Acid-aided protein recovery from enzyme-rich Pacific whiting

Y. J. Choi; Jae W. Park

doi:10.1111/j.1365-2621.2002.tb08846.x

Acid-aided protein recovery from enzyme-rich Pacific whiting

Y. J. Choi, Jae W. Park

Department of Food Technology

Research output: Contribution to journal › Article › peer-review

115 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	2962-2967
Number of pages	6
Journal	Journal of Food Science
Volume	67
Issue number	8
DOIs	https://doi.org/10.1111/j.1365-2621.2002.tb08846.x
Publication status	Published - 2002 Oct

Keywords

Acid-aided protein recovery
Pacific whiting
Solubility
Surimi

ASJC Scopus subject areas

Food Science

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10.1111/j.1365-2621.2002.tb08846.x

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abstract = "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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AU - Choi, Y. J.

AU - Park, Jae W.

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AB - 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.

KW - Acid-aided protein recovery

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KW - Solubility

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Acid-aided protein recovery from enzyme-rich Pacific whiting

Abstract

Keywords

ASJC Scopus subject areas

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