Premium
Thermal Gelation Properties of Protein Fractions from Pork and Chicken Breast Muscles
Author(s) -
LAN Y.H.,
NOVAKOFSKI J.,
McCUSKER R.H.,
BREWER M.S.,
CARR T.R.,
McKEITH F.K.
Publication year - 1995
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/j.1365-2621.1995.tb06219.x
Subject(s) - myofibril , chicken breast , myosin , chemistry , food science , sarcoplasm , biochemistry , endoplasmic reticulum
Thermal gelation properties of myosin, actin, myofibrils (MF), sarcoplasmic protein (SP) and connective tissue (CTS) from pork semimem‐branosus and chicken breast (CB) were evaluated. Gels were prepared at pH 6.0, 2% NaCl and cooked to 70°C at 0.7°C/min. Pork myosin had a higher gel strength and a lower cooking loss than CB myosin at 7% protein. Actin from both species did not form a measurable gel. MF gels from pork and CB had the lowest cooking loss while CTS and SP had the highest cooking loss. Difference in gel strength between muscle and MF+SP+CTS at 7% protein was not consistent with that at 10% protein.