Water-soluble myofibrillar proteins prepared by high-pressure homogenisation: a comparison study on the composition and functionality
Water-soluble myofibrillar proteins prepared by high-pressure homogenisation: a comparison study on the composition and functionality
复制标题
高压均质制备水溶性肌原纤维蛋白：组成和功能的比较研究
DOI：
10.1111/ijfs.13515
复制
发表时间：
2017-11-01
影响因子：
3.3
通讯作者：
Zhou, Guanghong
中科院分区：
文献类型：
--
作者：
Chen, Xing;Li, Yong;Zhou, Guanghong
为了扩大肉类在各种产品中的应用，通过与大豆分离蛋白(SPI)和乳清分离蛋白(WPI)的比较，确定了高压匀浆(HPH)诱导的水溶性肌原纤维蛋白(WSMP)的性质和功能。WSMP蛋白质含量较高(87.40%)，主要由肌球蛋白、肌动蛋白和原肌球蛋白组成。WSMP的必需氨基酸达到粮农组织/WHO/UNO(2007)学龄前儿童标准，其赖氨酸和含硫氨基酸的含量高于SPI，适合儿童配方。WSMP具有较高的表面疏水性，其水溶性与SPI相近，但低于WPI。WSMP具有优异的吸水吸油性能和乳化性能。WSMP的纤维状结构和高疏水活性特性能够稳定亚微米级的油滴，从而使其具有优异的乳化性能。
To expand utilisation of meat in various products, the characterisation and functionalities of water-soluble myofibrillar proteins (WSMP) induced by high-pressure homogenisation (HPH) were determined by comparison with those of soy protein isolate (SPI) and whey protein isolate (WPI). WSMP had high contents of protein (87.40%), which was mainly composed of myosin, actin and tropomyosin. The essential amino acids of WSMP achieved the FAO/WHO/UNO (2007) standards for preschool children, and the contents of lysine and sulphur-containing amino acids of WSMP were higher than those of SPI, making it desirable for children formulations. WSMP showed higher surface hydrophobicity while its water solubility was similar to that of SPI, but lower than that of WPI. WSMP demonstrated superior water/oil absorption capacities and emulsifying properties. The fibrous structure and high hydrophobic activity characteristics of WSMP were able to stabilise oil droplets with submicron droplet size, consequently responsible for its excellent emulsifying properties.