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| Physicochemical and Functional Properties of Collagen Peptides Derived from Ultrasonic-Assisted Alkaline Protease Hydrolysis of Chicken Claws |
| ZHOU Ting, WU Yujie, LU Fangyun, YANG Biao, MA Jingjing, YANG Jing, ZOU Ye, WANG Daoying, XU Weimin |
| 1. Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Science, Nanjing 210014, China; 2. College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China |
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Abstract The physicochemical properties (color appearance, isoelectric point, molecular mass, SDS polyacrylamide gel electrophoresis pattern, amino acid composition and hydrolysis degree) of collagen peptides produced by ultrasonic-assisted alkaline protease hydrolysis of chicken claws were determined as well as the functional characteristics such as foaming ability, foam stability, emulsification ability and emulsion stability. The results showed that the molecular mass distribution of the collagen peptides was below the α2-chain, small peptides being the major ones. The collagen peptides contained a wide variety of amino acids, with glycine and proline being the predominant ones. The hydrolysis degree of the collagen peptides prepared under the optimized conditions, having good foaming ability (133.33%) and foam stability (126.67%), having good emulsification capacity and emulsion stability, was about 28.65%.
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2021, Vol. 35 
