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Water‐soluble myofibrillar proteins prepared by high‐pressure homogenisation: a comparison study on the composition and functionality
Author(s) -
Chen Xing,
Li Yong,
Zhou Ruiyun,
Liu Dongmei,
Xu Xinglian,
Zhou Guanghong
Publication year - 2017
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13515
Subject(s) - chemistry , myofibril , solubility , food science , myosin , whey protein isolate , tropomyosin , composition (language) , water soluble , absorption of water , chemical engineering , lysine , chromatography , amino acid , whey protein , biochemistry , organic chemistry , materials science , linguistics , philosophy , engineering , composite material
Summary 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.