Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions
Protein solubility of Pacific whiting muscle with isoelectric point at pH 5.5 was significantly affected by pH. The highest breaking force was measured from fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Texture of gels made using the conventional method...
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ftoregonstate:ir.library.oregonstate.edu:0z709076j 2024-09-15T17:35:36+00:00 Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions Kim, Young S. Park, Jae W. Food Science and Technology Oregon State University. Graduate School https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0z709076j English [eng] eng unknown Oregon State University https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0z709076j All rights reserved Surimi Fishery processing Muscle proteins Masters Thesis ftoregonstate 2024-07-22T18:06:05Z Protein solubility of Pacific whiting muscle with isoelectric point at pH 5.5 was significantly affected by pH. The highest breaking force was measured from fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Texture of gels made using the conventional method were quite inferior to gels made using fish proteins treated at pH 2 or 11, while color of conventional gels was significantly better than the other treatments. SDS-PAGE revealed that fish proteins were highly denatured during acid or alkali treatment. High cathepsin B-like activity was detected from acid-aided fish proteins. Strong cathepsin L-like activity was found in fish proteins treated at pH 10.5, which corresponded with the lower breaking force and deformation obtained from those samples. Disulfide bonds contributed to high texture value in fish proteins treated at pH 11. Physicochemical characteristics of sarcoplasmic proteins (SP) from rockfish and their interaction with Alaska pollock surimi (myofibrillar proteins) were investigated. Solubility of SP was significantly suppressed at acidic pH (2-4) plus high salt concentration (0.5 M NaCl). This was also supported by SDS-PAGE results (extensively degraded SP). DSC results revealed SP gave three endothermic transitions. The least amount ofproteins was lost when treated at pH 2 or 3 followed by precipitation at pH 5.5. SP did not enhance the gelation properties of myofibrillar proteins, but positively contributed to gelation with myofibrillar proteins when compared to sucrose. Myofibrillar proteins were primary components contributing to heat-induced gelation. Salt effect on acid- or alkali-treated surimi gel was investigated. Good gels were obtained without salt using acid- and alkali-treated fish proteins. Their texture properties decreased as NaCl content increased, unlike conventional surimi gels. Consequently, NaCl did not solubilize myofibrillar proteins once the fish proteins were treated by acid or alkali. Solubility was apparently not a key factor for ... Master Thesis alaska pollock Alaska ScholarsArchive@OSU (Oregon State University) |
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ftoregonstate |
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English unknown |
topic |
Surimi Fishery processing Muscle proteins |
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Surimi Fishery processing Muscle proteins Kim, Young S. Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
topic_facet |
Surimi Fishery processing Muscle proteins |
description |
Protein solubility of Pacific whiting muscle with isoelectric point at pH 5.5 was significantly affected by pH. The highest breaking force was measured from fish proteins treated at pH 11, while high deformation values were obtained at pH 2 and 11. Texture of gels made using the conventional method were quite inferior to gels made using fish proteins treated at pH 2 or 11, while color of conventional gels was significantly better than the other treatments. SDS-PAGE revealed that fish proteins were highly denatured during acid or alkali treatment. High cathepsin B-like activity was detected from acid-aided fish proteins. Strong cathepsin L-like activity was found in fish proteins treated at pH 10.5, which corresponded with the lower breaking force and deformation obtained from those samples. Disulfide bonds contributed to high texture value in fish proteins treated at pH 11. Physicochemical characteristics of sarcoplasmic proteins (SP) from rockfish and their interaction with Alaska pollock surimi (myofibrillar proteins) were investigated. Solubility of SP was significantly suppressed at acidic pH (2-4) plus high salt concentration (0.5 M NaCl). This was also supported by SDS-PAGE results (extensively degraded SP). DSC results revealed SP gave three endothermic transitions. The least amount ofproteins was lost when treated at pH 2 or 3 followed by precipitation at pH 5.5. SP did not enhance the gelation properties of myofibrillar proteins, but positively contributed to gelation with myofibrillar proteins when compared to sucrose. Myofibrillar proteins were primary components contributing to heat-induced gelation. Salt effect on acid- or alkali-treated surimi gel was investigated. Good gels were obtained without salt using acid- and alkali-treated fish proteins. Their texture properties decreased as NaCl content increased, unlike conventional surimi gels. Consequently, NaCl did not solubilize myofibrillar proteins once the fish proteins were treated by acid or alkali. Solubility was apparently not a key factor for ... |
author2 |
Park, Jae W. Food Science and Technology Oregon State University. Graduate School |
format |
Master Thesis |
author |
Kim, Young S. |
author_facet |
Kim, Young S. |
author_sort |
Kim, Young S. |
title |
Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
title_short |
Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
title_full |
Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
title_fullStr |
Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
title_full_unstemmed |
Physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various pH conditions |
title_sort |
physicochemical characteristics of fish myofibrillar and sarcoplasmic proteins treated at various ph conditions |
publisher |
Oregon State University |
url |
https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0z709076j |
genre |
alaska pollock Alaska |
genre_facet |
alaska pollock Alaska |
op_relation |
https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/0z709076j |
op_rights |
All rights reserved |
_version_ |
1810468494411563008 |