Investigating on the calcium binding characteristics of black protein hydrolysate
Investigating on the calcium binding characteristics of black protein hydrolysate
复制标题
黑色蛋白水解物钙结合特性的研究
DOI:
10.1039/d0fo01708f
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发表时间:
2020
期刊:
影响因子:
6.1
通讯作者:
Yuanfa Liu
中科院分区:
文献类型:
--
作者:
Man Wang;Zhaojun Zheng;Chunhuan Liu;Hong Sun;Yuanfa Liu
The black bean protein has been widely utilized to prepare hydrolysates with different bioactive properties. Herein, we hydrolyzed the black bean protein to prepare hydrolysate with calcium binding activity and characterized its behavior. Our results showed that ficin was superior in obtaining hydrolysate with calcium binding capacity in comparison with trypsin, alcalase and bromelain. In particular, the optimal capacity of ficin hydrolysate reached 77.54 ± 1.61 μg mg−1, where the optimal hydrolysis conditions of ficin were a temperature of 70 °C, a pH value of 6.2, an enzyme concentration of 1.61% and a time of 3 h. This might be due to high proportions of aspartic acid and glutamic acid (35.59%). Further spectral analysis evidenced the formation of hydrolysate–calcium complexes, demonstrating that the interaction between hydrolysate and calcium ions primarily occur on carboxyl oxygen atoms and amino nitrogen atoms. These findings provide a possible utilization of black bean hydrolysate to serve as a calcium supplement nutraceutical to enhance the absorption and bioavailability.