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Evaluation of pH ‐treated fish sarcoplasmic proteins on rheological properties of fish myofibrillar protein mediated by microbial transglutaminase
Author(s) -
Hemung BungOrn,
Chin Koo B.
Publication year - 2014
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.12569
Subject(s) - myofibril , tissue transglutaminase , chemistry , sarcoplasm , rheology , denaturation (fissile materials) , food science , fish <actinopterygii> , protein isolate , water holding capacity , chromatography , biochemistry , enzyme , nuclear chemistry , fishery , biology , materials science , endoplasmic reticulum , composite material
Summary Fish sarcoplasmic protein ( SP ) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH ‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein ( MP ) with microbial transglutaminase ( MTG ). The denaturation temperature ( T d ) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH ‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH ‐treated SPs, while the breaking forces were similar to control. The result indicated that pH ‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties.