Journal
JOURNAL OF FOOD SCIENCE
Volume 67, Issue 8, Pages 2962-2967Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2621.2002.tb08846.x
Keywords
acid-aided protein recovery; surimi; Pacific whiting; solubility
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Relatively higher protein recovery was obtained in acid-aided processing. Solubility was lowest at pH 5 and gradually increased up to pH 11.0. A sharp increase in solubility occurred at alkaline pH between 9.5 and 11.0 and at acidic pH between 3.0, and 1.5. Cathepsin B and L showed higher activities in acid surimi than conventional surimi. Acid-aided surimi did not show Ca- and Mg-ATPase activity and also had lower surface hydrophobicity and sulfurhydryl contents than conventional surimi. Acid processing resulted in low breaking force, possibly due to the activity of retained cathepsin L enzymes. Myosin heavy chain (MHC) and actin were degraded in acid processing and produced major bands right below MHC and actin.
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