构特征和稳定性。通过单因素实验和响应面法确定了TBCP（TBCP-Ca）钙螯合的最佳条件，在最佳条件下钙螯合能力达到90%以上。氨基酸组成表明，Asp和Glu在TBCP-Ca的形成中起重要作用。通过光谱分析确定的结构表征表明，-COO、N-H、C=O和C-O等官能团参与了TBCP-Ca的形成。粒度分布和扫描电子显微镜结果表明，在螯合物中发现了肽的折叠和聚集。稳定性研究表明，TBCP-Ca在热加工过程中相对稳定，而在模拟胃消化中观察到更明显的变化，推测酸性环境是导致TBCP-Ca解离的主要因素。本研究结果为新型钙补充剂的制备提供了科学依据，有利于金枪鱼骨的综合利用。
