Premium
Effect of sarcoplasmic proteins oxidation on the gel properties of myofibrillar proteins from pork muscles
Author(s) -
Feng Xiaolong,
Wu Di,
Yang Kun,
Wang Limei,
Wang Xian,
Ma Jing,
Zhang Yunhua,
Wang Caili,
Zhou Yuanhua,
Sun Weiqing
Publication year - 2021
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/1750-3841.15687
Subject(s) - myofibril , chemistry , covalent bond , sarcoplasm , disulfide bond , ascorbic acid , chromatography , nuclear chemistry , biochemistry , organic chemistry , food science , endoplasmic reticulum
Abstract This study investigated the influence of sarcoplasmic proteins (SPs) treated by the oxidation system (0.1 mmol/L FeCl 3 , 0.1 mmol/L ascorbic acid, and 0, 1, 5, 10 mmol/L H 2 O 2 ) on the properties of pork myofibrillar proteins (MPs) gel. After oxidation treatment, the SPs showed an increased in carbonyl content and a decreased in total sulfhydryl content, coupled with the cross‐linking of protein components by disulfide bonds and covalent bonds. The MPs gel with SPs oxidized at 1 mmol/L H 2 O 2 exhibited the maximal strength while the minimal water holding capacity (WHC). The WHC of MPs gel was significantly decreased with increasing SPs oxidation, leading to the increase of free water and the decrease of immobilized water in the gel system. The microstructures of MPs gels with moderately (1 mmol/L H 2 O 2 ) oxidized SPs showed a more compact and smaller pore gel network than MPs alone, suggesting adding oxidized SPs can expel water trapped in the gel. Furthermore, the environmental polarity of aliphatic C‐H groups increased with SPs oxidation.