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Acid‐Aided Protein Recovery from Enzyme‐rich Pacific Whiting
Author(s) -
Choi Y.J.,
Park J.W.
Publication year - 2002
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.1365-2621.2002.tb08846.x
Subject(s) - chemistry , cathepsin , solubility , myosin , cathepsin l , biochemistry , enzyme , whiting , food science , chromatography , fish <actinopterygii> , biology , organic chemistry , fishery
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.